BRCA1 Antibody [N12F20] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:50

Application
WB, IP

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
220 kDa

Positive Control	HT-29 cells; HeLa cells; MCF7 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
BRCA1 Antibody [N12F20] detects endogenous levels of total BRCA1 protein.

Clone
N12F20

Synonym(s)
Breast cancer type 1 susceptibility protein; RING finger protein 53; RING-type E3 ubiquitin transferase BRCA1; BRCA1; RNF53

Background
BRCA1 (Breast Cancer 1), encoded by the tumor suppressor gene mutated in hereditary breast and ovarian cancer syndrome, functions primarily as a scaffold coordinator of homologous recombination (HR) repair by recruiting PALB2, BRCA2, and RAD51 to double-strand breaks while repressing error-prone non-homologous end joining (NHEJ) during S and G2 phases, thereby maintaining genomic stability through cell cycle checkpoint activation and chromatin remodeling. BRCA1 (approximately 1863 amino acids) features an N-terminal RING domain with a Cys3HisCys4 motif (Cys24, Cys27, Cys37 catalytic for E2 ubiquitin ligase activity), central BRCT domains that contain phospho-serine binding pockets with conserved Ser988 and Ser1423 recognition sites, and multiple SQ/TQ phosphorylation sites (such as Ser1387 and Ser1524 targeted by ATM/ATR) that dynamically regulate protein interactions during the DNA damage response. BRCA1 orchestrates HR repair by ubiquitinylating histone H2A to recruit repair factors, phosphorylates CtIP to promote end resection and the creation of 3'-single-stranded DNA tails for RAD51 loading, activates the G2/M checkpoint via Chk1/2, and transcriptionally represses proliferation genes through p53 and BARD1 interactions. BRCA1 undergoes hyperphosphorylation during late G1/S (at Aurora A/CDK2 target sites Ser308 and Ser1497), peaking in M phase before partial dephosphorylation in early G1. Inactivating mutations (over 3000 identified) abolish HR capacity, causing accumulation of double-strand breaks, genomic instability, and tumorigenesis with a lifetime risk of breast cancer and ovarian cancer.

Background

BRCA1 (Breast Cancer 1), encoded by the tumor suppressor gene mutated in hereditary breast and ovarian cancer syndrome, functions primarily as a scaffold coordinator of homologous recombination (HR) repair by recruiting PALB2, BRCA2, and RAD51 to double-strand breaks while repressing error-prone non-homologous end joining (NHEJ) during S and G2 phases, thereby maintaining genomic stability through cell cycle checkpoint activation and chromatin remodeling. BRCA1 (approximately 1863 amino acids) features an N-terminal RING domain with a Cys3HisCys4 motif (Cys24, Cys27, Cys37 catalytic for E2 ubiquitin ligase activity), central BRCT domains that contain phospho-serine binding pockets with conserved Ser988 and Ser1423 recognition sites, and multiple SQ/TQ phosphorylation sites (such as Ser1387 and Ser1524 targeted by ATM/ATR) that dynamically regulate protein interactions during the DNA damage response. BRCA1 orchestrates HR repair by ubiquitinylating histone H2A to recruit repair factors, phosphorylates CtIP to promote end resection and the creation of 3'-single-stranded DNA tails for RAD51 loading, activates the G2/M checkpoint via Chk1/2, and transcriptionally represses proliferation genes through p53 and BARD1 interactions. BRCA1 undergoes hyperphosphorylation during late G1/S (at Aurora A/CDK2 target sites Ser308 and Ser1497), peaking in M phase before partial dephosphorylation in early G1. Inactivating mutations (over 3000 identified) abolish HR capacity, causing accumulation of double-strand breaks, genomic instability, and tumorigenesis with a lifetime risk of breast cancer and ovarian cancer.

References
https://pubmed.ncbi.nlm.nih.gov/27542409/ https://pubmed.ncbi.nlm.nih.gov/24451979/

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%