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PerkinElmer cinaedi
Western blot analysis, after electrophoresis, showing reactivity of sera from an H. <t>cinaedi</t> -immunized rabbit (1:15,000) (A), an H. cinaedi -infected patient (1:1,500) (B), and a His-MAP30 Hc -immunized rabbit (1:15,000) (C) to His-MAP30 Hc (0.6 μg)
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1) Product Images from "Identification of the Major Antigenic Protein of Helicobacter cinaedi and Its Immunogenicity in Humans with H. cinaedi Infections ▿"

Article Title: Identification of the Major Antigenic Protein of Helicobacter cinaedi and Its Immunogenicity in Humans with H. cinaedi Infections ▿

Journal:

doi: 10.1128/CVI.00439-07

Western blot analysis, after electrophoresis, showing reactivity of sera from an H. cinaedi -immunized rabbit (1:15,000) (A), an H. cinaedi -infected patient (1:1,500) (B), and a His-MAP30 Hc -immunized rabbit (1:15,000) (C) to His-MAP30 Hc (0.6 μg)
Figure Legend Snippet: Western blot analysis, after electrophoresis, showing reactivity of sera from an H. cinaedi -immunized rabbit (1:15,000) (A), an H. cinaedi -infected patient (1:1,500) (B), and a His-MAP30 Hc -immunized rabbit (1:15,000) (C) to His-MAP30 Hc (0.6 μg)

Techniques Used: Western Blot, Electrophoresis, Infection

Western blot analysis of responses to recombinant His-MAP30 Hc in serum from H. cinaedi -infected patients (A) and controls (B to D). Sample (lane) numbers above the image correlate with those in the respective groups in Fig. . Each lane
Figure Legend Snippet: Western blot analysis of responses to recombinant His-MAP30 Hc in serum from H. cinaedi -infected patients (A) and controls (B to D). Sample (lane) numbers above the image correlate with those in the respective groups in Fig. . Each lane

Techniques Used: Western Blot, Recombinant, Infection

Western blotting assessment of immunoreactivity of H. cinaedi proteins. (A) Serially diluted (dilution, 1-, 5-, 25-, and 125-fold) H. cinaedi whole-cell lysates (left; 1.3 μg of protein) were electrophoresed and reacted with anti- H. cinaedi rabbit
Figure Legend Snippet: Western blotting assessment of immunoreactivity of H. cinaedi proteins. (A) Serially diluted (dilution, 1-, 5-, 25-, and 125-fold) H. cinaedi whole-cell lysates (left; 1.3 μg of protein) were electrophoresed and reacted with anti- H. cinaedi rabbit

Techniques Used: Western Blot

Time course of serum response in patients with suspected or true H. cinaedi infection and analyzed via recombinant His-MAP30 Hc -based ELISA. Day 0 indicates the time that cellulitis (patients 1 to 4) and fever (patient 5) were first recognized in the patients.
Figure Legend Snippet: Time course of serum response in patients with suspected or true H. cinaedi infection and analyzed via recombinant His-MAP30 Hc -based ELISA. Day 0 indicates the time that cellulitis (patients 1 to 4) and fever (patient 5) were first recognized in the patients.

Techniques Used: Infection, Recombinant, Enzyme-linked Immunosorbent Assay

Antibody responses of H. cinaedi -infected patients (lanes 1 to 8) and an immunized rabbit (A) or control groups (B to D) to proteins in H. cinaedi whole-cell lysate as obtained via Western blotting. Each lane contained 6.5 μg of protein. Rabbit
Figure Legend Snippet: Antibody responses of H. cinaedi -infected patients (lanes 1 to 8) and an immunized rabbit (A) or control groups (B to D) to proteins in H. cinaedi whole-cell lysate as obtained via Western blotting. Each lane contained 6.5 μg of protein. Rabbit

Techniques Used: Infection, Western Blot

Western blot analysis of proteins encoded by plasmid clones obtained by immunoscreening via anti- H. cinaedi rabbit serum. Cell lysates (6.5 μg of protein/lane) of E. coli clones or H. cinaedi were subjected to Western blotting using anti- H. cinaedi
Figure Legend Snippet: Western blot analysis of proteins encoded by plasmid clones obtained by immunoscreening via anti- H. cinaedi rabbit serum. Cell lysates (6.5 μg of protein/lane) of E. coli clones or H. cinaedi were subjected to Western blotting using anti- H. cinaedi

Techniques Used: Western Blot, Plasmid Preparation, Clone Assay

Recombinant His-MAP30 Hc -based ELISA results. Serum antibody levels of H. cinaedi -infected patients ( n = 8) were compared with those of control groups: H. pylori -infected patients ( n = 10), controls 1 (age- and sex-matched subjects) ( n
Figure Legend Snippet: Recombinant His-MAP30 Hc -based ELISA results. Serum antibody levels of H. cinaedi -infected patients ( n = 8) were compared with those of control groups: H. pylori -infected patients ( n = 10), controls 1 (age- and sex-matched subjects) ( n

Techniques Used: Recombinant, Enzyme-linked Immunosorbent Assay, Infection

2) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

3) Product Images from "Morphine Enhances HIV Infection of Human Blood Mononuclear Phagocytes through Modulation of ?-Chemokines and CCR5 Receptor"

Article Title: Morphine Enhances HIV Infection of Human Blood Mononuclear Phagocytes through Modulation of ?-Chemokines and CCR5 Receptor

Journal: Journal of investigative medicine : the official publication of the American Federation for Clinical Research

doi:

Effect of morphine on HIV receptor expression in MDM. ( A ) MDM cultured for 7 days were incubated with or without morphine at the indicated concentrations for 4 hours. Total cellular RNA was extracted from the cell cultures and subjected to RT-PCR using the primer pairs for CCR5, CXCR4, and CD4 receptor genes. Marker , 100 base pair DNA ladder. The amplified PCR products (189 base pairs for CCR5, 371 bp for CXCR4, and 437 bp for CD4) were visualized on an ethidium bromide-stained 3% agarose gel. β-actin was used to monitor the amount and integrity of RNA in each sample. ( B ) MDM cultured for 7 days were incubated with or without morphine at 10 −10 M for 24 hours, and the expression of CCR5, CD4, CXCR4, and CD14 on MDM were determined by performing direct immunofluorescence cytometry. The results shown are the percentages of MDM positive for the receptors analyzed and are representative of four experiments. *, p
Figure Legend Snippet: Effect of morphine on HIV receptor expression in MDM. ( A ) MDM cultured for 7 days were incubated with or without morphine at the indicated concentrations for 4 hours. Total cellular RNA was extracted from the cell cultures and subjected to RT-PCR using the primer pairs for CCR5, CXCR4, and CD4 receptor genes. Marker , 100 base pair DNA ladder. The amplified PCR products (189 base pairs for CCR5, 371 bp for CXCR4, and 437 bp for CD4) were visualized on an ethidium bromide-stained 3% agarose gel. β-actin was used to monitor the amount and integrity of RNA in each sample. ( B ) MDM cultured for 7 days were incubated with or without morphine at 10 −10 M for 24 hours, and the expression of CCR5, CD4, CXCR4, and CD14 on MDM were determined by performing direct immunofluorescence cytometry. The results shown are the percentages of MDM positive for the receptors analyzed and are representative of four experiments. *, p

Techniques Used: Expressing, Cell Culture, Incubation, Reverse Transcription Polymerase Chain Reaction, Marker, Amplification, Polymerase Chain Reaction, Staining, Agarose Gel Electrophoresis, Immunofluorescence, Cytometry

4) Product Images from "Contribution of C3d-P28 repeats to enhancement of immune responses against HBV-preS2/S induced by gene immunization"

Article Title: Contribution of C3d-P28 repeats to enhancement of immune responses against HBV-preS2/S induced by gene immunization

Journal: World Journal of Gastroenterology : WJG

doi: 10.3748/wjg.v10.i14.2072

Semiquantitative RT-PCR for expression of the preS2/S-P28 fusion proteins. Lane 1: DNA marker; Lanes 2,3 and 5: RT-PCR with preS2/Ss and preS2/Sa primers that am-plified an entire coding region (858 bp) of preS2/S, using RNA extracted from pVAON33, pVAON33-S2/S
Figure Legend Snippet: Semiquantitative RT-PCR for expression of the preS2/S-P28 fusion proteins. Lane 1: DNA marker; Lanes 2,3 and 5: RT-PCR with preS2/Ss and preS2/Sa primers that am-plified an entire coding region (858 bp) of preS2/S, using RNA extracted from pVAON33, pVAON33-S2/S

Techniques Used: Reverse Transcription Polymerase Chain Reaction, Expressing, Marker

5) Product Images from "Hybrid mouse-prokaryotic DNA (cytosine-5) methyltransferases retain the specificity of the parental C-terminal domain"

Article Title: Hybrid mouse-prokaryotic DNA (cytosine-5) methyltransferases retain the specificity of the parental C-terminal domain

Journal: The EMBO Journal

doi: 10.1093/emboj/19.9.2103

Fig. 4. De novo methylation catalyzed by the hybrid MTases. ( A ) Total DNA from High Five cells expressing Dnmt1– Hha I, Dnmt1– Hpa II, Dnmt1– Sss I or Dnmt1 was extracted 48 h post-infection. Each lane represents DNA digested with the restriction enzymes indicated (+) above each lane. Lane M contains a Hin dIII digest of λ DNA molecular weight marker. ( B ) De novo methylation of the hybrid MTase genes. Southern blots of total DNA probed with the Bam HI 2100 bp N-terminal fragment of the mouse Dnmt1 cDNA. Each lane represents either a single or double restriction digest as indicated (+). The 2100 bp band is indicated by an arrow. ( C ) De novo methylation of viral upstream and polyhedrin promoter sequences. Southern blots of total DNA probed with a 2200 bp Nsi I fragment consisting of the viral upstream sequences, polyhedrin promoter and a part of the N-terminus of the mouse Dnmt1. Each lane represents either a single or double restriction digest as indicated (+). The 2200 bp band is shown by an arrow. ( D ) Key features of the hybrid MTase and conceptual restriction maps of the Bam HI (2100 bp) and Nsi I (2200 bp) fragments. Features of the hybrid MTase are presented schematically. A 3400 bp cDNA containing the mouse Dnmt1, indicated by black shading, was fused to the N-terminus of the prokaryotic MTase, as shown in grey. The hatched line represents the upstream baculovirus ORF. pPH marks the polyhedrin promoter. Fragments analyzed by restriction enzyme digests [ Bam HI (∼2100 bp) and Nsi I (∼2200 bp)] are indicated by B and N. Restriction enzymes used for methylation analysis are listed on the left. The numbers of target sites and sequences are on the right. Restriction sites are indicated by vertical black lines.
Figure Legend Snippet: Fig. 4. De novo methylation catalyzed by the hybrid MTases. ( A ) Total DNA from High Five cells expressing Dnmt1– Hha I, Dnmt1– Hpa II, Dnmt1– Sss I or Dnmt1 was extracted 48 h post-infection. Each lane represents DNA digested with the restriction enzymes indicated (+) above each lane. Lane M contains a Hin dIII digest of λ DNA molecular weight marker. ( B ) De novo methylation of the hybrid MTase genes. Southern blots of total DNA probed with the Bam HI 2100 bp N-terminal fragment of the mouse Dnmt1 cDNA. Each lane represents either a single or double restriction digest as indicated (+). The 2100 bp band is indicated by an arrow. ( C ) De novo methylation of viral upstream and polyhedrin promoter sequences. Southern blots of total DNA probed with a 2200 bp Nsi I fragment consisting of the viral upstream sequences, polyhedrin promoter and a part of the N-terminus of the mouse Dnmt1. Each lane represents either a single or double restriction digest as indicated (+). The 2200 bp band is shown by an arrow. ( D ) Key features of the hybrid MTase and conceptual restriction maps of the Bam HI (2100 bp) and Nsi I (2200 bp) fragments. Features of the hybrid MTase are presented schematically. A 3400 bp cDNA containing the mouse Dnmt1, indicated by black shading, was fused to the N-terminus of the prokaryotic MTase, as shown in grey. The hatched line represents the upstream baculovirus ORF. pPH marks the polyhedrin promoter. Fragments analyzed by restriction enzyme digests [ Bam HI (∼2100 bp) and Nsi I (∼2200 bp)] are indicated by B and N. Restriction enzymes used for methylation analysis are listed on the left. The numbers of target sites and sequences are on the right. Restriction sites are indicated by vertical black lines.

