XRCC5 Antibody

Cusabio

XRCC5 Antibody

20

ImmunoPrecipitation, Western Blot, ELISA, ImmunoHistoChemistry

Research Use Only

Polyclonal

Unconjugated

XRCC5

X-ray repair cross complementing 5

86 kDa subunit of Ku antigen; ATP-dependent DNA helicase 2 subunit 2; ATP-dependent DNA helicase II 80 kDa subunit; CTC box-binding factor 85 kDa subunit; CTC85; CTCBF; DNA repair protein XRCC5; KARP1; KARP-1; Ku autoantigen, 80kDa; KU80; Ku86; Ku86 autoantigen related protein 1; KUB2; lupus Ku autoantigen protein p86; NFIV; nuclear factor IV; thyroid-lupus autoantigen; TLAA; X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining); X-ray repair cross-complementing protein 5

Rabbit

IgG

X-ray repair cross-complementing protein 5

Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3\\\-5\\\ direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:20383123). The XRCC5/6 dimer probably also acts as a 5\\\-deoxyribose-5-phosphate lyase (5\\\-dRP lyase), by catalyzing the beta-elimination of the 5\\\ deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5\\\-dRP activity, and allows to \\\clean\\\ the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488).

Human

-20°C or -80°C

12352203