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Promega complementary dna cdna synthesis kit
Complementary Dna Cdna Synthesis Kit, supplied by Promega, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 88 stars, based on 2 article reviews
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complementary dna cdna synthesis kit - by Bioz Stars, 2020-08
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Article Title: Synergistic effect of bromocriptine and tumor necrosis factor-α on reversing hepatocellular carcinoma multidrug resistance in nude mouse MDR1 model of liver neoplasm
Article Snippet: Reverse transcription (RT) was performed with random primers by a complementary DNA (cDNA) synthesis kit (Promega).

Article Title: Correlation of expression of multidrug resistance protein and messenger RNA with 99mTc-methoxyisobutyl isonitrile (MIBI) imaging in patients with hepatocellular carcinoma
Article Snippet: RT was performed with random primers with a complementary DNA (cDNA) synthesis kit (Promega, Madison, WI).

Article Title: Effects of adrenomedullin gene overexpression on biological behavior of hepatic stellate cells
Article Snippet: RT was performed with oligo (dT) primer using a complementary DNA (cDNA) synthesis kit (Promega, German).

Article Title: Nude mice model of human hepatocellular carcinoma via orthotopic implantation of histologically intact tissue
Article Snippet: Reverse transcription ( RT) was performed with random primers using a complementary DNA (cDNA) synthesis kit (promega).

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  • 93
    Promega first strand cdna synthesis kit
    Protective effects of paeoniflorin (PF) on H 2 O 2 -induced differentiated ARPE-19 cells. A : Levels of retinal pigment epithelium 65 (RPE65) and fibroblast growth factor receptor-1 (FGFR-1) mRNA were measured by Reverse transcriptase PCR in undifferentiated (Undiff ARPE-19) and differentiated (Diff ARPE-19) ARPE-19 cells. Total <t>RNA</t> from undifferentiated or differentiated ARPE-19 cells was reverse transcribed and amplified using primers for RPE65 and FGFR1. A reaction omitting the <t>cDNA</t> was used as a negative control (NC). B : Cell viability of differentiated ARPE-19 cells following H 2 O 2 exposure were measured by MTT assay. The cells were treated with or without different concentrations of H 2 O 2 (100–2,000 μM) for 24 h. Cell viability was measured by an MTT assay. The results are expressed as percentage of control, and each value represents the mean±SEM of three independent experiments (n=3 experiments, *p
    First Strand Cdna Synthesis Kit, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 297 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/first strand cdna synthesis kit/product/Promega
    Average 93 stars, based on 297 article reviews
    Price from $9.99 to $1999.99
    first strand cdna synthesis kit - by Bioz Stars, 2020-08
    93/100 stars
      Buy from Supplier

    80
    Promega full length rab cdna
    Mapping of the minimal region of eps15 required for binding to NPF-containing proteins. ( A ) Secondary structure prediction of the amino-terminal region of Eps15 (containing the three EH domains) by a Chou–Fasman–Rose algorithm. (Vertical lines) α-Helices; (thick shaded bars) β-sheets; (thinner solid bars) coils; (small solid boxes) turn. Amino acid positions are also indicated. ( B ) Schematic representation of the Eps15 amino-terminal domain and of the GST fusion proteins engineered, with predicted turns indicated by solid boxes. The indicated fragments of Eps15 were engineered into GST fusion proteins and used for in vitro binding experiments. The EH construct contains all three EH domains. The M2 construct contains the region encompassing the second EH domain flanked by the natural regions pedicting the turns shown in A. Amino acid positions are also indicated in parentheses. ( C ) In vitro bindings. The GST fusions shown in B were used to bind the 35 S-labeled <t>RAB</t> protein, obtained by in vitro transcription/translation of the RAB <t>cDNA.</t> Detection was by autoradiography. The lane marked T/T was loaded with the primary product of the in vitro transcription/translation to serve as a reference. The positions of RAB are also indicated.
    Full Length Rab Cdna, supplied by Promega, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/full length rab cdna/product/Promega
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    full length rab cdna - by Bioz Stars, 2020-08
    80/100 stars
      Buy from Supplier