Techniques Used: Methylation, Expressing, Infection, Molecular Weight, Marker

Fig. 6. Time course of methylation catalyzed by the hybrid Dnmt1– Hha I. ( A ) Reactions contained 30 nM hybrid Dnmt1– Hha I, 50 µM CG [poly (dG-dC)·poly (dG-dC)] and 1, 5 or 10 µM AdoMet and were incubated at 37°C. Duplicate 25 µl samples of each reaction were spotted onto DE81 paper, processed as described in Materials and methods, and 3 H incorporation was measured. The mean values, with standard deviation, for the time points are plotted as filled diamonds (1 µM AdoMet), open circles (5 µM AdoMet) or filled circles (10 µM AdoMet). ( B ) Linearity of methyltransfer reaction as a function of enzyme concentration. Duplicate reactions in 25 µl contained 50 µM CG, 5 µM AdoMet and various mouse Dnmt1– Hha I concentrations (5, 10, 20, 30, 40 and 50 µM) and were incubated at 37°C for 30 min and processed. The solid circles depict the mean values of the [ 3 H]methyl group incorporation.
Figure Legend Snippet: Fig. 6. Time course of methylation catalyzed by the hybrid Dnmt1– Hha I. ( A ) Reactions contained 30 nM hybrid Dnmt1– Hha I, 50 µM CG [poly (dG-dC)·poly (dG-dC)] and 1, 5 or 10 µM AdoMet and were incubated at 37°C. Duplicate 25 µl samples of each reaction were spotted onto DE81 paper, processed as described in Materials and methods, and 3 H incorporation was measured. The mean values, with standard deviation, for the time points are plotted as filled diamonds (1 µM AdoMet), open circles (5 µM AdoMet) or filled circles (10 µM AdoMet). ( B ) Linearity of methyltransfer reaction as a function of enzyme concentration. Duplicate reactions in 25 µl contained 50 µM CG, 5 µM AdoMet and various mouse Dnmt1– Hha I concentrations (5, 10, 20, 30, 40 and 50 µM) and were incubated at 37°C for 30 min and processed. The solid circles depict the mean values of the [ 3 H]methyl group incorporation.

Techniques Used: Methylation, Incubation, Standard Deviation, Concentration Assay

Fig. 2. Expression and purification of hybrid MTases. ( A ) Western blot analysis of High Five cell extracts expressing the hybrid methyltransferases using a mouse Dnmt1 specific Ab 334. The relative positions of biotinylated mol. wt markers (165, 105, 76) are in kDa. His-MMT3 is a His 6 ). An uninfected High Five cell extract was used as a control (C). The MTase bands are indicated by the arrow. The hybrid proteins are indicated above each lane. ( B ) Two purified hybrid MTases, Dnmt1– Hpa II and Dnmt1– Hha I resolved on SDS–PAGE and stained with Coomassie Blue. The broad range molecular weight markers are indicated on the left in kDa. The hybrid MTases are indicated by the arrow.
Figure Legend Snippet: Fig. 2. Expression and purification of hybrid MTases. ( A ) Western blot analysis of High Five cell extracts expressing the hybrid methyltransferases using a mouse Dnmt1 specific Ab 334. The relative positions of biotinylated mol. wt markers (165, 105, 76) are in kDa. His-MMT3 is a His 6 ). An uninfected High Five cell extract was used as a control (C). The MTase bands are indicated by the arrow. The hybrid proteins are indicated above each lane. ( B ) Two purified hybrid MTases, Dnmt1– Hpa II and Dnmt1– Hha I resolved on SDS–PAGE and stained with Coomassie Blue. The broad range molecular weight markers are indicated on the left in kDa. The hybrid MTases are indicated by the arrow.

Techniques Used: Expressing, Purification, Western Blot, SDS Page, Staining, Molecular Weight

6) Product Images from "Dendritic Cells Phagocytose and Are Activated by Treponema pallidum"

Article Title: Dendritic Cells Phagocytose and Are Activated by Treponema pallidum

Journal: Infection and Immunity

doi: 10.1128/IAI.69.1.518-528.2001

XS52 cells express mRNA for tlr2 and tlr4 . (A) Total RNA was extracted from RAW cells and XS52 cells and analyzed by Northern blotting with radioactive probes specific for either tlr2 (TLR2) or tlr4 (TLR4). Membranes were rehybridized with a radioactive probe for GAPDH to ensure equal loading of RNA in each gel lane. X-ray film was exposed to membranes for various periods of time to detect radioactive signals ( tlr2 , 2 h; tlr4 , 2 days; GAPDH, 1 h). (B) Detection of tlr2 and tlr4 mRNA in RAW cells and XS52 cells by RT-PCR. DNase-treated RNA (50 ng) was used as the template in each reaction. PCR products in lanes 1, 4, 7, and 10 were amplified with TLR2-specific primers. PCR products in lanes 2, 5, 8, and 11 were amplified using TLR4-specific primers. Products in lanes 3, 6, 9, and 12 were amplified with GAPDH-specific primers. + and −, reaction mixtures containing and lacking reverse transcriptase (RT), respectively. DNA fragment size markers are indicated on the left.
Figure Legend Snippet: XS52 cells express mRNA for tlr2 and tlr4 . (A) Total RNA was extracted from RAW cells and XS52 cells and analyzed by Northern blotting with radioactive probes specific for either tlr2 (TLR2) or tlr4 (TLR4). Membranes were rehybridized with a radioactive probe for GAPDH to ensure equal loading of RNA in each gel lane. X-ray film was exposed to membranes for various periods of time to detect radioactive signals ( tlr2 , 2 h; tlr4 , 2 days; GAPDH, 1 h). (B) Detection of tlr2 and tlr4 mRNA in RAW cells and XS52 cells by RT-PCR. DNase-treated RNA (50 ng) was used as the template in each reaction. PCR products in lanes 1, 4, 7, and 10 were amplified with TLR2-specific primers. PCR products in lanes 2, 5, 8, and 11 were amplified using TLR4-specific primers. Products in lanes 3, 6, 9, and 12 were amplified with GAPDH-specific primers. + and −, reaction mixtures containing and lacking reverse transcriptase (RT), respectively. DNA fragment size markers are indicated on the left.

Techniques Used: Northern Blot, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Amplification

7) Product Images from "Fetal Liver-Derived Mesenchymal Stem Cell Engraftment After Allogeneic In Utero Transplantation into Rabbits"

Article Title: Fetal Liver-Derived Mesenchymal Stem Cell Engraftment After Allogeneic In Utero Transplantation into Rabbits

Journal: Stem Cells and Development

doi: 10.1089/scd.2010.0483

Long-term assessment of allogeneic EGFP + -fl-MSC engraftment into young rabbit tissues after fetal transplantation (Part I): PCR-derived distribution assessment and FISH-mediated localization. (A) PCR-mediated detection of integrated, EGFP + -fl-MSC-derived,
Figure Legend Snippet: Long-term assessment of allogeneic EGFP + -fl-MSC engraftment into young rabbit tissues after fetal transplantation (Part I): PCR-derived distribution assessment and FISH-mediated localization. (A) PCR-mediated detection of integrated, EGFP + -fl-MSC-derived,

Techniques Used: Transplantation Assay, Polymerase Chain Reaction, Derivative Assay, Fluorescence In Situ Hybridization

Long-term assessment of allogeneic EGFP + -fl-MSC engraftment into young rabbit tissues after fetal transplantation (Part II): immunohistochemical evaluation of transgenic EGFP expression. Immunostaining for EGFP-expressing cells was performed on PCR-positive
Figure Legend Snippet: Long-term assessment of allogeneic EGFP + -fl-MSC engraftment into young rabbit tissues after fetal transplantation (Part II): immunohistochemical evaluation of transgenic EGFP expression. Immunostaining for EGFP-expressing cells was performed on PCR-positive

Techniques Used: Transplantation Assay, Immunohistochemistry, Transgenic Assay, Expressing, Immunostaining, Polymerase Chain Reaction

8) Product Images from "Development of oligonucleotide microarrays for simultaneous multi‐species identification of Phellinus tree‐pathogenic fungi"

Article Title: Development of oligonucleotide microarrays for simultaneous multi‐species identification of Phellinus tree‐pathogenic fungi

Journal: Microbial Biotechnology

doi: 10.1111/1751-7915.12341

Sensitivity analysis of the P hellinus microarray. Agarose gel electrophoresis ( GE ) and reverse dot‐blot hybridization against microarrays were performed with PCR ‐amplified (A) P . weirii or (B) P . noxius ITS primers that were serially diluted to derive samples respectively containing 1 ng, 100 pg, 10 pg, 1 pg, 100 fg or 10 fg of starting DNA . Biotin – PVC : Biotin‐labelled primer amplicons hybridized to probes on PVC chip; DIG – PVC : DIG ‐labelled primer amplicons hybridized to probes on PVC chip; Biotin – NY‐M : Biotin‐labelled primer amplicons hybridized to probes on nylon membrane; DIG – NY‐M : DIG ‐labelled primer amplicons hybridized to probes on nylon membrane.
Figure Legend Snippet: Sensitivity analysis of the P hellinus microarray. Agarose gel electrophoresis ( GE ) and reverse dot‐blot hybridization against microarrays were performed with PCR ‐amplified (A) P . weirii or (B) P . noxius ITS primers that were serially diluted to derive samples respectively containing 1 ng, 100 pg, 10 pg, 1 pg, 100 fg or 10 fg of starting DNA . Biotin – PVC : Biotin‐labelled primer amplicons hybridized to probes on PVC chip; DIG – PVC : DIG ‐labelled primer amplicons hybridized to probes on PVC chip; Biotin – NY‐M : Biotin‐labelled primer amplicons hybridized to probes on nylon membrane; DIG – NY‐M : DIG ‐labelled primer amplicons hybridized to probes on nylon membrane.

Techniques Used: Microarray, Agarose Gel Electrophoresis, Dot Blot, Hybridization, Polymerase Chain Reaction, Amplification, Chromatin Immunoprecipitation

9) Product Images from "Cloning and Characterization of a Family B DNA Polymerase from the Hyperthermophilic Crenarchaeon Pyrobaculum islandicum †"

Article Title: Cloning and Characterization of a Family B DNA Polymerase from the Hyperthermophilic Crenarchaeon Pyrobaculum islandicum †

Journal: Journal of Bacteriology

doi:

Application of DNA polymerase from P. islandicum in PCR. Reactions were carried out in a buffer containing 15 mM Tris-HCl (pH 8.6), 12.5 mM KCl, 2.5 mM (NH 4 ) 2 SO 4 , 1.25 mM MgCl 2 , and 20 μg of BSA per ml. One unit of DNA polymerase from P. islandicum was used to amplify 500 bp (lane 1), 1,000 bp (lane 2), and 1,500 bp (lane 3) of a λ DNA template. Control PCR was performed with 2.5 U of High Fidelity enzyme (lane 4). Twenty microliters of each PCR product was applied on an 1% agarose gel. The corresponding molecular sizes of the marker (lane 5) are indicated in kilobase pairs.
Figure Legend Snippet: Application of DNA polymerase from P. islandicum in PCR. Reactions were carried out in a buffer containing 15 mM Tris-HCl (pH 8.6), 12.5 mM KCl, 2.5 mM (NH 4 ) 2 SO 4 , 1.25 mM MgCl 2 , and 20 μg of BSA per ml. One unit of DNA polymerase from P. islandicum was used to amplify 500 bp (lane 1), 1,000 bp (lane 2), and 1,500 bp (lane 3) of a λ DNA template. Control PCR was performed with 2.5 U of High Fidelity enzyme (lane 4). Twenty microliters of each PCR product was applied on an 1% agarose gel. The corresponding molecular sizes of the marker (lane 5) are indicated in kilobase pairs.

Techniques Used: Polymerase Chain Reaction, Agarose Gel Electrophoresis, Marker

10) Product Images from "Functional implications of calcium permeability of the channel formed by pannexin 1"

Article Title: Functional implications of calcium permeability of the channel formed by pannexin 1

Journal: The Journal of Cell Biology

doi: 10.1083/jcb.200601115

Pannexin1 (PanX1) mRNA is ubiquitously expressed in prostate cell lines. 2% agarose gel showing the expression of the PanX transcripts in human prostate cell line: LNCaP, PNT1A, DU-145, and PC-3, as well as in HEK-293 cells. A no-template control (H 2 O) was also run with the PCR samples, where the cDNA was replaced with water.
Figure Legend Snippet: Pannexin1 (PanX1) mRNA is ubiquitously expressed in prostate cell lines. 2% agarose gel showing the expression of the PanX transcripts in human prostate cell line: LNCaP, PNT1A, DU-145, and PC-3, as well as in HEK-293 cells. A no-template control (H 2 O) was also run with the PCR samples, where the cDNA was replaced with water.

