Human XRCC5 & XRCC6 recombinant protein

Human XRCC5 & XRCC6 recombinant protein

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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). {PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488}.

X-ray repair cross-complementing protein 5

G22P2

P13010

XRCC5; G22P2

Baculovirus-Insect Cells

A DNA sequence encoding the XRCC5 (P13010) (Met 1-Ile 732) was fused with a polyhistidine tag at the N-terminus, constructed the plasmid 1; A DNA sequence encoding the XRCC6 (P12956) (Met 1-Asp 609) was fused with a polyhistidine tag at the N-terminus, constructed the plasmid 2. The two plasmids were co-expressed and the heterodimer was purified.

Human

The recombinant heterodimer of human XRCC5/XRCC5 comprises 1379 (751 + 628) amino acids and has a calculated molecular mass of 157 (85 + 72) kDa. The apparent molecular mass of rh XRCC5/XRCC5 heterodimer is approximately 70 & 85 kDa respectively in SDS-PAGE under reducing conditions.

> 90 % as determined by SDS-PAGE