BRCA1 Antibody (Mouse mAb) [K2A11]

Application: Reactivity: Human, Mouse

Usage Information

Dilution
WB1:1000 IF1:3000

Application
WB, IP, IHC, IF, ChIP, ELISA

Reactivity
Human, Mouse

Source
Mouse 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
208 kDa

Positive Control	MCF7 cells; HeLa cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
BRCA1 Antibody (Mouse mAb) [K2A11] detects endogenous levels of total BRCA1 protein.

Clone
K2A11

Synonym(s)
BRCA1 DNA repair associated , BRCAI , BRCC1 , BROVCA1 , FANCS , IRIS , PNCA4 , PPP1R53 , PSCP , RNF53

Background
BRCA1 is a nuclear tumor suppressor protein that acts as a central coordinator of the DNA damage response, especially through homologous recombination (HR)-mediated repair of double-strand DNA breaks. Its N-terminal RING domain provides E3 ubiquitin ligase activity by heterodimerizing with BARD1, while its C-terminal tandem BRCT domains recognize phosphorylated serine motifs on partner proteins. This structural organization integrates the two termini into a cohesive unit that governs the timing and specificity of DNA repair. During S and G2 phases, when a double-strand break occurs, BRCA1 is rapidly recruited to the damage site. It antagonizes the 53BP1-associated complex, which would otherwise promote non-homologous end joining (NHEJ), thereby channeling repair toward the more accurate, resection-dependent HR pathway. Together, BRCA1-BARD1 stimulates nucleolytic resection of the DNA ends to generate single-stranded 3’ overhangs, the essential substrate for RAD51 filament assembly. BRCA1 supports RAD51 loading and stabilization onto single-stranded DNA via cooperation with PALB2 and BRCA2, forming a molecular bridge that enables strand invasion into the homologous template, driving synaptic complex formation and strand exchange. The recruitment, activity, and release of BRCA1 are further regulated by post-translational modifications including phosphorylation, ubiquitination, and sumoylation. BRCA1 also associates with stalled replication forks, protecting them from nucleolytic degradation during replication stress. Loss of BRCA1 function shifts DNA repair toward error-prone alternative pathways, resulting in chromosomal rearrangements and genomic instability. This deficiency also underlies the pronounced sensitivity to PARP inhibitors: unresolved lesions collapse into double-strand breaks that cannot be faithfully repaired in the absence of functional HR. Germline mutations in BRCA1 predispose individuals to early-onset breast and ovarian cancers, while dysregulation of BRCA1 activity in sporadic tumors also affects end-resection and RAD51 loading, contributing to tumorigenesis.

Background

BRCA1 is a nuclear tumor suppressor protein that acts as a central coordinator of the DNA damage response, especially through homologous recombination (HR)-mediated repair of double-strand DNA breaks. Its N-terminal RING domain provides E3 ubiquitin ligase activity by heterodimerizing with BARD1, while its C-terminal tandem BRCT domains recognize phosphorylated serine motifs on partner proteins. This structural organization integrates the two termini into a cohesive unit that governs the timing and specificity of DNA repair. During S and G2 phases, when a double-strand break occurs, BRCA1 is rapidly recruited to the damage site. It antagonizes the 53BP1-associated complex, which would otherwise promote non-homologous end joining (NHEJ), thereby channeling repair toward the more accurate, resection-dependent HR pathway. Together, BRCA1-BARD1 stimulates nucleolytic resection of the DNA ends to generate single-stranded 3’ overhangs, the essential substrate for RAD51 filament assembly. BRCA1 supports RAD51 loading and stabilization onto single-stranded DNA via cooperation with PALB2 and BRCA2, forming a molecular bridge that enables strand invasion into the homologous template, driving synaptic complex formation and strand exchange. The recruitment, activity, and release of BRCA1 are further regulated by post-translational modifications including phosphorylation, ubiquitination, and sumoylation. BRCA1 also associates with stalled replication forks, protecting them from nucleolytic degradation during replication stress. Loss of BRCA1 function shifts DNA repair toward error-prone alternative pathways, resulting in chromosomal rearrangements and genomic instability. This deficiency also underlies the pronounced sensitivity to PARP inhibitors: unresolved lesions collapse into double-strand breaks that cannot be faithfully repaired in the absence of functional HR. Germline mutations in BRCA1 predispose individuals to early-onset breast and ovarian cancers, while dysregulation of BRCA1 activity in sporadic tumors also affects end-resection and RAD51 loading, contributing to tumorigenesis.

References
https://pubmed.ncbi.nlm.nih.gov/40480845/ https://pubmed.ncbi.nlm.nih.gov/22306997/

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

Tech Support

Handling Instructions

Tel: +1-832-582-8158 Ext:3

If you have any other enquiries, please leave a message.

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%