Techniques Used: Agarose Gel Electrophoresis, Expressing, Polymerase Chain Reaction

11) Product Images from "Morphine Enhances HIV Infection of Human Blood Mononuclear Phagocytes through Modulation of ?-Chemokines and CCR5 Receptor"

Article Title: Morphine Enhances HIV Infection of Human Blood Mononuclear Phagocytes through Modulation of ?-Chemokines and CCR5 Receptor

Journal: Journal of investigative medicine : the official publication of the American Federation for Clinical Research

doi:

Effect of morphine on HIV receptor expression in MDM. ( A ) MDM cultured for 7 days were incubated with or without morphine at the indicated concentrations for 4 hours. Total cellular RNA was extracted from the cell cultures and subjected to RT-PCR using the primer pairs for CCR5, CXCR4, and CD4 receptor genes. Marker , 100 base pair DNA ladder. The amplified PCR products (189 base pairs for CCR5, 371 bp for CXCR4, and 437 bp for CD4) were visualized on an ethidium bromide-stained 3% agarose gel. β-actin was used to monitor the amount and integrity of RNA in each sample. ( B ) MDM cultured for 7 days were incubated with or without morphine at 10 −10 M for 24 hours, and the expression of CCR5, CD4, CXCR4, and CD14 on MDM were determined by performing direct immunofluorescence cytometry. The results shown are the percentages of MDM positive for the receptors analyzed and are representative of four experiments. *, p
Figure Legend Snippet: Effect of morphine on HIV receptor expression in MDM. ( A ) MDM cultured for 7 days were incubated with or without morphine at the indicated concentrations for 4 hours. Total cellular RNA was extracted from the cell cultures and subjected to RT-PCR using the primer pairs for CCR5, CXCR4, and CD4 receptor genes. Marker , 100 base pair DNA ladder. The amplified PCR products (189 base pairs for CCR5, 371 bp for CXCR4, and 437 bp for CD4) were visualized on an ethidium bromide-stained 3% agarose gel. β-actin was used to monitor the amount and integrity of RNA in each sample. ( B ) MDM cultured for 7 days were incubated with or without morphine at 10 −10 M for 24 hours, and the expression of CCR5, CD4, CXCR4, and CD14 on MDM were determined by performing direct immunofluorescence cytometry. The results shown are the percentages of MDM positive for the receptors analyzed and are representative of four experiments. *, p

Techniques Used: Expressing, Cell Culture, Incubation, Reverse Transcription Polymerase Chain Reaction, Marker, Amplification, Polymerase Chain Reaction, Staining, Agarose Gel Electrophoresis, Immunofluorescence, Cytometry

12) Product Images from "Substance P antagonist (CP-96,345) inhibits HIV-1 replication in human mononuclear phagocytes"

Article Title: Substance P antagonist (CP-96,345) inhibits HIV-1 replication in human mononuclear phagocytes

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.071052298

Effect of CP-96,345 and/or anti-SP antibody on SP-enhanced HIV replication. HIV Bal strain was used to infect MDM in the presence or absence of SP (10 −6 M), CP-96,345 (10 −6 M), or anti-SP antibody (1:1,000 dilution) as indicated. CP, CP-96,345. HIV only, untreated and HIV Bal strain-infected MDM was used as a control. HIV RT activity ( A ) in the culture supernatants was determined 12 days after infection, and HIV gag mRNA copy numbers ( B ) were quantified by using real-time RT-PCR 12 days after infection ( B ). The data shown are presented as the mean ± SD of triplicate cultures and are representative of three experiments (*, P
Figure Legend Snippet: Effect of CP-96,345 and/or anti-SP antibody on SP-enhanced HIV replication. HIV Bal strain was used to infect MDM in the presence or absence of SP (10 −6 M), CP-96,345 (10 −6 M), or anti-SP antibody (1:1,000 dilution) as indicated. CP, CP-96,345. HIV only, untreated and HIV Bal strain-infected MDM was used as a control. HIV RT activity ( A ) in the culture supernatants was determined 12 days after infection, and HIV gag mRNA copy numbers ( B ) were quantified by using real-time RT-PCR 12 days after infection ( B ). The data shown are presented as the mean ± SD of triplicate cultures and are representative of three experiments (*, P

Techniques Used: Infection, Activity Assay, Quantitative RT-PCR

Effect of CP-96,345 on CCR5 mRNA expression in MDM. −, PCR negative control, which represents lack of PCR products when RT was omitted from the RT reaction by using RNA extracted from untreated MDM. MDM only, untreated MDM was used as a control. MDM were incubated with CP-96,345 (10 −8 to 10 −6 M) as indicated for 3 h, and CCR5 mRNA was then amplified by using RT-PCR. M, 100-bp DNA ladder coelectrophoresed as markers. β-actin was used to monitor the amount and integrity of RNA in each sample.
Figure Legend Snippet: Effect of CP-96,345 on CCR5 mRNA expression in MDM. −, PCR negative control, which represents lack of PCR products when RT was omitted from the RT reaction by using RNA extracted from untreated MDM. MDM only, untreated MDM was used as a control. MDM were incubated with CP-96,345 (10 −8 to 10 −6 M) as indicated for 3 h, and CCR5 mRNA was then amplified by using RT-PCR. M, 100-bp DNA ladder coelectrophoresed as markers. β-actin was used to monitor the amount and integrity of RNA in each sample.

Techniques Used: Expressing, Polymerase Chain Reaction, Negative Control, Incubation, Amplification, Reverse Transcription Polymerase Chain Reaction

Effect of CP-96,345 on the levels of HIV gag mRNA. The HIV Bal strain was used to infect MDM in the presence or absence of CP-96,345 (10 −11 to 10 −7 M). HIV gag mRNA levels were determined by RT-PCR and real-time RT-PCR by using RNA extracted from the MDM 12 days after infection. β-actin was used as the control to monitor the amount and integrity of RNA in each sample. ( A ) RT-PCR: −, negative control; +, DNA isolated from ACH-2 cells was used as a PCR positive control (100 copies). HIV only: HIV Bal infected MDM as an infection control; MDM were infected with HIV Bal strain in the presence of CP-96,345 (10 −11 M to 10 −7 M) as indicated. M: 100-bp DNA ladder coelectrophoresed as markers. ( B ) Real-time RT-PCR: HIV gag mRNA levels were quantified by real-time RT-PCR by using the same RNA samples as indicated in A , and the data are expressed as HIV gag mRNA copy numbers per PCR. The data shown are presented as the mean ± SD of triplicate cultures and are representative of three experiments (*, P
Figure Legend Snippet: Effect of CP-96,345 on the levels of HIV gag mRNA. The HIV Bal strain was used to infect MDM in the presence or absence of CP-96,345 (10 −11 to 10 −7 M). HIV gag mRNA levels were determined by RT-PCR and real-time RT-PCR by using RNA extracted from the MDM 12 days after infection. β-actin was used as the control to monitor the amount and integrity of RNA in each sample. ( A ) RT-PCR: −, negative control; +, DNA isolated from ACH-2 cells was used as a PCR positive control (100 copies). HIV only: HIV Bal infected MDM as an infection control; MDM were infected with HIV Bal strain in the presence of CP-96,345 (10 −11 M to 10 −7 M) as indicated. M: 100-bp DNA ladder coelectrophoresed as markers. ( B ) Real-time RT-PCR: HIV gag mRNA levels were quantified by real-time RT-PCR by using the same RNA samples as indicated in A , and the data are expressed as HIV gag mRNA copy numbers per PCR. The data shown are presented as the mean ± SD of triplicate cultures and are representative of three experiments (*, P

Techniques Used: Reverse Transcription Polymerase Chain Reaction, Quantitative RT-PCR, Infection, Negative Control, Isolation, Polymerase Chain Reaction, Positive Control

13) Product Images from "Benzalkonium Chloride Suppresses Rabbit Corneal Endothelium Intercellular Gap Junction Communication"

Article Title: Benzalkonium Chloride Suppresses Rabbit Corneal Endothelium Intercellular Gap Junction Communication

Journal: PLoS ONE

doi: 10.1371/journal.pone.0109708

Effects of BAK on Cx43 distribution. In untreated cornea, Cx43 exhibited a great uniformity in appearance with numerous big gap junction plaque. The distribution of Cx43 became disorganized and large gap junction plaques were rarely noticeable in 0.05% and 0.1% BAK-treated group (A). Western blot analysis for 1% Triton X-100 insoluble Cx43 (B) and quantitative analysis of insoluble Cx43 abundance were shown (C). Data are means ± SE from three independent experiments. **P value
Figure Legend Snippet: Effects of BAK on Cx43 distribution. In untreated cornea, Cx43 exhibited a great uniformity in appearance with numerous big gap junction plaque. The distribution of Cx43 became disorganized and large gap junction plaques were rarely noticeable in 0.05% and 0.1% BAK-treated group (A). Western blot analysis for 1% Triton X-100 insoluble Cx43 (B) and quantitative analysis of insoluble Cx43 abundance were shown (C). Data are means ± SE from three independent experiments. **P value

Techniques Used: Western Blot

Effect of BAK treatment on co-localization and interaction of Cx43 and ZO-1. Cx43 (red) and ZO-1 (green) co-localization was observed under laser scanning confocal microscope (A). In control group, corneal endothelium presented large gap junction plaques and the co-localization of ZO-1 and Cx43 was obvious. Exposure to 0.05% and 0.1%BAK disturbed the distribution of Cx43 and ZO-1. IP was performed with goat polyclonal anti-Cx43 followed by immunoblotting with mouse monoclonal anti-ZO-1 (B). The ratio of ZO-1 to Cx43 which is normalized with control reduced significantly after BAK treatment especially in 0.05% and 0.1% BAK group (C). Data are means ± SE from three independent experiments. ***P value
Figure Legend Snippet: Effect of BAK treatment on co-localization and interaction of Cx43 and ZO-1. Cx43 (red) and ZO-1 (green) co-localization was observed under laser scanning confocal microscope (A). In control group, corneal endothelium presented large gap junction plaques and the co-localization of ZO-1 and Cx43 was obvious. Exposure to 0.05% and 0.1%BAK disturbed the distribution of Cx43 and ZO-1. IP was performed with goat polyclonal anti-Cx43 followed by immunoblotting with mouse monoclonal anti-ZO-1 (B). The ratio of ZO-1 to Cx43 which is normalized with control reduced significantly after BAK treatment especially in 0.05% and 0.1% BAK group (C). Data are means ± SE from three independent experiments. ***P value

Techniques Used: Microscopy

Effect of BAK treatment on Cx43 and ZO-1 expression. The significant decrease of Cx43 protein was induced by topical application of BAK at the concentration of 0.05% and 0.1% (C, D). In comparison, there was no significant decrease of Cx43 and ZO-1 mRNA in BAK treated group (A, B). Similarly, the expression of ZO-1 protein was consistent with mRNA level of ZO-1. Quantitative analysis of Cx43 mRNA and protein in corneal endothelium was shown in (B) and (D) respectively. Data are means ± SE from three independent experiments. *P value
Figure Legend Snippet: Effect of BAK treatment on Cx43 and ZO-1 expression. The significant decrease of Cx43 protein was induced by topical application of BAK at the concentration of 0.05% and 0.1% (C, D). In comparison, there was no significant decrease of Cx43 and ZO-1 mRNA in BAK treated group (A, B). Similarly, the expression of ZO-1 protein was consistent with mRNA level of ZO-1. Quantitative analysis of Cx43 mRNA and protein in corneal endothelium was shown in (B) and (D) respectively. Data are means ± SE from three independent experiments. *P value

Techniques Used: Expressing, Concentration Assay

BAK treatment increased Cx43 phosphorylation status. Exposure to BAK induced the increase of phosphorylated Cx43 (A). In 0.05% and 0.1%BAK group, P-Cx43 increased significantly compared with control cornea. Quantitative analysis of P-Cx43 abundance was shown in (B). Data are means ± SE from three independent experiments. **P value
Figure Legend Snippet: BAK treatment increased Cx43 phosphorylation status. Exposure to BAK induced the increase of phosphorylated Cx43 (A). In 0.05% and 0.1%BAK group, P-Cx43 increased significantly compared with control cornea. Quantitative analysis of P-Cx43 abundance was shown in (B). Data are means ± SE from three independent experiments. **P value

Techniques Used:

14) Product Images from "Random Amplified Polymorphic DNA (RAPD) for differentiation between Thai and Myanmar strains of Wuchereria bancrofti"

Article Title: Random Amplified Polymorphic DNA (RAPD) for differentiation between Thai and Myanmar strains of Wuchereria bancrofti

Journal: Filaria Journal

doi: 10.1186/1475-2883-6-6

Random Amplified Polymorphic DNA (RAPD) profile of Thai and Myanmar strains of Wuchereria bancrofti . The RAPD profile of the Thai and Myanmar strains of W. bancrofti using Primer 1 (5'-dGGTGCGGGAA-3'): Lane M: 100 bp DNA marker; Lane 1–6: the Thai strain of W. bancrofti ; Lane 7–12: the Myanmar strain of W. bancrofti ; Lane C: Negative Control (uninfected human blood sample). The 300 bp and 795 bp fragments (arrows) are specific to the Myanmar strain of W. bancrofti . The 645, 705, 1290, and 1400 bp fragments were common in both the Thai and Myanmar strains of W. bancrofti .
Figure Legend Snippet: Random Amplified Polymorphic DNA (RAPD) profile of Thai and Myanmar strains of Wuchereria bancrofti . The RAPD profile of the Thai and Myanmar strains of W. bancrofti using Primer 1 (5'-dGGTGCGGGAA-3'): Lane M: 100 bp DNA marker; Lane 1–6: the Thai strain of W. bancrofti ; Lane 7–12: the Myanmar strain of W. bancrofti ; Lane C: Negative Control (uninfected human blood sample). The 300 bp and 795 bp fragments (arrows) are specific to the Myanmar strain of W. bancrofti . The 645, 705, 1290, and 1400 bp fragments were common in both the Thai and Myanmar strains of W. bancrofti .

