1 Antibody

Rare Species
Code CSB-PA018353XA01EEB
Size US$299
Image
  • Western Blot
    Positive WB detected in: recombinant protein
    All lanes: 1 Antibody at 1:1000
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 30 kDa
    Observed band size: 30 kDa
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Product Details

Uniprot No.
Target Names
1
Alternative Names
T7 RNA polymerase (DNA-directed RNA polymerase) (EC 2.7.7.6) 1
Species Reactivity
Enterobacteria phage T7 (Bacteriophage T7)
Immunogen
Recombinant Enterobacteria phage T7 (Bacteriophage T7) 1 protein (710-805aa)
Immunogen Species
Enterobacteria phage T7 (Bacteriophage T7)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Affinity-chromatography
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Description

To produce polyclonal antibodies against Enterobacteria phage T7 (Bacteriophage T7) 1 protein (T7 gp1), a rabbit undergoes repetitive immunizations with recombinant Enterobacteria phage T7 (Bacteriophage T7) 1 protein (710-805aa). Upon reaching an optimal antibody titer, the rabbit is bled, and antibodies are purified from the serum using affinity chromatography. The functionality of the resulting T7 gp1 antibody is subsequently evaluated through ELISA and WB applications, demonstrating its ability to interact with Enterobacteria phage T7 (Bacteriophage T7) 1 protein.

The Enterobacteria phage T7 1 protein is a crucial component during the early stages of the phage infection cycle. The T7 gp1 protein interacts with the T7 RNA polymerase, enhancing its specificity for the T7 phage promoters and preventing it from indiscriminately binding to host bacterial DNA. This ensures that the transcriptional machinery is accurately targeted to the phage genes, facilitating the efficient expression of phage genes and enabling the replication of the phage within the host bacterium during the infection process.

Usage
For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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Target Background

Function
Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Plays also a role in viral DNA packaging, probably by pausing the transcription at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process.
Gene References into Functions
  1. Using correlation analysis, it was found that the promoter strength characterized by reporter gene expression was closely correlated with rupture force and the binding percentage of T7 RNA polymerase by force spectroscopy. PMID: 29187520
  2. From the docking of the minimum energy representative structures of T7 lysozyme at different pH strengths (obtained from the free energy landscape analysis) with T7RNAP structures at same pH strengths, we saw strong interaction patterns at pH 7.9 and pH 5. PMID: 28545576
  3. Data suggest that comparative transcriptional fidelities/mutation rates for DNA-directed RNA polymerases are as follows: human mitochondrial POLRMT [2x10(-5)]; Saccharomyces cerevisiae mitochondrial Rpo41 [6x10(-6)]; phage T7 single-subunit RNA polymerase [2x10(-6)]. PMID: 28882896
  4. Molecular dynamics simulation study described the behavior of the two magnesium ions in RNAP activity during genetic transcription. PMID: 28205291
  5. The control of the discrimination between dNTP and rNTP in DNA and RNA polymerases has been described. PMID: 27480935
  6. The study provides evidence that the intrinsic infidelity of T7 RNAP in transcription brings significant phenotypic consequences, observed as frameshift mutation restoration and the production of a heterogenous population of the full-length protein. PMID: 25824942
  7. We show here that DNA-protein cross-links constitute strong but not absolute blocks to in vitro transcription catalyzed by T7 RNAP. PMID: 22235136
  8. Hydrogen bonds of RNA polymerase play an important role in the efficiency of transcription. PMID: 22044042
  9. introducing a nuclear transgene, ST7, encoding a light-regulated plastid-targeted T7RNAP by cross-pollination. PMID: 15517992
  10. T7 promoter-polymerase interaction weakening facilitates promoter release PMID: 15711016
  11. An amino acid substitution weakens promoter binding but markedly reduces abortive cycling over a variety of initial sequences. PMID: 15831591
  12. structure activity relationship PMID: 16301518
  13. Active T7RNAP elongation by showing that both rapidly elongating and halted complexes are equally sensitive to pyrophosphate. PMID: 16516229
  14. Collapse of the DNA from the downstream end of the bubble is a major contributor to the characteristic instability of the abortive T7 RNA polymerase transcription complex. PMID: 16790422
  15. Poto-regulation of transcription reaction by azobenzene-tethered promoter was attributed to the change of binding property of RNAP to the promoter by trans-cis isomerization of azobenzene. PMID: 17150558
  16. transition to an elongation complex by T7 RNA polymerase is a multistep process PMID: 17548349
  17. site-specifically tethered chemical nucleases and functional characterization of directed T7 RNAP mutants to both reveal the architecture of the duplex DNA PMID: 17580086
  18. G-rich sequences located in the transcribed strand do not affect transcription by either polymerase, but when the sequences are located in the non-transcribed strand, they partially arrest both polymerases PMID: 18292094
  19. study reports crystal structures of T7 RNAP bound to promoter DNA containing either a 7- or an 8-nucleotide (nt) RNA transcript that illuminate intermediate states along the transition pathway PMID: 18948533

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Protein Families
Phage and mitochondrial RNA polymerase family
Database Links

KEGG: vg:1261050

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