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    Protective effects of paeoniflorin (PF) on H 2 O 2 -induced differentiated ARPE-19 cells. A : Levels of retinal pigment epithelium 65 (RPE65) and fibroblast growth factor receptor-1 (FGFR-1) mRNA were measured by Reverse transcriptase PCR in undifferentiated (Undiff ARPE-19) and differentiated (Diff ARPE-19) ARPE-19 cells. Total RNA from undifferentiated or differentiated ARPE-19 cells was reverse transcribed and amplified using primers for RPE65 and FGFR1. A reaction omitting the cDNA was used as a negative control (NC). B : Cell viability of differentiated ARPE-19 cells following H 2 O 2 exposure were measured by MTT assay. The cells were treated with or without different concentrations of H 2 O 2 (100–2,000 μM) for 24 h. Cell viability was measured by an MTT assay. The results are expressed as percentage of control, and each value represents the mean±SEM of three independent experiments (n=3 experiments, *p

    Journal: Molecular Vision

    Article Title: Protective effect of paeoniflorin against oxidative stress in human retinal pigment epithelium in vitro

    doi:

    Figure Lengend Snippet: Protective effects of paeoniflorin (PF) on H 2 O 2 -induced differentiated ARPE-19 cells. A : Levels of retinal pigment epithelium 65 (RPE65) and fibroblast growth factor receptor-1 (FGFR-1) mRNA were measured by Reverse transcriptase PCR in undifferentiated (Undiff ARPE-19) and differentiated (Diff ARPE-19) ARPE-19 cells. Total RNA from undifferentiated or differentiated ARPE-19 cells was reverse transcribed and amplified using primers for RPE65 and FGFR1. A reaction omitting the cDNA was used as a negative control (NC). B : Cell viability of differentiated ARPE-19 cells following H 2 O 2 exposure were measured by MTT assay. The cells were treated with or without different concentrations of H 2 O 2 (100–2,000 μM) for 24 h. Cell viability was measured by an MTT assay. The results are expressed as percentage of control, and each value represents the mean±SEM of three independent experiments (n=3 experiments, *p

    Article Snippet: Reverse transcription was then performed by using 100 ng of RNA and the First-Strand cDNA Synthesis kit (Promega, Madison, WI).

    Techniques: Polymerase Chain Reaction, Amplification, Negative Control, MTT Assay

    A, Ethidium bromide-stained agarose gel of dsRNA. Lanes a and b contain dsRNA extracts from two representative strains of Lentinula edodes FMRI0339 mycovirus (LeV-FMRI0339) and Pleurotus ostreatus ASI2792 mycovirus (ASI2792-PoV) with the characteristic 12-kb viral genome of LeV and approximately 8.0-kb viral genome of ASI2792-PoV, respectively. Lanes 1 to 14 contain dsRNA extracts from 14 isolates obtained by the mycelia fragmentation method described in “Materials and Methods”; B, Northern blot analysis of the corresponding gel with the dsRNA using a partial cDNA clone (792 bp) encoding the RNA-dependent RNA polymerase (RdRp) protein in the PoV-ASI2792 as a probe. Arrowheads indicate the mycovirus genome segment from PoV-ASI2792.