Techniques Used: Amplification, Marker, Negative Control

15) Product Images from "Combining Rational and Random Strategies in β-Glucosidase Zm-p60.1 Protein Library Construction"

Article Title: Combining Rational and Random Strategies in β-Glucosidase Zm-p60.1 Protein Library Construction

Journal: PLoS ONE

doi: 10.1371/journal.pone.0108292

Hydrolysis rates for substrates p NPG (A) and t ZOG (B) by β-glucosidase Zm-p60.1 variants produced in the course of saturation mutagenesis of the W373position.
Figure Legend Snippet: Hydrolysis rates for substrates p NPG (A) and t ZOG (B) by β-glucosidase Zm-p60.1 variants produced in the course of saturation mutagenesis of the W373position.

Techniques Used: Produced, Mutagenesis

Bioinformatics-based estimation of variability in the set of 167 β-glycosidases defined by Zhao et al. [13] at the position corresponding to W373 in β-glucosidase Zm-p60.1. The whole alignment is included as File S2 and S3 .
Figure Legend Snippet: Bioinformatics-based estimation of variability in the set of 167 β-glycosidases defined by Zhao et al. [13] at the position corresponding to W373 in β-glucosidase Zm-p60.1. The whole alignment is included as File S2 and S3 .

Techniques Used:

Comparison of projected costs of randomized codon-based saturation mutagenesis library creation and one-by-one site-directed mutagenesis (SDM). Empirically determined results for the combined β-glucosidase Zm-p60.1 mutagenesis approach are also shown (experimental).
Figure Legend Snippet: Comparison of projected costs of randomized codon-based saturation mutagenesis library creation and one-by-one site-directed mutagenesis (SDM). Empirically determined results for the combined β-glucosidase Zm-p60.1 mutagenesis approach are also shown (experimental).

Techniques Used: Mutagenesis

16) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

17) Product Images from "Kinetic studies of the production of nitric oxide (NO) and tumour necrosis factor-alpha (TNF-?) in macrophages stimulated with Burkholderia pseudomallei endotoxin"

Article Title: Kinetic studies of the production of nitric oxide (NO) and tumour necrosis factor-alpha (TNF-?) in macrophages stimulated with Burkholderia pseudomallei endotoxin

Journal: Clinical and Experimental Immunology

doi: 10.1046/j.1365-2249.2000.01386.x

Kinetics of inducible nitric oxide synthase (iNOS) and TNF-α mRNA expression from mouse macrophage cells (RAW 264.7) activated by lipopolysaccharide (LPS). The macrophage cells were activated with LPS from Burkholderia pseudomallei (BP-LPS; 100 ng/ml) or Escherichia coli -LPS (10 ng/ml) for 15, 30, 60 and 120 min. After 9 h of incubation, the synthesized cDNA from macrophage cell RNA was subjected to polymerase chain reaction following by hybridization with appropriate radiolabelled probes. The β-actin served as an internal control. Data are representative of three independent experiments with similar results.
Figure Legend Snippet: Kinetics of inducible nitric oxide synthase (iNOS) and TNF-α mRNA expression from mouse macrophage cells (RAW 264.7) activated by lipopolysaccharide (LPS). The macrophage cells were activated with LPS from Burkholderia pseudomallei (BP-LPS; 100 ng/ml) or Escherichia coli -LPS (10 ng/ml) for 15, 30, 60 and 120 min. After 9 h of incubation, the synthesized cDNA from macrophage cell RNA was subjected to polymerase chain reaction following by hybridization with appropriate radiolabelled probes. The β-actin served as an internal control. Data are representative of three independent experiments with similar results.

Techniques Used: Expressing, Incubation, Synthesized, Polymerase Chain Reaction, Hybridization

18) Product Images from "Characterization of Listeria monocytogenes Isolates from Human Listeriosis Cases in Italy "

Article Title: Characterization of Listeria monocytogenes Isolates from Human Listeriosis Cases in Italy

Journal: Journal of Clinical Microbiology

doi: 10.1128/JCM.00102-09

Agarose gel electrophoresis of inlA , inlC , and inlJ amplicons obtained from representative human isolates of L. monocytogenes . Lanes: MW (molecular weight), 1-kbp DNA ladder (Promega); 1 to 6, PCR products from human isolates analyzed in this study. Molecular sizes corresponding to the amplified fragments are given on the right.
Figure Legend Snippet: Agarose gel electrophoresis of inlA , inlC , and inlJ amplicons obtained from representative human isolates of L. monocytogenes . Lanes: MW (molecular weight), 1-kbp DNA ladder (Promega); 1 to 6, PCR products from human isolates analyzed in this study. Molecular sizes corresponding to the amplified fragments are given on the right.

Techniques Used: Agarose Gel Electrophoresis, Molecular Weight, Polymerase Chain Reaction, Amplification

19) Product Images from "Characterization of shark complement factor I gene(s): genomic analysis of a novel shark-specific sequence"

Article Title: Characterization of shark complement factor I gene(s): genomic analysis of a novel shark-specific sequence

Journal: Molecular immunology

doi: 10.1016/j.molimm.2009.04.002

Result of PCR amplification of SSR site-specific sequence. Lanes designated Mass ladder and GcIf indicate a standard size marker (low DNA mass ladder, Invitrogen) and the sample (GcfI). A sense primer positioned from 53 to 73 and an antisense primer from 327 to 308 in the nucleotide sequence of GcfI-1 were used in this experiment. PCR amplification was performed under the following condition: forty cycles of 94°C for 30 sec, 53°C for 30 sec, and 72°C for 40 sec. The mass ladder and sample were loaded on a 0.8% agarose/EtBr gel in 1 X TAE buffer. The size of the PCR amplified product ranged from ~179-bp to 275-bp.
Figure Legend Snippet: Result of PCR amplification of SSR site-specific sequence. Lanes designated Mass ladder and GcIf indicate a standard size marker (low DNA mass ladder, Invitrogen) and the sample (GcfI). A sense primer positioned from 53 to 73 and an antisense primer from 327 to 308 in the nucleotide sequence of GcfI-1 were used in this experiment. PCR amplification was performed under the following condition: forty cycles of 94°C for 30 sec, 53°C for 30 sec, and 72°C for 40 sec. The mass ladder and sample were loaded on a 0.8% agarose/EtBr gel in 1 X TAE buffer. The size of the PCR amplified product ranged from ~179-bp to 275-bp.

Techniques Used: Polymerase Chain Reaction, Amplification, Sequencing, Marker, Size-exclusion Chromatography

20) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

21) Product Images from "Characterization of Listeria monocytogenes Isolates from Human Listeriosis Cases in Italy "

Article Title: Characterization of Listeria monocytogenes Isolates from Human Listeriosis Cases in Italy

Journal: Journal of Clinical Microbiology

doi: 10.1128/JCM.00102-09

Agarose gel electrophoresis of inlA , inlC , and inlJ amplicons obtained from representative human isolates of L. monocytogenes . Lanes: MW (molecular weight), 1-kbp DNA ladder (Promega); 1 to 6, PCR products from human isolates analyzed in this study. Molecular sizes corresponding to the amplified fragments are given on the right.
Figure Legend Snippet: Agarose gel electrophoresis of inlA , inlC , and inlJ amplicons obtained from representative human isolates of L. monocytogenes . Lanes: MW (molecular weight), 1-kbp DNA ladder (Promega); 1 to 6, PCR products from human isolates analyzed in this study. Molecular sizes corresponding to the amplified fragments are given on the right.

Techniques Used: Agarose Gel Electrophoresis, Molecular Weight, Polymerase Chain Reaction, Amplification

22) Product Images from "Characterization of Listeria monocytogenes Isolates from Human Listeriosis Cases in Italy "

Article Title: Characterization of Listeria monocytogenes Isolates from Human Listeriosis Cases in Italy

Journal: Journal of Clinical Microbiology

doi: 10.1128/JCM.00102-09

Agarose gel electrophoresis of inlA , inlC , and inlJ amplicons obtained from representative human isolates of L. monocytogenes . Lanes: MW (molecular weight), 1-kbp DNA ladder (Promega); 1 to 6, PCR products from human isolates analyzed in this study. Molecular sizes corresponding to the amplified fragments are given on the right.
Figure Legend Snippet: Agarose gel electrophoresis of inlA , inlC , and inlJ amplicons obtained from representative human isolates of L. monocytogenes . Lanes: MW (molecular weight), 1-kbp DNA ladder (Promega); 1 to 6, PCR products from human isolates analyzed in this study. Molecular sizes corresponding to the amplified fragments are given on the right.

Techniques Used: Agarose Gel Electrophoresis, Molecular Weight, Polymerase Chain Reaction, Amplification

23) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

24) Product Images from "HIV-1 Infection of Placental Cord Blood Monocyte-Derived Dendritic Cells"

Article Title: HIV-1 Infection of Placental Cord Blood Monocyte-Derived Dendritic Cells

Journal: Journal of hematotherapy & stem cell research

doi: 10.1089/152581601753193823

RT-PCR analysis of CD4 and CCR5 mRNA expression in cord MDDC and MDM. Cord monocytes were cultured in the presence or absence of GM-CSF, IL-4, and TNF- α . Total cellular RNA was extracted from equal numbers of cord MDDC and MDM (0.5 × 10 6 cells) at days 7, 10, and 13 in cultures. D, MDDC; M, MDM. Results shown are representative of experiments with three cord blood samples.
Figure Legend Snippet: RT-PCR analysis of CD4 and CCR5 mRNA expression in cord MDDC and MDM. Cord monocytes were cultured in the presence or absence of GM-CSF, IL-4, and TNF- α . Total cellular RNA was extracted from equal numbers of cord MDDC and MDM (0.5 × 10 6 cells) at days 7, 10, and 13 in cultures. D, MDDC; M, MDM. Results shown are representative of experiments with three cord blood samples.

Techniques Used: Reverse Transcription Polymerase Chain Reaction, Expressing, Cell Culture

Flow cytometry analysis of membrane CD4 and CCR5 expression on cord MDDC and MDM. Cord monocytes cultured in the presence or absence of GM-CSF, IL-4, and TNF- α for 7, 10, or 13 days were harvested and stained with a mAb against CD4 and CCR5 receptors. Results are shown as the percentage of CD4 + or CCR5 + cells (mean +SE) and represent an average of flow cytometry data obtained from experiments using five cord blood samples.
Figure Legend Snippet: Flow cytometry analysis of membrane CD4 and CCR5 expression on cord MDDC and MDM. Cord monocytes cultured in the presence or absence of GM-CSF, IL-4, and TNF- α for 7, 10, or 13 days were harvested and stained with a mAb against CD4 and CCR5 receptors. Results are shown as the percentage of CD4 + or CCR5 + cells (mean +SE) and represent an average of flow cytometry data obtained from experiments using five cord blood samples.

