Recombinant Epstein-Barr virus DNA polymerase catalytic subunit (BALF5) ,partial CSB-EP355978EFA
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
BALF5DNA polymerase catalytic subunit; EC 2.7.7.7
Species: (Organism)
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Gene Names:
BALF5
Tag info:
N-terminal 6xHis-SUMO-tagged
Target Protein AA Sequence:
MSGGLFYNPFLRPNKGLLKKPDKEYLRLIPKCFQTPGAAGVVDVRGPQPPLCFYQDSLTVVGGDEDGKGMWWRQRAQEGTARPEADTHGSPLDFHVYDILETVYTHEKCAVIPSDKQGYVVPCGIVIKLLGRRKADGASVCVNVFGQQAYFYASAPQGLDVEFAVLSALKASTFDRRTPCRVSVEKVTRRSIMGYGNHAGDYHKITLSHP
Expression Region:
1-210aa
Subcellular Location:
Host nucleus
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
39.2 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Others
Function:
Replicates viral genomic DNA in the late phase of lytic infection, producing long concatemeric DNA. The replication complex is composed of six viral proteins
Involvement in disease:
Relevance:
Replicates viral genomic DNA in the late phase of lytic infection, producing long concateric DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein.
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.
Protein Families:
DNA polymerase type-B family
Reference:
A functional and structural basis for TCR cross-reactivity in multiple sclerosis.Lang H.L.E., Jacobsen H., Ikemizu S., Andersson C., Harlos K., Madsen L., Hjorth P., Sondergaard L., Svejgaard A., Wucherpfennig K., Stuart D.I., Bell J.I., Jones E.Y., Fugger L.Nat. Immunol. 3:940-943(2002)
