plasmid dna (Boehringer Mannheim)
86
Structured Review
Boehringer Mannheim
plasmid dna
Plasmid Dna, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/plasmid dna/product/Boehringer Mannheim
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
Plasmid Dna, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/plasmid dna/product/Boehringer Mannheim
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
plasmid dna - by Bioz Stars,
2021-03
86/100 stars
Images
1) Product Images from "Identification of a Haemophilus influenzae 5?-Nucleotidase Protein: Cloning of the nucA Gene and Immunogenicity and Characterization of the NucA Protein"
Article Title: Identification of a Haemophilus influenzae 5?-Nucleotidase Protein: Cloning of the nucA Gene and Immunogenicity and Characterization of the NucA Protein
Journal: Infection and Immunity
doi:
Figure Legend Snippet: Complete nucleotide and amino acid sequences of NucA. The presumed ribosome binding site is labeled RBS. Amino acids are listed starting with the initiation codon, methionine. The signal sequence is underlined, and the start codon, lysine, of the mature sequence is shown by an arrow. The locations of various restriction sites are displayed above the sequence. The boxed region demarcates the region of strong protein homology observed among known 5′-nucleotidases. Arrows below the DNA sequence at the 3′ end of the gene depict an inverted-repeat region. ORF, open reading frame.
Techniques Used: Binding Assay, Labeling, Sequencing
2) Product Images from "PTTG/securin activates expression of p53 and modulates its function"
Article Title: PTTG/securin activates expression of p53 and modulates its function
Journal: Molecular Cancer
doi: 10.1186/1476-4598-3-18
![Electrophoretic mobility shift assays show the binding of c-myc protein to the c-myc/max sequence. A : Nuclear extract prepared from HEK293 cells transfected either with pcDNA3.1 (lane 1) or pcDNA3.1- PTTG (lane 2) and [ 32 P]-labeled p53 gene promoter sequence carrying a normal c-myc/max binding site. Addition of a 20-fold molar excess of specific unlabeled DNA resulted in almost complete disappearance of the DNA-protein complex (lane 3). An arrow indicates the specific DNA-protein complex. B : Nuclear extracts prepared from HEK293 cells transfected either with pcDNA3.1 (lane 1) or pcDNA3.1- PTTG (lane 2) and [ 32 P]-labeled p53 promoter sequence carrying a normal c-myc/max binding site. Addition of antibody directed against the N-terminal of c-myc resulted in a supershift (lane 3, indicated by an arrow) whereas no supershift was obtained when the [ 32 P]-labeled-D-172/-89 c-myc sequence was used as a probe (lane 5). Addition of antibodies directed against the C-terminal of c-myc did not result in supershift (lanes 4 6) when either of the probes was used in the binding reaction indicating that C-terminal of c-myc is not assessable. N.S indicates non-specific complex.](https://storage.googleapis.com/bioz_article_images/PMC479695/1476-4598-3-18-5.jpg "... of a 20-fold molar excess of specific unlabeled DNA resulted in almost complete disappearance of the DNA-protein ...")
Figure Legend Snippet: Electrophoretic mobility shift assays show the binding of c-myc protein to the c-myc/max sequence. A : Nuclear extract prepared from HEK293 cells transfected either with pcDNA3.1 (lane 1) or pcDNA3.1- PTTG (lane 2) and [ 32 P]-labeled p53 gene promoter sequence carrying a normal c-myc/max binding site. Addition of a 20-fold molar excess of specific unlabeled DNA resulted in almost complete disappearance of the DNA-protein complex (lane 3). An arrow indicates the specific DNA-protein complex. B : Nuclear extracts prepared from HEK293 cells transfected either with pcDNA3.1 (lane 1) or pcDNA3.1- PTTG (lane 2) and [ 32 P]-labeled p53 promoter sequence carrying a normal c-myc/max binding site. Addition of antibody directed against the N-terminal of c-myc resulted in a supershift (lane 3, indicated by an arrow) whereas no supershift was obtained when the [ 32 P]-labeled-D-172/-89 c-myc sequence was used as a probe (lane 5). Addition of antibodies directed against the C-terminal of c-myc did not result in supershift (lanes 4 6) when either of the probes was used in the binding reaction indicating that C-terminal of c-myc is not assessable. N.S indicates non-specific complex.