    Journal: Mycobiology

    Article Title: Viral Effects of a dsRNA Mycovirus (PoV-ASI2792) on the Vegetative Growth of the Edible Mushroom Pleurotus ostreatus

    doi: 10.5941/MYCO.2016.44.4.283

    Figure Lengend Snippet: A, Ethidium bromide-stained agarose gel of dsRNA. Lanes a and b contain dsRNA extracts from two representative strains of Lentinula edodes FMRI0339 mycovirus (LeV-FMRI0339) and Pleurotus ostreatus ASI2792 mycovirus (ASI2792-PoV) with the characteristic 12-kb viral genome of LeV and approximately 8.0-kb viral genome of ASI2792-PoV, respectively. Lanes 1 to 14 contain dsRNA extracts from 14 isolates obtained by the mycelia fragmentation method described in “Materials and Methods”; B, Northern blot analysis of the corresponding gel with the dsRNA using a partial cDNA clone (792 bp) encoding the RNA-dependent RNA polymerase (RdRp) protein in the PoV-ASI2792 as a probe. Arrowheads indicate the mycovirus genome segment from PoV-ASI2792.

    Article Snippet: Cloning and sequence analysis of the partial RdRp gene To obtain a cDNA clone that corresponded to the mycovirus RdRp, cDNA synthesis was conducted as described procedure using a cDNA synthesis kit (Promega, Fitchburg, WI, USA) and reverse transcription-PCR (RT-PCR) was performed as described previously [ ].

    Techniques: Staining, Agarose Gel Electrophoresis, Northern Blot

    Gel pictures resulting from cathepsin B, cathepsin H, and calpain RT-PCR experiments. Lanes (from the left): 1, 100-bp marker from Promega; 2, PCR control without cDNA; 5, 8, and 11, RT controls for which mRNA was not reverse transcribed; 3 and 4, 6 and 7, and 9 and 10, PCR carried out with, respectively, 0.1 and 0.3 μl of cDNA. (A) Cathepsin H results after 35 cycles of PCR with specific primers annealing at 55°C, which show a slightly higher level of expression in vegetative cells. (B) Cathepsin B results after 35 cycles of PCR with specific primers annealing at 55°C, which show a strong differential expression in vegetative cells. (C) Calpain results after 45 cycles of PCR with specific primers annealing at 55°C, which show an apparent absence of expression in cysts and 1-h excysting cells.

    Journal: Eukaryotic Cell

    Article Title: Cysteine Proteases and Cell Differentiation: Excystment of the Ciliated Protist Sterkiella histriomuscorum

    doi: 10.1128/EC.2.6.1234-1245.2003

    Figure Lengend Snippet: Gel pictures resulting from cathepsin B, cathepsin H, and calpain RT-PCR experiments. Lanes (from the left): 1, 100-bp marker from Promega; 2, PCR control without cDNA; 5, 8, and 11, RT controls for which mRNA was not reverse transcribed; 3 and 4, 6 and 7, and 9 and 10, PCR carried out with, respectively, 0.1 and 0.3 μl of cDNA. (A) Cathepsin H results after 35 cycles of PCR with specific primers annealing at 55°C, which show a slightly higher level of expression in vegetative cells. (B) Cathepsin B results after 35 cycles of PCR with specific primers annealing at 55°C, which show a strong differential expression in vegetative cells. (C) Calpain results after 45 cycles of PCR with specific primers annealing at 55°C, which show an apparent absence of expression in cysts and 1-h excysting cells.

    Article Snippet: RNAs from 2-h excysting cells were extracted, and double-stranded cDNAs were obtained by following the procedures of the manufacturer (cDNA synthesis kit; Promega).

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

    Mapping of the minimal region of eps15 required for binding to NPF-containing proteins. ( A ) Secondary structure prediction of the amino-terminal region of Eps15 (containing the three EH domains) by a Chou–Fasman–Rose algorithm. (Vertical lines) α-Helices; (thick shaded bars) β-sheets; (thinner solid bars) coils; (small solid boxes) turn. Amino acid positions are also indicated. ( B ) Schematic representation of the Eps15 amino-terminal domain and of the GST fusion proteins engineered, with predicted turns indicated by solid boxes. The indicated fragments of Eps15 were engineered into GST fusion proteins and used for in vitro binding experiments. The EH construct contains all three EH domains. The M2 construct contains the region encompassing the second EH domain flanked by the natural regions pedicting the turns shown in A. Amino acid positions are also indicated in parentheses. ( C ) In vitro bindings. The GST fusions shown in B were used to bind the 35 S-labeled RAB protein, obtained by in vitro transcription/translation of the RAB cDNA. Detection was by autoradiography. The lane marked T/T was loaded with the primary product of the in vitro transcription/translation to serve as a reference. The positions of RAB are also indicated.