Techniques Used: Flow Cytometry, Cytometry, Expressing, Cell Culture, Staining

Correlation of membrane CCR5 expression and HIV replication in cord MDDC. Cord monocytes cultured in the presence of GM-CSF, IL-4, and TNF- α were harvested and stained with a mAb against CCR5 at days 7, 10, and 13 post-isolation. MDDC from the same cord blood sample cultured under identical culture conditions were challenged with HIV pseudotyped with ADA Env at the indicated time points. Luciferase activity was quantitated in cell lysates 72 h after infection. Results shown are representative of three experiments.
Figure Legend Snippet: Correlation of membrane CCR5 expression and HIV replication in cord MDDC. Cord monocytes cultured in the presence of GM-CSF, IL-4, and TNF- α were harvested and stained with a mAb against CCR5 at days 7, 10, and 13 post-isolation. MDDC from the same cord blood sample cultured under identical culture conditions were challenged with HIV pseudotyped with ADA Env at the indicated time points. Luciferase activity was quantitated in cell lysates 72 h after infection. Results shown are representative of three experiments.

Techniques Used: Expressing, Cell Culture, Staining, Isolation, Luciferase, Activity Assay, Infection

25) Product Images from "Alcohol Potentiates HIV-1 Infection of Human Blood Mononuclear Phagocytes"

Article Title: Alcohol Potentiates HIV-1 Infection of Human Blood Mononuclear Phagocytes

Journal: Alcoholism, clinical and experimental research

doi: 10.1097/01.ALC.0000042148.50808.04

Effect of alcohol on CCR5 mRNA expression in MDM. Seven-day-cultured MDM were incubated with or without alcohol at the indicated concentrations for 4 hr. Total cellular RNA was extracted from the cell cultures and subjected to RT-PCR (A) or real-time PCR (B). (A) The amplified PCR products (189 bp for CCR5) were visualized on an ethidium bromide–stained 3% agarose gel. β -actin was used to monitor the amount and integrity of RNA in each sample. (B) CCR5 cDNA transcribed from the total RNA was also subjected to real-time PCR for quantification of CCR5 mRNA copy numbers. CCR5 mRNA copy numbers were normalized with GAPDH mRNA. The results are expressed as CCR5 mRNA copies per 100,000 GAPDH mRNA. Data shown are mean ± SEM of duplicate cultures and are representative of experiments using cells from six different donors (** p
Figure Legend Snippet: Effect of alcohol on CCR5 mRNA expression in MDM. Seven-day-cultured MDM were incubated with or without alcohol at the indicated concentrations for 4 hr. Total cellular RNA was extracted from the cell cultures and subjected to RT-PCR (A) or real-time PCR (B). (A) The amplified PCR products (189 bp for CCR5) were visualized on an ethidium bromide–stained 3% agarose gel. β -actin was used to monitor the amount and integrity of RNA in each sample. (B) CCR5 cDNA transcribed from the total RNA was also subjected to real-time PCR for quantification of CCR5 mRNA copy numbers. CCR5 mRNA copy numbers were normalized with GAPDH mRNA. The results are expressed as CCR5 mRNA copies per 100,000 GAPDH mRNA. Data shown are mean ± SEM of duplicate cultures and are representative of experiments using cells from six different donors (** p

Techniques Used: Expressing, Cell Culture, Incubation, Reverse Transcription Polymerase Chain Reaction, Real-time Polymerase Chain Reaction, Amplification, Polymerase Chain Reaction, Staining, Agarose Gel Electrophoresis

26) Product Images from "Up-regulation of the tumour-associated marker CD44V6 in experimental kidney disease"

Article Title: Up-regulation of the tumour-associated marker CD44V6 in experimental kidney disease

Journal: Clinical and Experimental Immunology

doi: 10.1046/j.1365-2249.2000.01313.x

Analysis of CD44V6 mRNA isoforms in normal rat kidney and NRK52E tubular epithelial cells. A biotinylated sense V6 oligonucleotide (V6 no. 3) and streptavidin magnetic beads were used to capture cDNA containing the CD44V6 sequence. cDNA samples before (no capture) and after capture (V6 capture) were subjected to reverse transcription-polymerase chain reaction (RT-PCR) using a S2/S7 primer pair. The PCR products were analysed by Southern blotting using: (a) S3 probe, or (b) V6 no. 2 probe. Positions of molecular weight markers (base pair) are shown.
Figure Legend Snippet: Analysis of CD44V6 mRNA isoforms in normal rat kidney and NRK52E tubular epithelial cells. A biotinylated sense V6 oligonucleotide (V6 no. 3) and streptavidin magnetic beads were used to capture cDNA containing the CD44V6 sequence. cDNA samples before (no capture) and after capture (V6 capture) were subjected to reverse transcription-polymerase chain reaction (RT-PCR) using a S2/S7 primer pair. The PCR products were analysed by Southern blotting using: (a) S3 probe, or (b) V6 no. 2 probe. Positions of molecular weight markers (base pair) are shown.

Techniques Used: Magnetic Beads, Sequencing, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Southern Blot, Molecular Weight

27) Product Images from "Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of the mammalian sperm receptor ZP2"

Article Title: Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of the mammalian sperm receptor ZP2

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi:

cDNA sequence and translated single-letter amino acid sequence of gp69/64 protein. The N-terminal pre-pro-peptide sequence and the C-terminal peptide sequence after the putative furin cleavage site (RRKR) is italicized. The chemically determined peptide sequences are underlined and in boldface. The four putative N-glycosylation sites are underlined. The polyadenylation signal (AATAAA) is in boldface.
Figure Legend Snippet: cDNA sequence and translated single-letter amino acid sequence of gp69/64 protein. The N-terminal pre-pro-peptide sequence and the C-terminal peptide sequence after the putative furin cleavage site (RRKR) is italicized. The chemically determined peptide sequences are underlined and in boldface. The four putative N-glycosylation sites are underlined. The polyadenylation signal (AATAAA) is in boldface.

Techniques Used: Sequencing

( A ) Comparison of chemically determined amino acid sequences of gp69 and gp64 starting from three different sites in the polypeptide: site 1, N terminus of intact, mature gp69 and gp64; site 2, N terminus of the proteolytically processed forms of gp69 and gp64 (gp66 and gp61) after egg activation; and site 3, the 65- and 60-kDa forms generated by treatment of eggs with type I collagenase. ( B ) Deglycosylation of gp69 and gp64. Intact gp69/64, PNGase F-treated, and trifluoromethanesulfonic acid-treated gp69/64 were separated by using SDS/PAGE, transferred onto a membrane, and Western blotted with the specific anti-gp69/64 antibody.
Figure Legend Snippet: ( A ) Comparison of chemically determined amino acid sequences of gp69 and gp64 starting from three different sites in the polypeptide: site 1, N terminus of intact, mature gp69 and gp64; site 2, N terminus of the proteolytically processed forms of gp69 and gp64 (gp66 and gp61) after egg activation; and site 3, the 65- and 60-kDa forms generated by treatment of eggs with type I collagenase. ( B ) Deglycosylation of gp69 and gp64. Intact gp69/64, PNGase F-treated, and trifluoromethanesulfonic acid-treated gp69/64 were separated by using SDS/PAGE, transferred onto a membrane, and Western blotted with the specific anti-gp69/64 antibody.

Techniques Used: Activation Assay, Generated, SDS Page, Western Blot

Protein homology of Xenopus gp69/64 VE protein with mammalian ZP2. ( A ) The sequence of Xenopus ). At each position, residues that are identical in 3 of 4 sequences are boxed. The ZP domain is overlined. The 16 conserved cysteines are indicated by closed squares. The putative furin-cleavage site is underlined. ( B ) Comparison of hydropathy plots of Xenopus gp69/64 and mouse and human ZP2s. Hydropathy plots were made by using DNA Strider and the Kyte–Doolittle algorithm. Plots were aligned at the conserved ZP domain. A putative signal peptide (SP) and a C-terminal hydrophobic domain (TM) are present in all three sequences. ( C ) Protein-matrix plots (pam250 matrix) of mouse ZP2 protein vs. the Xenopus gp69/64. Parameters: Window size = 8, Minimum % score = 60; Hash value = 2. ( D ) Western blot of total VE proteins with polyclonal antiserum against mouse ZP2 protein.
Figure Legend Snippet: Protein homology of Xenopus gp69/64 VE protein with mammalian ZP2. ( A ) The sequence of Xenopus ). At each position, residues that are identical in 3 of 4 sequences are boxed. The ZP domain is overlined. The 16 conserved cysteines are indicated by closed squares. The putative furin-cleavage site is underlined. ( B ) Comparison of hydropathy plots of Xenopus gp69/64 and mouse and human ZP2s. Hydropathy plots were made by using DNA Strider and the Kyte–Doolittle algorithm. Plots were aligned at the conserved ZP domain. A putative signal peptide (SP) and a C-terminal hydrophobic domain (TM) are present in all three sequences. ( C ) Protein-matrix plots (pam250 matrix) of mouse ZP2 protein vs. the Xenopus gp69/64. Parameters: Window size = 8, Minimum % score = 60; Hash value = 2. ( D ) Western blot of total VE proteins with polyclonal antiserum against mouse ZP2 protein.

Techniques Used: Sequencing, Western Blot

The N terminus of gp69/64 is essential for sperm binding. ( A ) Comparison of the inhibitory activity of gp69/64, gp66/61, and gp65/60 on sperm–egg binding. Each protein (5 μg/ml) was used as competitor in the sperm-binding competition assays. ( B ) Comparison of anti-gp69/64 antibody staining of the surface of a dejellied unfertilized egg before ( Left ) and after ( Right ) treatment with type I collagenase. The apparent “staining” seen after collagenase on the vegetal hemisphere is an artifact caused by autofluorescence.
Figure Legend Snippet: The N terminus of gp69/64 is essential for sperm binding. ( A ) Comparison of the inhibitory activity of gp69/64, gp66/61, and gp65/60 on sperm–egg binding. Each protein (5 μg/ml) was used as competitor in the sperm-binding competition assays. ( B ) Comparison of anti-gp69/64 antibody staining of the surface of a dejellied unfertilized egg before ( Left ) and after ( Right ) treatment with type I collagenase. The apparent “staining” seen after collagenase on the vegetal hemisphere is an artifact caused by autofluorescence.

Techniques Used: Binding Assay, Activity Assay, Staining

28) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

29) Product Images from "Interleukin-1? stimulates macrophage inflammatory protein-1? and -1? expression in human neuronal cells (NT2-N)"

Article Title: Interleukin-1? stimulates macrophage inflammatory protein-1? and -1? expression in human neuronal cells (NT2-N)

Journal: Journal of neurochemistry

doi:

Effect of NF-κB inhibitor CAPE on IL-1β-induced activation of the NF-κB promoter (a) and MIP-1α and -1β expression (b) in NT2-N. (a) NT2-N cells were transfected with plasmid containing the NF-κB promoter (pNF-κB-luc). The cells were then incubated with or without IL-1β and/or CAPE for 12 h. Data are mean ± SD of triplicate cultures, representative of three independent experiments. (b) NT2-N cells were preincubated with or without CAPE (25 μg/mL) for 2 h. The cells were then treated with IL-1β (4 ng/mL) for 6 h. Total cellular RNA was extracted and subjected to real-time RT–PCR to detect MIP-1α and -1β mRNA expression. Data are mean ± SD of triplicate cultures, representative of two independent experiments.
Figure Legend Snippet: Effect of NF-κB inhibitor CAPE on IL-1β-induced activation of the NF-κB promoter (a) and MIP-1α and -1β expression (b) in NT2-N. (a) NT2-N cells were transfected with plasmid containing the NF-κB promoter (pNF-κB-luc). The cells were then incubated with or without IL-1β and/or CAPE for 12 h. Data are mean ± SD of triplicate cultures, representative of three independent experiments. (b) NT2-N cells were preincubated with or without CAPE (25 μg/mL) for 2 h. The cells were then treated with IL-1β (4 ng/mL) for 6 h. Total cellular RNA was extracted and subjected to real-time RT–PCR to detect MIP-1α and -1β mRNA expression. Data are mean ± SD of triplicate cultures, representative of two independent experiments.