Techniques Used: Electrophoretic Mobility Shift Assay, Binding Assay, Sequencing, Transfection, Labeling
3) Product Images from "Functional Interaction between the pp71 Protein of Human Cytomegalovirus and the PML-Interacting Protein Human Daxx"
Article Title: Functional Interaction between the pp71 Protein of Human Cytomegalovirus and the PML-Interacting Protein Human Daxx
Journal: Journal of Virology
doi: 10.1128/JVI.76.11.5769-5783.2002
Figure Legend Snippet: Delineation of the pp71 interaction domain within hDaxx. (A, B, and C) Yeast cells were transformed with two separate vectors, one of which encoded either PML as a positive control (A) or pp71 (C) fused to the GAL4 DNA-binding domain. The second plasmid encoded amino- or carboxy-terminal fragments of hDaxx as fusion with the GAL4 activation domain; the amino acids contained in the respective deletion mutants are indicated in panel B. Yeast colonies were selected for the presence of both plasmids on dropout medium lacking tryptophane and leucine and subsequently analyzed for the expression of β-galactosidase by filter lift assays. As negative controls, the activation domain vector pGAD424 (pGAD) was either transformed with the pp71 or the PML DNA-binding domain fusion (lanes 11, panels A and C, respectively). The pp71 interaction domain within hDaxx is depicted by the box. (D) Interaction between pp71 and hDaxx deletion mutants after coimmunoprecipitation from 293 cells. The hDaxx mutants were precipitated with the anti-FLAG monoclonal antibody; therafter, bound pp71 protein was detected in Western blot experiments employing the anti-myc antibody. Lanes: 1, lysates from untransfected cells; 2, transfection with plasmid myc-pp71 alone; 3, transfection with vector FLAG-hDaxx alone; 4, transfection with a combination of vectors encoding myc-pp71 and FLAG-hDaxx; 5, transfection with a plasmid encoding FLAG-hDaxx 43-501; 6, transfection with vectors encoding myc-pp71 and FLAG-hDaxx 43-501; 7, transfection with vector FLAG-hDaxx 43-371; 8, transfection with a combination of vectors myc-pp71 and FLAG-hDaxx 43-371; 9, transfection with a plasmid expressing FLAG-hDaxx 197-439; 10, transfection with vectors encoding myc-pp71 and FLAG-hDaxx 197-439; 11, transfection with plasmid FLAG-hDaxx 371-740; 12, transfection with a combination of vector myc-pp71 and FLAG-hDaxx 371-740; 13, transfection with a plasmid encoding FLAG-hDaxx 538-740; 14, transfection with vectors expressing myc-pp71 and FLAG-hDaxx 538-740. (E) Western blot analysis of the cell lysates used for immunoprecipitation in panel D. The expression of the hDaxx deletion mutants was investigated with the anti-FLAG monoclonal antibody. Molecular masses are indicated in kilodaltons. Abbreviations: IP, immunoprecipitation; wb, Western blot; IgG, immunoglobulin G.
Techniques Used: Transformation Assay, Positive Control, Binding Assay, Plasmid Preparation, Activation Assay, Expressing, Western Blot, Transfection, Immunoprecipitation
4) Product Images from "Transient Expression of Cellular Polypyrimidine-Tract Binding Protein Stimulates Cap-Independent Translation Directed by Both Picornaviral and Flaviviral Internal Ribosome Entry Sites In Vivo"
Article Title: Transient Expression of Cellular Polypyrimidine-Tract Binding Protein Stimulates Cap-Independent Translation Directed by Both Picornaviral and Flaviviral Internal Ribosome Entry Sites In Vivo
Journal: Molecular and Cellular Biology
doi:
Figure Legend Snippet: Immunoblot detection of PTB in transfected BS-C-1 and Huh-7 cells in comparison to increases in translation directed by the wt IRES of HAV. (A) Relative expression of renilla luciferase (RLuc) following DNA transfection of cells with a dicistronic plasmid expressing wt PTB from the upstream cistron, compared with a matched control plasmid encoding the PTB null mutant, Δ87-531, in the upstream cistron. RLuc was translated from the downstream cistron by a cap-independent process under control of the wt 5′NTR of HAV. Transfection was by a liposome-mediated procedure. (B) Immunoblot analysis of BS-C-1 and Huh-7 cells following DNA transfection under conditions identical to those used in panel A with monocistronic plasmids expressing either wt PTB or the null mutant, Δ87-531. C, cytoplasmic fraction; N, nuclear fraction.