    Journal: Genes & Development

    Article Title: Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module

    doi:

    Figure Lengend Snippet: Mapping of the minimal region of eps15 required for binding to NPF-containing proteins. ( A ) Secondary structure prediction of the amino-terminal region of Eps15 (containing the three EH domains) by a Chou–Fasman–Rose algorithm. (Vertical lines) α-Helices; (thick shaded bars) β-sheets; (thinner solid bars) coils; (small solid boxes) turn. Amino acid positions are also indicated. ( B ) Schematic representation of the Eps15 amino-terminal domain and of the GST fusion proteins engineered, with predicted turns indicated by solid boxes. The indicated fragments of Eps15 were engineered into GST fusion proteins and used for in vitro binding experiments. The EH construct contains all three EH domains. The M2 construct contains the region encompassing the second EH domain flanked by the natural regions pedicting the turns shown in A. Amino acid positions are also indicated in parentheses. ( C ) In vitro bindings. The GST fusions shown in B were used to bind the 35 S-labeled RAB protein, obtained by in vitro transcription/translation of the RAB cDNA. Detection was by autoradiography. The lane marked T/T was loaded with the primary product of the in vitro transcription/translation to serve as a reference. The positions of RAB are also indicated.

    Article Snippet: [35 S]methionine-labeled RAB protein, employed in the experiments in Figure , was synthesized by in vitro transcription–translation using a commercial kit (Promega) and the full-length RAB cDNA.

    Techniques: Binding Assay, In Vitro, Construct, Labeling, Autoradiography

    Human RAB and RAB-R cDNAs and proteins. ( A ) The structures of the human RAB (hRAB) and RAB-R (hRAB-R) cDNAs are depicted. The ORFs are labeled. Positions are indicated in kb. The nucleotide positions of initatior and terminator codons are also indicated. Canonical polyadenylation sites (AATAAA) are at positions 2499, 2542, and 2556 of the RAB sequence; no polyadenylation site was found in the isolated hRAB-R cDNA (not shown). ( B . In the hRAB-R sequence, only nonidentical amino acids are reported, except for the FG and NPF motifs. Dashes indicate gaps introduced to maximize the alignment. Accepted conservation, employed to calculate relatedness, are D, E, N, Q; L, I, V, M; K, R, H; F, Y, W; and A, G, P, S, T. The FG, zinc-finger, and NPF motifs are indicated in reverse print.

    Journal: Genes & Development

    Article Title: Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module

    doi:

    Figure Lengend Snippet: Human RAB and RAB-R cDNAs and proteins. ( A ) The structures of the human RAB (hRAB) and RAB-R (hRAB-R) cDNAs are depicted. The ORFs are labeled. Positions are indicated in kb. The nucleotide positions of initatior and terminator codons are also indicated. Canonical polyadenylation sites (AATAAA) are at positions 2499, 2542, and 2556 of the RAB sequence; no polyadenylation site was found in the isolated hRAB-R cDNA (not shown). ( B . In the hRAB-R sequence, only nonidentical amino acids are reported, except for the FG and NPF motifs. Dashes indicate gaps introduced to maximize the alignment. Accepted conservation, employed to calculate relatedness, are D, E, N, Q; L, I, V, M; K, R, H; F, Y, W; and A, G, P, S, T. The FG, zinc-finger, and NPF motifs are indicated in reverse print.

    Article Snippet: [35 S]methionine-labeled RAB protein, employed in the experiments in Figure , was synthesized by in vitro transcription–translation using a commercial kit (Promega) and the full-length RAB cDNA.

    Techniques: Labeling, Sequencing, Isolation