Anti-XRCC5 Antibody (3S578) is a Mouse antibody targeting XRCC5. Anti-XRCC5 Antibody (3S578) can be used in WB,ICC/IF.

IgG1, Kappa

3S578

Human

1. Cell line: HeLa
Fixative: 100% Ice-cold methanol
Permeabilization: 0.1% TritonX-100
Primary ab dilution: 1:50
Primary incubation condition: 4°C overnight Nuclear counter stain: DAPI (Blue)
Counter stain: Tubulin (Red)
Comment: Color green is the positive signal for TMAB-14222
2. Blocking buffer: 5% NFDM/TBST
Primary ab dilution: 1:1000
Primary ab incubation condition: 4°C overnight
Lysate: HeLa, Jurkat, A549
Protein loading quantity: 20 μg
Exposure time: 30 s
Predicted MW: 86 kDa
Observed MW: 86 kDa

WB: 1:500-2000; ICC/IF: 1:50-200

Monoclonal

XRCC5

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. 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. 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.