BRE Antibody [F1N20] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000-1:10000 IHC1:50-1:100 IF1:50-1:100

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 Observed MW
44 kDa 44 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
BRE Antibody [F1N20] detects endogenous levels of total BRE protein.

Clone
F1N20

Synonym(s)
BRCC45, BRE, BABAM2, BRISC and BRCA1-A complex member 2, BRCA1-A complex subunit BRE, BRCA1/BRCA2-containing complex subunit 45, Brain and reproductive organ-expressed protein

Background
BRCC45/BRE is a conserved adaptor protein that functions as a core subunit of both the BRCA1‑A DNA damage–response complex and the BRISC deubiquitinase complex, placing it at the interface of Lys63‑linked ubiquitin signaling, homologous recombination repair, mitotic spindle control, and interferon receptor regulation. The protein lacks recognizable catalytic domains and belongs to a BRE‑like family defined by an N‑terminal BRE domain and C‑terminal low‑complexity regions that support stable incorporation into BRCA1‑A and BRISC cores together with BRCC36, MERIT40, and Abraxas‑family scaffold proteins. Within the nuclear BRCA1‑A complex, BRCC45/BRE cooperates with RAP80, Abraxas‑1, BRCC36, and MERIT40 to recognize Lys63‑linked polyubiquitin chains on histones H2A and H2AX at sites of DNA double‑strand breaks, and acts as an adaptor that bridges BABAM1/NBA1 to the rest of the complex, a role that is essential for complex integrity, efficient ubiquitin binding, and recruitment and positioning of the BRCA1–BARD1 E3 ligase at damaged chromatin. BRCA1‑A–associated BRCC36 provides deubiquitinase activity that specifically removes Lys63‑linked ubiquitin from H2A/H2AX, and BRCC45/BRE modulates this activity by stabilizing the holoenzyme architecture and coordinating histone deubiquitination with BRCA1 sequestration and checkpoint control during G2/M DNA damage responses. As a cytoplasmic counterpart, the BRISC complex consists of BRCC45/BRE, BRCC36, MERIT40, and Abraxas‑2 and functions as a Lys63‑specific deubiquitinase that trims but does not completely remove Lys63 chains from substrates involved in stress and immune signaling. BRISC deubiquitinates the type I interferon receptor IFNAR1, increases IFNAR1 stability and surface expression, and down‑regulates the amplitude and duration of responses to bacterial lipopolysaccharide by limiting ubiquitin‑mediated receptor turnover, thereby shaping tonic and induced interferon signaling. BRISC also deubiquitinates the mitotic spindle organizer NuMA1, and BRCC45/BRE is required for BRISC‑dependent control of mitotic spindle assembly and proper microtubule–kinetochore attachment, functions that couple ubiquitin editing to chromosome segregation fidelity. BRE/BRCC45 additionally influences the stability of the cell‑cycle phosphatase CDC25A by recruiting the deubiquitinase USP7 to CDC25A after DNA damage, which counteracts ubiquitin‑dependent CDC25A degradation and modulates checkpoint adaptation in BRCA2‑deficient backgrounds. BRCC45/BRE is expressed in brain and reproductive organs and is distributed in both cytoplasm and nucleus; it acts as a death‑receptor‑associated anti‑apoptotic protein that binds TNFR1 complexes and inhibits BID‑mediated mitochondrial apoptosis, and shows overexpression in hepatocellular carcinoma and altered levels in other malignancies, where its roles in BRCA1‑A, BRISC, and USP7–CDC25A axes support survival, DNA repair capacity, and proliferative signaling.

Background

BRCC45/BRE is a conserved adaptor protein that functions as a core subunit of both the BRCA1‑A DNA damage–response complex and the BRISC deubiquitinase complex, placing it at the interface of Lys63‑linked ubiquitin signaling, homologous recombination repair, mitotic spindle control, and interferon receptor regulation. The protein lacks recognizable catalytic domains and belongs to a BRE‑like family defined by an N‑terminal BRE domain and C‑terminal low‑complexity regions that support stable incorporation into BRCA1‑A and BRISC cores together with BRCC36, MERIT40, and Abraxas‑family scaffold proteins. Within the nuclear BRCA1‑A complex, BRCC45/BRE cooperates with RAP80, Abraxas‑1, BRCC36, and MERIT40 to recognize Lys63‑linked polyubiquitin chains on histones H2A and H2AX at sites of DNA double‑strand breaks, and acts as an adaptor that bridges BABAM1/NBA1 to the rest of the complex, a role that is essential for complex integrity, efficient ubiquitin binding, and recruitment and positioning of the BRCA1–BARD1 E3 ligase at damaged chromatin. BRCA1‑A–associated BRCC36 provides deubiquitinase activity that specifically removes Lys63‑linked ubiquitin from H2A/H2AX, and BRCC45/BRE modulates this activity by stabilizing the holoenzyme architecture and coordinating histone deubiquitination with BRCA1 sequestration and checkpoint control during G2/M DNA damage responses. As a cytoplasmic counterpart, the BRISC complex consists of BRCC45/BRE, BRCC36, MERIT40, and Abraxas‑2 and functions as a Lys63‑specific deubiquitinase that trims but does not completely remove Lys63 chains from substrates involved in stress and immune signaling. BRISC deubiquitinates the type I interferon receptor IFNAR1, increases IFNAR1 stability and surface expression, and down‑regulates the amplitude and duration of responses to bacterial lipopolysaccharide by limiting ubiquitin‑mediated receptor turnover, thereby shaping tonic and induced interferon signaling. BRISC also deubiquitinates the mitotic spindle organizer NuMA1, and BRCC45/BRE is required for BRISC‑dependent control of mitotic spindle assembly and proper microtubule–kinetochore attachment, functions that couple ubiquitin editing to chromosome segregation fidelity. BRE/BRCC45 additionally influences the stability of the cell‑cycle phosphatase CDC25A by recruiting the deubiquitinase USP7 to CDC25A after DNA damage, which counteracts ubiquitin‑dependent CDC25A degradation and modulates checkpoint adaptation in BRCA2‑deficient backgrounds. BRCC45/BRE is expressed in brain and reproductive organs and is distributed in both cytoplasm and nucleus; it acts as a death‑receptor‑associated anti‑apoptotic protein that binds TNFR1 complexes and inhibits BID‑mediated mitochondrial apoptosis, and shows overexpression in hepatocellular carcinoma and altered levels in other malignancies, where its roles in BRCA1‑A, BRISC, and USP7–CDC25A axes support survival, DNA repair capacity, and proliferative signaling.

References
pmc.ncbi.nlm.nih.gov/articles/PMC4802329/ https://pubmed.ncbi.nlm.nih.gov/29416040/

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%