Techniques Used: Transfection, Expressing, Luciferase, Plasmid Preparation, Mutagenesis
Figure Legend Snippet: Northern blot analysis of the poly(A) fraction of RNA extracted from BS-C-1 cells following DNA transfection with constructs containing the HAV IRES, pPwt/AC (lane 1), or its related null mutant pΔ87-531/AC (lane 2). Lane 3 was loaded with RNA from mock-transfected cells. The probe for hybridization was complementary to the CAT sequence.
Techniques Used: Northern Blot, Transfection, Construct, Mutagenesis, Hybridization, Sequencing
5) Product Images from "Pax8 has a key role in thyroid cell differentiation"
Article Title: Pax8 has a key role in thyroid cell differentiation
Journal: Proceedings of the National Academy of Sciences of the United States of America
doi:
Figure Legend Snippet: Analysis of the transcriptional properties of Pax8 splicing isoforms. ( A ) Northern blot analysis of total RNA prepared from PCPy cells stably transfected with Pax8 splicing isoforms. Tg expression was analyzed in two different pools of clones for each transfected DNA. The GAPDH hybridization was used to normalize the amount of RNA present in each lane. ( B ) Reverse transcription–PCR analysis of cDNA derived from total RNA from the same cells as in A . Pax8 expression was analyzed in two different pools of clones for each transfected DNA.
Techniques Used: Northern Blot, Stable Transfection, Transfection, Expressing, Clone Assay, Hybridization, Polymerase Chain Reaction, Derivative Assay
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![Fig. 2. hHR6A is a CDK substrate in vitro and is phosphorylated during the G 2 /M cell cycle phase in vivo . ( A ) Purified His 6 -hHR6A (top panel) or GST–pRb 773–928 (bottom panel) was incubated in the presence of [γ- 32 P]ATP, in either the absence (Control) or presence of purified cyclin D1–CDK4, cyclin E–CDK2, cyclin A–CDK2, cyclin A–CDK1 or cyclin B–CDK1, resolved by SDS–PAGE and visualized by autoradiography. ( B ) CHO cells transfected with either pCMV-Tag2 vector (Control) or pCMV-Tag2-hHR6A (hHR6A) were labelled with [ 32 P]phosphate and incubated with either dimethylsulfoxide (left and middle lanes) or 50 µM roscovitine (right lane) during the labelling period. Following labelling, hHR6A was immunoprecipitated, separated by SDS–PAGE and visualized by autoradiography. ( C ) CHO cells transfected with pCMV-Tag2-hHR6A (hHR6A) were synchronized by blocking in the G 2 /M cell cycle phase with nocodazole, then initiated to re-enter the cell cycle by nocodazole removal, harvested at various time points for DNA analysis by flow cytometry, and the proportion of cells in G 1 , S and G 2 M phases determined. ( D ) CHO cells transfected with either pCMV-Tag2 vector (Control) or pCMV-Tag2-hHR6A (hHR6A) were synchronized by blocking in the G 2 /M cell cycle phase with nocodazole (time = 0), initiated to re-enter the cell cycle by nocodazole removal and then lysed at various time points (as indicated). The cells were pulse-labelled with [ 32 P]phosphate for 3 h prior to lysis. Following lysis, hHR6A was immunoprecipitated, separated by SDS–PAGE and visualized by autoradiography (upper panel) or western blotting with an anti-FLAG antibody (lower panel). Phosphorylated hHR6A and the co-immunoprecipitating phosphoprotein (asterisk) are indicated with arrows.](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC125963/bin/cdf187f2a.jpg)