5 Antibody

Code CSB-PA365450XA01EEB
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Product Details

Full Product Name
Rabbit anti-Enterobacteria phage T7 (Bacteriophage T7) 5 Polyclonal antibody
Uniprot No.
Target Names
5
Alternative Names
5DNA-directed DNA polymerase antibody; EC 2.7.7.7 antibody; EC 3.1.11.- antibody; Gene product 5 antibody; Gp5 antibody
Raised in
Rabbit
Species Reactivity
Enterobacteria phage T7 (Bacteriophage T7)
Immunogen
Recombinant Enterobacteria phage T7 (Bacteriophage T7) 5 protein
Immunogen Species
Enterobacteria phage T7 (Bacteriophage T7)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
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 (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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Target Background

Function
Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction. Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.
Gene References into Functions
  1. Data suggest replication loop is released at nick formed in lagging-strand DNA when polymerase (gp5) encounters previously synthesized Okazaki fragment (OF), releasing lagging-strand DNA, and retaining gp5 at replication fork for synthesis of next OF. PMID: 26620561
  2. Results suggest that the interaction between the C-terminal tail of the helicase and the basic patch of gp5 is critical for initiation of strand-displacement synthesis. PMID: 21606333
  3. Small angle X-ray scattering studies combined with nuclease footprinting reveal two conformations of T7 DNA polymerase, one in the free state and one upon binding to E. coli thioredoxin PMID: 20696935
  4. single-molecule imaging approach to visualize the interaction of fluorescently labeled T7 DNA polymerase with double-stranded DNA PMID: 20080681
  5. the thioredoxin-binding domain is a molecular switch that regulates the interaction of T7 DNA polymerase with other proteins of the replisome PMID: 15795374
  6. Escherichia coli thioredoxin, the processivity factor, binds with bacteriophage T7 DNA polymerase and helicase PMID: 18757858
  7. Results describe the nucleotidyl transfer reaction mechanism in the well-characterized high-fidelity replicative DNA polymerase from phage T7. PMID: 19389406

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Protein Families
DNA polymerase type-A family
Database Links

KEGG: vg:1261044

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