Recombinant Enterobacteria phage RB69 DNA polymerase (43), partial

Code CSB-YP655714ELM
MSDS
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Source Yeast
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Code CSB-EP655714ELM-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP655714ELM
MSDS
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Source Baculovirus
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Code CSB-MP655714ELM
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
43
Uniprot No.
Alternative Names
43DNA-directed DNA polymerase; EC 2.7.7.7; EC 3.1.11.-; Gp43
Species
Enterobacteria phage RB69 (Bacteriophage RB69)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose.
Gene References into Functions
  1. Co(2+) and Mn(2+) enhanced ground-state binding of both correct and incorrect dNTPs to RB69pol:dideoxy-terminated primer-template complexes. PMID: 27096230
  2. Data indicate that alanine replacement of residues distant from the active site of the replicative RB69 DNA polymerase renders the enzyme incapable of sustaining phage replication in vivo. PMID: 24116139
  3. structures of the various RB69pol ternary complexes can be used to rationalize the results obtained from pre-steady-state kinetic assays[review] PMID: 24720884
  4. Determined is the crystal structure of the dATP/tC(o)-containing ternary complex of the RB69 DNA polymerase Y567A mutant at 1.9 A resolution; the incoming dATP formed two hydrogen bonds with an imino-tautomerized form of tC(o). PMID: 22616982
  5. evaluated the contribution of minor groove hydrogen bonding interactions with RB69pol PMID: 22571765
  6. The miscoding potential of 5-hydroxycytosine arises due to template instability in the DNA polymerase active site. PMID: 22026756
  7. The authors show that the S565G/Y567A mutant generally had greater base selectivity than the Y567A mutant and that the kinetic parameters for dNMP insertion, excision of the 3'-terminal nucleotide residue, and primer extension beyond a mispair differed. PMID: 21216248
  8. The structure of an RB69 pol ternary complex at 1.8 A is reported. A network of five highly ordered, buried water molecules can be seen to interact with the N3 and O2 atoms in the minor groove of the DNA duplex. PMID: 21158418
  9. When Y567A and S565G replacements were combined, mutator activity was strongly decreased compared to that with Y567A replacement alone. PMID: 20950625
  10. Data describe the crystal structures of the pol alpha family RB69 DNA polymerase with DNA containing the two most prevalent, spontaneously generated premutagenic lesions PMID: 15057282
  11. Results describe the structure of the bacteriophage RB69 replicative DNA polymerase attempting to process an abasic site analog. PMID: 15057283
  12. The Y619F substitution would disrupt the hydrogen bond network at the primer terminus and may affect the alignment of the 3' primer terminus at the polymerase active site, slowing chemistry and overall DNA synthesis. PMID: 17321543
  13. Binding of a metal ion to the A site is required for the nucleotidyl transfer reaction, but is insufficient to initiate the enzyme isomerization. Binding of a dNTP, in the absence of a metal ion, is sufficient to induce this conformational change. PMID: 19228036
  14. The effect of A and B metal ion site occupancy on the rates of Fingers closing and on the affinity of Rh.dTTP for the E.D binary complex of the catalytic site of RB69 DNA polymerase was studied. PMID: 19228037

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Protein Families
DNA polymerase type-B family
Database Links

KEGG: vg:1494172

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