Techniques Used: Activation Assay, Expressing, Transfection, Plasmid Preparation, Incubation, Quantitative RT-PCR

Effect of cytokines on MIP-1α and -1β mRNA expression in human NT2-N cells. NT2-N cells were incubated with medium alone (Control), TNF-a (10 ng/mL), GM-CSF (10 ng/mL), IL-1β (4 ng/mL), IL-3 (10 ng/mL), IL-4 (10 ng/mL), IL-6 (10 ng/mL) or LPS (10 ng/mL) for 6 h. Total cellular RNA was isolated and subjected to real-time RT–PCR using specific primers for MIP-1α (a) and -1β (b) Data are mean ± SD of triplicate cultures, representative of two independent experiments.
Figure Legend Snippet: Effect of cytokines on MIP-1α and -1β mRNA expression in human NT2-N cells. NT2-N cells were incubated with medium alone (Control), TNF-a (10 ng/mL), GM-CSF (10 ng/mL), IL-1β (4 ng/mL), IL-3 (10 ng/mL), IL-4 (10 ng/mL), IL-6 (10 ng/mL) or LPS (10 ng/mL) for 6 h. Total cellular RNA was isolated and subjected to real-time RT–PCR using specific primers for MIP-1α (a) and -1β (b) Data are mean ± SD of triplicate cultures, representative of two independent experiments.

Techniques Used: Expressing, Incubation, Isolation, Quantitative RT-PCR

Effect of IL-1β on MIP-1α and β expression in NT2-N cells. (a) NT2-N cells were incubated with IL-1β at the indicated concentrations for 6 h, and total RNA was isolated and subjected to RT–PCR and electrophoresis for MIP-1α and -1β mRNA. Expression of MIP-1α (b) and MIP-1β (c) mRNA in NT2-N cells was quantified by real-time RT–PCR. Data are mean ± SD of triplicate cultures, representative of three independent experiments.
Figure Legend Snippet: Effect of IL-1β on MIP-1α and β expression in NT2-N cells. (a) NT2-N cells were incubated with IL-1β at the indicated concentrations for 6 h, and total RNA was isolated and subjected to RT–PCR and electrophoresis for MIP-1α and -1β mRNA. Expression of MIP-1α (b) and MIP-1β (c) mRNA in NT2-N cells was quantified by real-time RT–PCR. Data are mean ± SD of triplicate cultures, representative of three independent experiments.

Techniques Used: Expressing, Incubation, Isolation, Reverse Transcription Polymerase Chain Reaction, Electrophoresis, Quantitative RT-PCR

Time course of IL-1β effect on MIP-1α and -1β mRNA expression in NT2-N cells. NT2-N cells were incubated with (+) or without (−) IL-1β (4 ng/mL) and expression was measured at the indicated times after treatment. (a) Total RNA was isolated and subjected to RT–PCR and electrophoresis for MIP-1α and -1β mRNA. Expression of MIP-1α (b) and MIP-1β (c) mRNA in NT2-N cells was also quantified by real-time RT–PCR. Data are means of triplicate cultures, representative of three independent experiments.
Figure Legend Snippet: Time course of IL-1β effect on MIP-1α and -1β mRNA expression in NT2-N cells. NT2-N cells were incubated with (+) or without (−) IL-1β (4 ng/mL) and expression was measured at the indicated times after treatment. (a) Total RNA was isolated and subjected to RT–PCR and electrophoresis for MIP-1α and -1β mRNA. Expression of MIP-1α (b) and MIP-1β (c) mRNA in NT2-N cells was also quantified by real-time RT–PCR. Data are means of triplicate cultures, representative of three independent experiments.

Techniques Used: Expressing, Incubation, Isolation, Reverse Transcription Polymerase Chain Reaction, Electrophoresis, Quantitative RT-PCR

Effect of IL-1βAb on IL-1β-induced MIP-1α and -1β mRNA expression in NT2-N cells. NT2-N cells were incubated with (+) or without (−) IL-1β (4 ng/mL) and/or IL-1βAb (10 μL) or normal rabbit IgG (10 μL) for 6 h. Total cellular RNA was isolated and subjected to real-time RT–PCR to quantify MIP-1α (a) and -1β (b) mRNA. Data are mean ± SD of triplicate cultures, representative of three independent experiments.
Figure Legend Snippet: Effect of IL-1βAb on IL-1β-induced MIP-1α and -1β mRNA expression in NT2-N cells. NT2-N cells were incubated with (+) or without (−) IL-1β (4 ng/mL) and/or IL-1βAb (10 μL) or normal rabbit IgG (10 μL) for 6 h. Total cellular RNA was isolated and subjected to real-time RT–PCR to quantify MIP-1α (a) and -1β (b) mRNA. Data are mean ± SD of triplicate cultures, representative of three independent experiments.

Techniques Used: Expressing, Incubation, Isolation, Quantitative RT-PCR

Effect of MDM culture supernatants (MDM-Sup) on MIP-1β mRNA expression in human NT2-N cells. NT2-N cells were incubated with or without LPS-stimulated MDM supernatants (1 : 5 dilution) and/or IL-1βAb for 6 h. Total cellular RNA was isolated and subjected to RT–PCR (insert) and real-time RT–PCR to quantify MIP-1β mRNA. Data are mean ± SD of triplicate cultures, representative of three independent experiments.
Figure Legend Snippet: Effect of MDM culture supernatants (MDM-Sup) on MIP-1β mRNA expression in human NT2-N cells. NT2-N cells were incubated with or without LPS-stimulated MDM supernatants (1 : 5 dilution) and/or IL-1βAb for 6 h. Total cellular RNA was isolated and subjected to RT–PCR (insert) and real-time RT–PCR to quantify MIP-1β mRNA. Data are mean ± SD of triplicate cultures, representative of three independent experiments.

Techniques Used: Expressing, Incubation, Isolation, Reverse Transcription Polymerase Chain Reaction, Quantitative RT-PCR

30) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

31) Product Images from "Suppression of angiogenesis and tumor growth in vitro and in vivo using an anti-angiopoietin-2 single-chain antibody"

Article Title: Suppression of angiogenesis and tumor growth in vitro and in vivo using an anti-angiopoietin-2 single-chain antibody

Journal: Experimental and Therapeutic Medicine

doi: 10.3892/etm.2014.1476

Presence of Ang-2 RNA by qPCR. Lane M, marker, GeneRuler 1 kb DNA Ladder. The band of Ang-2 was observed at the predicted location on the gel. Ang-2, angiopoietin-2; qPCR, quantitative PCR.
Figure Legend Snippet: Presence of Ang-2 RNA by qPCR. Lane M, marker, GeneRuler 1 kb DNA Ladder. The band of Ang-2 was observed at the predicted location on the gel. Ang-2, angiopoietin-2; qPCR, quantitative PCR.

Techniques Used: Real-time Polymerase Chain Reaction, Marker

32) Product Images from "1-Deoxy-d-Xylulose 5-Phosphate Reductoisomerase (IspC) from Mycobacterium tuberculosis: towards Understanding Mycobacterial Resistance to Fosmidomycin"

Article Title: 1-Deoxy-d-Xylulose 5-Phosphate Reductoisomerase (IspC) from Mycobacterium tuberculosis: towards Understanding Mycobacterial Resistance to Fosmidomycin

Journal: Journal of Bacteriology

doi: 10.1128/JB.187.24.8395-8402.2005

Effects of NADPH and DXP concentrations on Rv2870c activity. Reaction mixtures contained 100 mM MOPS, pH 7.9, 4 mM MgCl 2 , 0.01% CHAPS, and 66 nM Rv2870c. In some cases DXP was held at 100 μM and the concentration of NAPH was varied (A); in other cases NADPH was held at 100 μM and the concentration of DXP was varied (B). Reaction mixtures were incubated at 30°C for 5 min.
Figure Legend Snippet: Effects of NADPH and DXP concentrations on Rv2870c activity. Reaction mixtures contained 100 mM MOPS, pH 7.9, 4 mM MgCl 2 , 0.01% CHAPS, and 66 nM Rv2870c. In some cases DXP was held at 100 μM and the concentration of NAPH was varied (A); in other cases NADPH was held at 100 μM and the concentration of DXP was varied (B). Reaction mixtures were incubated at 30°C for 5 min.

Techniques Used: Activity Assay, Concentration Assay, Incubation

SDS-PAGE analysis of Rv2870c. Immobilized metal affinity chromatography-purified, recombinant Rv2870c was loaded in lane 1, and molecular mass markers were loaded in lane 2.
Figure Legend Snippet: SDS-PAGE analysis of Rv2870c. Immobilized metal affinity chromatography-purified, recombinant Rv2870c was loaded in lane 1, and molecular mass markers were loaded in lane 2.

Techniques Used: SDS Page, Affinity Chromatography, Purification, Recombinant

Effect of pH on Rv2870c activity. Reaction mixtures contained 300 μM DXP, 300 μM NADPH, 4 mM MgCl 2 , and 0.01% CHAPS. The buffer and pH used for each reaction mixture are indicated. Reaction mixtures were incubated at 30°C for 5 min.
Figure Legend Snippet: Effect of pH on Rv2870c activity. Reaction mixtures contained 300 μM DXP, 300 μM NADPH, 4 mM MgCl 2 , and 0.01% CHAPS. The buffer and pH used for each reaction mixture are indicated. Reaction mixtures were incubated at 30°C for 5 min.

Techniques Used: Activity Assay, Incubation

33) Product Images from "Isolation and Characterization of Diverse Halobenzoate-Degrading Denitrifying Bacteria from Soils and Sediments"

Article Title: Isolation and Characterization of Diverse Halobenzoate-Degrading Denitrifying Bacteria from Soils and Sediments

Journal: Applied and Environmental Microbiology

doi:

Phylogenetic relationship of halobenzoate-degrading isolates. The tree was constructed with 600 bases of the 16S rRNA gene by using a neighbor-joining tree and a 100 bootstrap for the confidence level.
Figure Legend Snippet: Phylogenetic relationship of halobenzoate-degrading isolates. The tree was constructed with 600 bases of the 16S rRNA gene by using a neighbor-joining tree and a 100 bootstrap for the confidence level.

Techniques Used: Construct

34) Product Images from "Characterization of shark complement factor I gene(s): genomic analysis of a novel shark-specific sequence"

Article Title: Characterization of shark complement factor I gene(s): genomic analysis of a novel shark-specific sequence

Journal: Molecular immunology

doi: 10.1016/j.molimm.2009.04.002

Results of gene expression analysis of the nurse shark GcIf in tissues. The size of RT-PCR amplified product is ~977–1025 bp for GcIf-1/-2 (Panel A) and ~909–957 bp for GcIf-1-4 (Panel B). Panel C are results for the positive control of nurse shark beta-actin. Lane 1 is the standard DNA-size marker (λDNA/Hind III fragments, Invitogen), and lanes 2 through 10 are tissue samples; kidney, spleen, brain, liver, intestine, ovary, muscle, heart, and pancreas, respectively. For each panel, conditions of RT-PCR are provided in corresponding parenthesis.
Figure Legend Snippet: Results of gene expression analysis of the nurse shark GcIf in tissues. The size of RT-PCR amplified product is ~977–1025 bp for GcIf-1/-2 (Panel A) and ~909–957 bp for GcIf-1-4 (Panel B). Panel C are results for the positive control of nurse shark beta-actin. Lane 1 is the standard DNA-size marker (λDNA/Hind III fragments, Invitogen), and lanes 2 through 10 are tissue samples; kidney, spleen, brain, liver, intestine, ovary, muscle, heart, and pancreas, respectively. For each panel, conditions of RT-PCR are provided in corresponding parenthesis.

Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Amplification, Positive Control, Marker

35) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

36) Product Images from "Characterization of shark complement factor I gene(s): genomic analysis of a novel shark-specific sequence"

Article Title: Characterization of shark complement factor I gene(s): genomic analysis of a novel shark-specific sequence

Journal: Molecular immunology

doi: 10.1016/j.molimm.2009.04.002

Results of gene expression analysis of the nurse shark GcIf in tissues. The size of RT-PCR amplified product is ~977–1025 bp for GcIf-1/-2 (Panel A) and ~909–957 bp for GcIf-1-4 (Panel B). Panel C are results for the positive control of nurse shark beta-actin. Lane 1 is the standard DNA-size marker (λDNA/Hind III fragments, Invitogen), and lanes 2 through 10 are tissue samples; kidney, spleen, brain, liver, intestine, ovary, muscle, heart, and pancreas, respectively. For each panel, conditions of RT-PCR are provided in corresponding parenthesis.
Figure Legend Snippet: Results of gene expression analysis of the nurse shark GcIf in tissues. The size of RT-PCR amplified product is ~977–1025 bp for GcIf-1/-2 (Panel A) and ~909–957 bp for GcIf-1-4 (Panel B). Panel C are results for the positive control of nurse shark beta-actin. Lane 1 is the standard DNA-size marker (λDNA/Hind III fragments, Invitogen), and lanes 2 through 10 are tissue samples; kidney, spleen, brain, liver, intestine, ovary, muscle, heart, and pancreas, respectively. For each panel, conditions of RT-PCR are provided in corresponding parenthesis.

Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Amplification, Positive Control, Marker

37) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

38) Product Images from "Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus"

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus

Journal: Journal of Bacteriology

doi: 10.1128/JB.184.21.5987-5998.2002

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).
Figure Legend Snippet: Schematic of vpma ORFs. The ORFs are represented by boxes and begin with a homologous 25-aa leader sequence (L) followed by regions that have homology between genes or regions that are repeated (R, followed by gene designation, or R' for truncated repeats) within a gene. Homologous regions or repeated sequences are indicated with the same pattern, and unique sequences are not shaded. The percentages of amino acid identity between homologous regions between genes are indicated, and the percentages of similarity are in parentheses. The theoretical molecular mass (kDa), pI, and percentage of charged amino acids, respectively, calculated from the mature polypeptides for VpmaU, VpmaV, VpmaW, VpmaX, VpmaY, and VpmaZ are 23.2, 6.90, and 37%; 35.0, 9.09, and 34%; 33.1, 9.43, and 31%; 22.4, 6.33, and 42%; 35.2, 8.27, and 34%; and 34.2, 7.01, and 32%. Arrowheads indicate possible epitopes involved in host cytadhesion based on those determined for vsps from M. bovis ).

Techniques Used: Sequencing

39) Product Images from "Substance P up-regulates macrophage inflammatory protein-1 ? expression in human T lymphocytes"

Article Title: Substance P up-regulates macrophage inflammatory protein-1 ? expression in human T lymphocytes

Journal: Journal of neuroimmunology

doi:

Effect of SP on the MIP-1β expression in J-SPR T cells. (A) J-SPR T cells were incubated with SP (10 −11 to 10 −7 M) for 3 h and total RNA was isolated and subjected to RT-PCR, electrophoresis (insert), and real-time PCR to quantify MIP-1β mRNA. The data are expressed as mean ± S.D. of triplicate cultures of MIP-1β mRNA copy number per 10 6 copies of GAPDH mRNA. (B) Effect of SP treatment on MIP-1β production in J-SPR T cells. MIP-1β protein was assayed using ELISA. The data shown are presented as mean ± S.D. of triplicate cultures and are representative of three independent experiments.
Figure Legend Snippet: Effect of SP on the MIP-1β expression in J-SPR T cells. (A) J-SPR T cells were incubated with SP (10 −11 to 10 −7 M) for 3 h and total RNA was isolated and subjected to RT-PCR, electrophoresis (insert), and real-time PCR to quantify MIP-1β mRNA. The data are expressed as mean ± S.D. of triplicate cultures of MIP-1β mRNA copy number per 10 6 copies of GAPDH mRNA. (B) Effect of SP treatment on MIP-1β production in J-SPR T cells. MIP-1β protein was assayed using ELISA. The data shown are presented as mean ± S.D. of triplicate cultures and are representative of three independent experiments.

Techniques Used: Expressing, SPR Assay, Incubation, Isolation, Reverse Transcription Polymerase Chain Reaction, Electrophoresis, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay

Time-course of SP on the MIP-1β expression in J-SPR T cells. J-SPR T cells were incubated with (+) or without (−) SP (10 −7 M), and total RNA was isolated from the cells after the indicated amount of time (h). (A) Real-time PCR: MIP-1β mRNA levels were quantified by real-time PCR using the same RNA samples as indicated, and the data are expressed as mean ± S.D. of MIP-1β mRNA copy number per 10 6 copies of GAPDH mRNA. (B) MIP-1β protein was assayed using ELISA. The data shown are presented as mean ± S.D. of triplicate cultures and are representative of three independent experiments.
Figure Legend Snippet: Time-course of SP on the MIP-1β expression in J-SPR T cells. J-SPR T cells were incubated with (+) or without (−) SP (10 −7 M), and total RNA was isolated from the cells after the indicated amount of time (h). (A) Real-time PCR: MIP-1β mRNA levels were quantified by real-time PCR using the same RNA samples as indicated, and the data are expressed as mean ± S.D. of MIP-1β mRNA copy number per 10 6 copies of GAPDH mRNA. (B) MIP-1β protein was assayed using ELISA. The data shown are presented as mean ± S.D. of triplicate cultures and are representative of three independent experiments.

Techniques Used: Expressing, SPR Assay, Incubation, Isolation, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay

Effect of SP antagonist, CP-96,345, on SP-induced MIP-1β expression in J-SPR T cells. (A) J-SPR T cells were incubated with SP (10 −7 M), SP (10 −7 M) plus CP-96,345 (10 −6 M), CP–96,345 (10 −6 M) and without compounds (as control) for 3 h. Cellular RNA was isolated and subjected to RT-PCR, electrophoresis (insert), and real-time RT-PCR to quantify MIP-1β mRNA. The data are expressed as mean ± S.D. of triplicate cultures and are representative of three independent experiments of MIP-1β mRNA copy number per 10 6 copies of GAPDH mRNA. (B) MIP-1β protein was assayed using ELISA. The data shown are presented as mean ± S.D. of triplicate cultures and are representative of three independent experiments.
Figure Legend Snippet: Effect of SP antagonist, CP-96,345, on SP-induced MIP-1β expression in J-SPR T cells. (A) J-SPR T cells were incubated with SP (10 −7 M), SP (10 −7 M) plus CP-96,345 (10 −6 M), CP–96,345 (10 −6 M) and without compounds (as control) for 3 h. Cellular RNA was isolated and subjected to RT-PCR, electrophoresis (insert), and real-time RT-PCR to quantify MIP-1β mRNA. The data are expressed as mean ± S.D. of triplicate cultures and are representative of three independent experiments of MIP-1β mRNA copy number per 10 6 copies of GAPDH mRNA. (B) MIP-1β protein was assayed using ELISA. The data shown are presented as mean ± S.D. of triplicate cultures and are representative of three independent experiments.

Techniques Used: Expressing, SPR Assay, Incubation, Isolation, Reverse Transcription Polymerase Chain Reaction, Electrophoresis, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay

Effect of SP on the MIP-1β production in PBL. PBL isolated from seven healthy donors (D1–D7) were pre-stimulated with PHA for 72 h. The cells were incubated with or without SP (10 −7 M) for 12 h. Total RNA was extracted from PBL isolated from different donors and nested-RT-PCR was performed to amplify NK-1R mRNA (395 bp) (insert). Cell-free supernatants were collected and MIP-1β protein was assayed using ELISA. The data shown are mean ± S.D. of MIP-1β in triplicate cultures. Plus (+) and minus (−) signs indicate presence or absence of SP.
Figure Legend Snippet: Effect of SP on the MIP-1β production in PBL. PBL isolated from seven healthy donors (D1–D7) were pre-stimulated with PHA for 72 h. The cells were incubated with or without SP (10 −7 M) for 12 h. Total RNA was extracted from PBL isolated from different donors and nested-RT-PCR was performed to amplify NK-1R mRNA (395 bp) (insert). Cell-free supernatants were collected and MIP-1β protein was assayed using ELISA. The data shown are mean ± S.D. of MIP-1β in triplicate cultures. Plus (+) and minus (−) signs indicate presence or absence of SP.

Techniques Used: Isolation, Incubation, Reverse Transcription Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay

40) Product Images from "Random Amplified Polymorphic DNA (RAPD) for differentiation between Thai and Myanmar strains of Wuchereria bancrofti"

Article Title: Random Amplified Polymorphic DNA (RAPD) for differentiation between Thai and Myanmar strains of Wuchereria bancrofti

Journal: Filaria Journal

doi: 10.1186/1475-2883-6-6

Random Amplified Polymorphic DNA (RAPD) profile of Thai and Myanmar strains of Wuchereria bancrofti . The RAPD profile of the Thai and Myanmar strains of W. bancrofti using Primer 1 (5'-dGGTGCGGGAA-3'): Lane M: 100 bp DNA marker; Lane 1–6: the Thai strain of W. bancrofti ; Lane 7–12: the Myanmar strain of W. bancrofti ; Lane C: Negative Control (uninfected human blood sample). The 300 bp and 795 bp fragments (arrows) are specific to the Myanmar strain of W. bancrofti . The 645, 705, 1290, and 1400 bp fragments were common in both the Thai and Myanmar strains of W. bancrofti .
Figure Legend Snippet: Random Amplified Polymorphic DNA (RAPD) profile of Thai and Myanmar strains of Wuchereria bancrofti . The RAPD profile of the Thai and Myanmar strains of W. bancrofti using Primer 1 (5'-dGGTGCGGGAA-3'): Lane M: 100 bp DNA marker; Lane 1–6: the Thai strain of W. bancrofti ; Lane 7–12: the Myanmar strain of W. bancrofti ; Lane C: Negative Control (uninfected human blood sample). The 300 bp and 795 bp fragments (arrows) are specific to the Myanmar strain of W. bancrofti . The 645, 705, 1290, and 1400 bp fragments were common in both the Thai and Myanmar strains of W. bancrofti .

Techniques Used: Amplification, Marker, Negative Control

Related Articles

Polymerase Chain Reaction:

Article Title: Characterization of divIVA and Other Genes Located in the Chromosomal Region Downstream of the dcw Cluster in Streptococcus pneumoniae †
Article Snippet: .. PCR products were amplified from the appropriate template DNA by using 1 U of Taq polymerase (Perkin-Elmer) in a Hybaid thermocycler. ..

Article Title: Use of PCR with Universal Primers and Restriction Endonuclease Digestions for Detection and Identification of Common Bacterial Pathogens in Cerebrospinal Fluid
Article Snippet: .. A reaction mixture containing approximately 50 ng of template DNA, PCR buffer (10 mM Tris-HCl, pH 8.3; 50 mM KCl; 2.5 mM MgCl2 ; 0.001% gelatin), a 0.2 μM concentration of each PCR primer, a 0.2 mM concentration of each deoxynucleoside triphosphate, and 2.5 U of Taq DNA polymerase (Perkin-Elmer, Norwalk, Conn.) in a total volume of 50 μl was prepared. ..

Article Title: Tandemization of a Subregion of the Enhancer Sequences from SRS 19-6 Murine Leukemia Virus Associated with T-Lymphoid but Not Other Leukemias
Article Snippet: .. PCR amplification of genomic tumor DNAs was performed in a 100-μl reaction mixture consisting of Taq polymerase buffer (Perkin-Elmer) containing 0.25 mM deoxynucleoside triphosphates, 20 pmol of each primer, 6 mM MgCl2 , 2.5 U of Taq polymerase (Perkin-Elmer), and 1 μg of genomic tumor DNA. .. Each reaction product was amplified by the following PCR schedule: 1 cycle of 94°C for 4 min, 56°C for 1 min, and 72°C for 2 min; 33 cycles of 94°C for 1 min, 56°C for 1 min, and 72°C for 1 min; and 1 cycle of 94°C for 1 min, 56°C for 1 min, and 72°C for 10 min in a Perkin-Elmer thermal cycler.

Article Title: Variation in the Spacer Regions Separating tRNA Genes in Renibacterium salmoninarum Distinguishes Recent Clinical Isolates from the Same Location
Article Snippet: .. PCR amplification was performed in a DNA thermal cycler (Perkin-Elmer). .. The reaction mixture was overlaid with mineral oil (Sigma), incubated at 94°C for 2 min, and then subjected to 44 cycles of 94°C for 30 s, 45°C for 30 s, and 72°C for 90 s and a final cycle of 94°C for 30 s, 45°C for 30 s, and 72°C for 10 min.

Article Title: Use of PCR in Diagnosis of Human American Tegumentary Leishmaniasis in Rio de Janeiro, Brazil
Article Snippet: .. PCR amplification was carried out in a DNA thermocycler (Perkin-Elmer) with 30 cycles of 94°C for 30 s, 50°C for 30 s, and 72°C for 30 s, with a final cycle of 10 min at 72°C. .. All recommended precautions were taken to avoid PCR artifacts.

