53BP1 Antibody [E7B6] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IHC1:200 - 1:800 IF1:1600 - 1:6400

Application
WB, IHC, IF

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
450 kDa

Datasheet & SDS

Biological Description

Specificity
53BP1 Antibody [E7B6] detects endogenous levels of total 53BP1 protein.

Clone
E7B6

Synonym(s)
TP53-binding protein 1, 53BP1, p53‑binding protein 1, p53BP1, TP53BP1

Background
53BP1, or tumor protein p53-binding protein 1, functions as a central mediator in the DNA damage response, originally identified as a p53 transcriptional coactivator and now recognized for orchestrating double-strand break (DSB) repair pathway choice. It features an N-terminal region with multiple ATM/ATR-phosphorylated S/TQ sites, a central oligomerization domain flanked by a GAR motif and LC8-binding site, tandem Tudor domains binding dimethylated histone H4K20, a ubiquitin-dependent recruitment (UDR) motif engaging H2AK15ub, and C-terminal BRCT repeats. Recruitment to DSBs occurs via H4K20me2 and H2AK15ub recognition following RNF8/RNF168 ubiquitination downstream of γH2AX-MDC1, with oligomerization amplifying chromatin binding and ST/Q phosphorylation recruiting effectors Rif1 and PTIP. 53BP1 promotes classical non-homologous end-joining (c-NHEJ) by recruiting Rif1 to block CtIP-dependent 5′ resection, favoring ligation over homology-directed repair (HDR), while PTIP aids NHEJ in BRCA1-deficient contexts; it enhances heterochromatic repair via BRCT-KAP1/EXPAND1 interactions and stimulates DSB mobility/synapsis for efficient joining in CSR and telomere fusion. ATM phosphorylates multiple sites including Ser25/29/166/Ser25, but these prove dispensable for focus formation yet essential for effector binding. 53BP1 ensures G2/M and intra-S checkpoints via p53/Chk2/Brca1 phosphorylation, supports immunoglobulin class switch recombination and V(D)J joining, and maintains telomere stability. Loss impairs G2/M arrest post-IR, reduces Brca1 foci, and shifts repair toward HDR, sensitizing to PARP inhibitors in BRCA1-null settings while promoting synthetic lethality reversal.

Background

53BP1, or tumor protein p53-binding protein 1, functions as a central mediator in the DNA damage response, originally identified as a p53 transcriptional coactivator and now recognized for orchestrating double-strand break (DSB) repair pathway choice. It features an N-terminal region with multiple ATM/ATR-phosphorylated S/TQ sites, a central oligomerization domain flanked by a GAR motif and LC8-binding site, tandem Tudor domains binding dimethylated histone H4K20, a ubiquitin-dependent recruitment (UDR) motif engaging H2AK15ub, and C-terminal BRCT repeats. Recruitment to DSBs occurs via H4K20me2 and H2AK15ub recognition following RNF8/RNF168 ubiquitination downstream of γH2AX-MDC1, with oligomerization amplifying chromatin binding and ST/Q phosphorylation recruiting effectors Rif1 and PTIP. 53BP1 promotes classical non-homologous end-joining (c-NHEJ) by recruiting Rif1 to block CtIP-dependent 5′ resection, favoring ligation over homology-directed repair (HDR), while PTIP aids NHEJ in BRCA1-deficient contexts; it enhances heterochromatic repair via BRCT-KAP1/EXPAND1 interactions and stimulates DSB mobility/synapsis for efficient joining in CSR and telomere fusion. ATM phosphorylates multiple sites including Ser25/29/166/Ser25, but these prove dispensable for focus formation yet essential for effector binding. 53BP1 ensures G2/M and intra-S checkpoints via p53/Chk2/Brca1 phosphorylation, supports immunoglobulin class switch recombination and V(D)J joining, and maintains telomere stability. Loss impairs G2/M arrest post-IR, reduces Brca1 foci, and shifts repair toward HDR, sensitizing to PARP inhibitors in BRCA1-null settings while promoting synthetic lethality reversal.

References
https://pubmed.ncbi.nlm.nih.gov/24094932/ https://pubmed.ncbi.nlm.nih.gov/12364621/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%