Anti-Phospho-Ku70/XRCC6 (Ser5) Polyclonal Antibody is a Rabbit antibody targeting Phospho-Ku70/XRCC6 (Ser5). Anti-Phospho-Ku70/XRCC6 (Ser5) Polyclonal Antibody can be used in WB,IHC-P,IHC-Fr,IF.

IgG

Mouse (predicted:Human)

1. Sample:
Lane 1: Mouse Heart tissue lysates
Lane 2: Human HL-60 cell lysates
Primary: Anti-phospho-Ku70 (Ser5) (TMAB-10900) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
Predicted band size: 70 kDa
Observed band size: 70 kDa
2. Paraformaldehyde-fixed, paraffin embedded (Mouse testis); Antigen retrieval by boiling in sodium citrate buffer (pH6.0) for 15 min; Block endogenous peroxidase by 3% hydrogen peroxide for 20 minutes; Blocking buffer (normal goat serum) at 37°C for 30 min; Antibody incubation with (phospho-Ku70 (Ser5)) Polyclonal Antibody, Unconjugated (TMAB-10900) at 1:400 overnight at 4°C, followed by operating according to SP Kit (Rabbit) instructions and DAB staining.

WB: 1:500-2000; IHC-P: 1:100-500; IHC-Fr: 1:100-500; IF: 1:100-500

Polyclonal

KLH conjugated synthesised phosphopeptide: human Ku70 around the phosphorylation site of Ser5

Human

XRCC6

X-ray repair cross-complementing protein 6

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. Required for osteocalcin gene expression. 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. 5'-dRP lyase activity 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.