Article Title: Surface Diversity in Mycoplasma agalactiae Is Driven by Site-Specific DNA Inversions within the vpma Multigene Locus
Article Snippet: .. The PCR cycling conditions for these probes were as follows: 1 cycle of 94°C for 1 min and 28 cycles of 94°C for 20 s, 55°C ( vpmaY ), 60°C ( vpmaW and vpmaX ), 65°C ( vpmaV ), or 70°C ( vpmaU ) for 30 s, and 72°C for 10 s ( vpmaV ), 18 s ( vpmaU , vpmaX , and vpmaY ), or 54 s ( vpmaW and vpmaZ ), followed by 1 cycle at 72°C (performed in a Perkin-Elmer GeneAmp PCR System 2400 thermocycler). .. The PCR cycling conditions for the primer pairs with 55-5 DNA as a template were 1 cycle of 94°C for 1 min and 28 cycles of 94°C for 20 s, 55°C (E2F-E2R) or 60°C (E1F-E1R and H4F-H4R) for 30 s, and 72°C for 18 s, followed by 1 cycle at 72°C for 7 min.

Article Title: Identification of the Major Antigenic Protein of Helicobacter cinaedi and Its Immunogenicity in Humans with H. cinaedi Infections ▿
Article Snippet: .. One of the ORFs found in clone 9-5, which was presumed to encode a 30-kDa major antigenic protein of H. cinaedi , henceforth tentatively called MAP30Hc , was amplified by PCR with a thermal cycler (GeneAmp PCR system 2400; PerkinElmer Inc., Waltham, MA) by using the Expand high-fidelity PCR system (Roche, Hoffman-La Roche Ltd., Basel, Switzerland). .. The template was 200 ng of clone 9-5 plasmid; thermal cycling conditions were 94°C for 2 min and 40 cycles of 94°C for 15 s, 55°C for 30 s, and 68°C for 1 min.

Concentration Assay:

Article Title: Use of PCR with Universal Primers and Restriction Endonuclease Digestions for Detection and Identification of Common Bacterial Pathogens in Cerebrospinal Fluid
Article Snippet: .. A reaction mixture containing approximately 50 ng of template DNA, PCR buffer (10 mM Tris-HCl, pH 8.3; 50 mM KCl; 2.5 mM MgCl2 ; 0.001% gelatin), a 0.2 μM concentration of each PCR primer, a 0.2 mM concentration of each deoxynucleoside triphosphate, and 2.5 U of Taq DNA polymerase (Perkin-Elmer, Norwalk, Conn.) in a total volume of 50 μl was prepared. ..

Amplification:

Article Title: Characterization of divIVA and Other Genes Located in the Chromosomal Region Downstream of the dcw Cluster in Streptococcus pneumoniae †
Article Snippet: .. PCR products were amplified from the appropriate template DNA by using 1 U of Taq polymerase (Perkin-Elmer) in a Hybaid thermocycler. ..

Article Title: Tandemization of a Subregion of the Enhancer Sequences from SRS 19-6 Murine Leukemia Virus Associated with T-Lymphoid but Not Other Leukemias
Article Snippet: .. PCR amplification of genomic tumor DNAs was performed in a 100-μl reaction mixture consisting of Taq polymerase buffer (Perkin-Elmer) containing 0.25 mM deoxynucleoside triphosphates, 20 pmol of each primer, 6 mM MgCl2 , 2.5 U of Taq polymerase (Perkin-Elmer), and 1 μg of genomic tumor DNA. .. Each reaction product was amplified by the following PCR schedule: 1 cycle of 94°C for 4 min, 56°C for 1 min, and 72°C for 2 min; 33 cycles of 94°C for 1 min, 56°C for 1 min, and 72°C for 1 min; and 1 cycle of 94°C for 1 min, 56°C for 1 min, and 72°C for 10 min in a Perkin-Elmer thermal cycler.

Article Title: Variation in the Spacer Regions Separating tRNA Genes in Renibacterium salmoninarum Distinguishes Recent Clinical Isolates from the Same Location
Article Snippet: .. PCR amplification was performed in a DNA thermal cycler (Perkin-Elmer). .. The reaction mixture was overlaid with mineral oil (Sigma), incubated at 94°C for 2 min, and then subjected to 44 cycles of 94°C for 30 s, 45°C for 30 s, and 72°C for 90 s and a final cycle of 94°C for 30 s, 45°C for 30 s, and 72°C for 10 min.

Article Title: Use of PCR in Diagnosis of Human American Tegumentary Leishmaniasis in Rio de Janeiro, Brazil
Article Snippet: .. PCR amplification was carried out in a DNA thermocycler (Perkin-Elmer) with 30 cycles of 94°C for 30 s, 50°C for 30 s, and 72°C for 30 s, with a final cycle of 10 min at 72°C. .. All recommended precautions were taken to avoid PCR artifacts.

Article Title: Identification of the Major Antigenic Protein of Helicobacter cinaedi and Its Immunogenicity in Humans with H. cinaedi Infections ▿
Article Snippet: .. One of the ORFs found in clone 9-5, which was presumed to encode a 30-kDa major antigenic protein of H. cinaedi , henceforth tentatively called MAP30Hc , was amplified by PCR with a thermal cycler (GeneAmp PCR system 2400; PerkinElmer Inc., Waltham, MA) by using the Expand high-fidelity PCR system (Roche, Hoffman-La Roche Ltd., Basel, Switzerland). .. The template was 200 ng of clone 9-5 plasmid; thermal cycling conditions were 94°C for 2 min and 40 cycles of 94°C for 15 s, 55°C for 30 s, and 68°C for 1 min.

Sequencing:

Article Title: Dimerization of ADAR2 is mediated by the double-stranded RNA binding domain
Article Snippet: .. The GFP2 -ADAR2 constructs were created by replacing the EGFP sequence of the EGFP-ADAR2 constructs with the GFP2 sequence form pGFP2 -β-arrestin2 (PerkinElmer). .. To obtain ADAR2 constructs with C-terminal tags, the open reading frames of Renilla luciferase and GFP2 were PCR amplified and inserted into the pcDNA3.1+ vector (Invitrogen) with EcoRI/XbaI and NotI/XhoI restriction sites, respectively.

Construct:

Article Title: Dimerization of ADAR2 is mediated by the double-stranded RNA binding domain
Article Snippet: .. The GFP2 -ADAR2 constructs were created by replacing the EGFP sequence of the EGFP-ADAR2 constructs with the GFP2 sequence form pGFP2 -β-arrestin2 (PerkinElmer). .. To obtain ADAR2 constructs with C-terminal tags, the open reading frames of Renilla luciferase and GFP2 were PCR amplified and inserted into the pcDNA3.1+ vector (Invitrogen) with EcoRI/XbaI and NotI/XhoI restriction sites, respectively.

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    PerkinElmer dna thermal cycler
    Application of <t>DNA</t> polymerase from P. islandicum in <t>PCR.</t> Reactions were carried out in a buffer containing 15 mM Tris-HCl (pH 8.6), 12.5 mM KCl, 2.5 mM (NH 4 ) 2 SO 4 , 1.25 mM MgCl 2 , and 20 μg of BSA per ml. One unit of DNA polymerase from P. islandicum was used to amplify 500 bp (lane 1), 1,000 bp (lane 2), and 1,500 bp (lane 3) of a λ DNA template. Control PCR was performed with 2.5 U of High Fidelity enzyme (lane 4). Twenty microliters of each PCR product was applied on an 1% agarose gel. The corresponding molecular sizes of the marker (lane 5) are indicated in kilobase pairs.
    Dna Thermal Cycler, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 94/100, based on 565 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    PerkinElmer geneamp pcr system 2400
    Application of <t>DNA</t> polymerase from P. islandicum in <t>PCR.</t> Reactions were carried out in a buffer containing 15 mM Tris-HCl (pH 8.6), 12.5 mM KCl, 2.5 mM (NH 4 ) 2 SO 4 , 1.25 mM MgCl 2 , and 20 μg of BSA per ml. One unit of DNA polymerase from P. islandicum was used to amplify 500 bp (lane 1), 1,000 bp (lane 2), and 1,500 bp (lane 3) of a λ DNA template. Control PCR was performed with 2.5 U of High Fidelity enzyme (lane 4). Twenty microliters of each PCR product was applied on an 1% agarose gel. The corresponding molecular sizes of the marker (lane 5) are indicated in kilobase pairs.
    Geneamp Pcr System 2400, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 93/100, based on 350 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/geneamp pcr system 2400/product/PerkinElmer
    Average 93 stars, based on 350 article reviews
    Price from $9.99 to $1999.99
    geneamp pcr system 2400 - by Bioz Stars, 2020-09
    93/100 stars
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    Application of DNA polymerase from P. islandicum in PCR. Reactions were carried out in a buffer containing 15 mM Tris-HCl (pH 8.6), 12.5 mM KCl, 2.5 mM (NH 4 ) 2 SO 4 , 1.25 mM MgCl 2 , and 20 μg of BSA per ml. One unit of DNA polymerase from P. islandicum was used to amplify 500 bp (lane 1), 1,000 bp (lane 2), and 1,500 bp (lane 3) of a λ DNA template. Control PCR was performed with 2.5 U of High Fidelity enzyme (lane 4). Twenty microliters of each PCR product was applied on an 1% agarose gel. The corresponding molecular sizes of the marker (lane 5) are indicated in kilobase pairs.

    Journal: Journal of Bacteriology

    Article Title: Cloning and Characterization of a Family B DNA Polymerase from the Hyperthermophilic Crenarchaeon Pyrobaculum islandicum †

    doi:

    Figure Lengend Snippet: Application of DNA polymerase from P. islandicum in PCR. Reactions were carried out in a buffer containing 15 mM Tris-HCl (pH 8.6), 12.5 mM KCl, 2.5 mM (NH 4 ) 2 SO 4 , 1.25 mM MgCl 2 , and 20 μg of BSA per ml. One unit of DNA polymerase from P. islandicum was used to amplify 500 bp (lane 1), 1,000 bp (lane 2), and 1,500 bp (lane 3) of a λ DNA template. Control PCR was performed with 2.5 U of High Fidelity enzyme (lane 4). Twenty microliters of each PCR product was applied on an 1% agarose gel. The corresponding molecular sizes of the marker (lane 5) are indicated in kilobase pairs.

    Article Snippet: After an initial denaturation step at 94°C for 2 min, 30 cycles with a temperature profile of 10 s at 94°C, 30 s at 46°C, and 90 s at 68°C were performed with a DNA thermal cycler (GeneAmp PCR System 2400; Perkin-Elmer).

    Techniques: Polymerase Chain Reaction, Agarose Gel Electrophoresis, Marker

    Random Amplified Polymorphic DNA (RAPD) profile of Thai and Myanmar strains of Wuchereria bancrofti . The RAPD profile of the Thai and Myanmar strains of W. bancrofti using Primer 1 (5'-dGGTGCGGGAA-3'): Lane M: 100 bp DNA marker; Lane 1–6: the Thai strain of W. bancrofti ; Lane 7–12: the Myanmar strain of W. bancrofti ; Lane C: Negative Control (uninfected human blood sample). The 300 bp and 795 bp fragments (arrows) are specific to the Myanmar strain of W. bancrofti . The 645, 705, 1290, and 1400 bp fragments were common in both the Thai and Myanmar strains of W. bancrofti .

    Journal: Filaria Journal

    Article Title: Random Amplified Polymorphic DNA (RAPD) for differentiation between Thai and Myanmar strains of Wuchereria bancrofti

    doi: 10.1186/1475-2883-6-6

    Figure Lengend Snippet: Random Amplified Polymorphic DNA (RAPD) profile of Thai and Myanmar strains of Wuchereria bancrofti . The RAPD profile of the Thai and Myanmar strains of W. bancrofti using Primer 1 (5'-dGGTGCGGGAA-3'): Lane M: 100 bp DNA marker; Lane 1–6: the Thai strain of W. bancrofti ; Lane 7–12: the Myanmar strain of W. bancrofti ; Lane C: Negative Control (uninfected human blood sample). The 300 bp and 795 bp fragments (arrows) are specific to the Myanmar strain of W. bancrofti . The 645, 705, 1290, and 1400 bp fragments were common in both the Thai and Myanmar strains of W. bancrofti .

    Article Snippet: The RAPD reaction was performed in a DNA thermal cycler (GeneAmp PCR System 2400, Perkin-Elmer, Norwalk, CT), for 1 cycle at 96°C for 4 min, followed by 40 cycles of 94°C for 1 min, 40°C for 1 min and 72°C for 2 min, respectively.

    Techniques: Amplification, Marker, Negative Control