DBC1 Antibody [E8N20] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:40 IHC1:2000 IF1:500 FCM1:700

Application
WB, IP, IHC, IF, FCM

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
103 kDa 130 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
DBC1 Antibody [E8N20] detects endogenous levels of total DBC1 protein.

Clone
E8N20

Synonym(s)
DBC1, KIAA1967, CCAR2, Cell cycle and apoptosis regulator protein 2, Cell division cycle and apoptosis regulator protein 2, DBIRD complex subunit KIAA1967, Deleted in breast cancer gene 1 protein, NET35, p30 DBC, DBC-1, DBC.1

Background
DBC1 (Deleted in Breast Cancer 1, also known as CCAR2/KIAA1967) is a large nuclear protein that functions as a multifunctional scaffold at the interface of chromatin regulation, transcriptional control, and stress signaling, where it integrates epigenetic modifiers, nuclear receptors, and checkpoint pathways to coordinate cell survival and genome integrity. The protein contains an N‑terminal S1-like RNA-binding domain, a central coiled-coil and leucine zipper region, and C‑terminal domains that include nuclear localization sequences and interaction motifs for partners such as SIRT1, HDAC3, PARP1, Rev-erbα, p53, and BRCA1, allowing DBC1 to assemble protein complexes that modulate acetylation status, transcriptional activity, and cell-cycle progression. DBC1 binds directly to the catalytic domain of SIRT1 and acts as an endogenous inhibitor of its deacetylase activity, maintaining higher acetylation of substrates such as p53 and thereby sustaining p53-dependent transcriptional programs and apoptotic competence under basal and genotoxic stress conditions. The interaction between DBC1 and SIRT1 is dynamic and responds to cellular energetic status: elevations in cAMP and activation of PKA and AMPK pathways induce dissociation of the DBC1–SIRT1 complex without changing NAD⁺ levels, which leads to increased SIRT1 activity and connects metabolic signaling to shifts in deacetylase output. DBC1 also interacts with the nuclear receptor Rev-erbα and stabilizes this core clock and metabolic regulator by limiting its ubiquitination and proteasomal degradation, enhancing Rev-erbα-mediated transcriptional repression of clock and metabolic genes and placing DBC1 within the circuitry that shapes circadian and metabolic transcription. Through additional binding to HDAC3, ERα, BRCA1, and components of NF‑κB and alternative NF‑κB pathways, DBC1 modulates hormone-dependent gene expression, DNA-damage responses, and B cell activation, acting as a context-dependent regulator that can either restrain or facilitate transcriptional programs linked to proliferation, apoptosis, and inflammation. Altered DBC1 expression or post-translational modification, including ATM/ATR‑dependent phosphorylation in response to DNA damage, associates with defects in SIRT1 control, p53 stability, and checkpoint signaling, and DBC1 is described as a tumor-suppressive factor in several settings through its role in p53 regulation and repression of oncogenic transcriptional drivers, while also participating in inflammatory and autoimmune pathogenesis through effects on NF‑κB-related networks.

Background

DBC1 (Deleted in Breast Cancer 1, also known as CCAR2/KIAA1967) is a large nuclear protein that functions as a multifunctional scaffold at the interface of chromatin regulation, transcriptional control, and stress signaling, where it integrates epigenetic modifiers, nuclear receptors, and checkpoint pathways to coordinate cell survival and genome integrity. The protein contains an N‑terminal S1-like RNA-binding domain, a central coiled-coil and leucine zipper region, and C‑terminal domains that include nuclear localization sequences and interaction motifs for partners such as SIRT1, HDAC3, PARP1, Rev-erbα, p53, and BRCA1, allowing DBC1 to assemble protein complexes that modulate acetylation status, transcriptional activity, and cell-cycle progression. DBC1 binds directly to the catalytic domain of SIRT1 and acts as an endogenous inhibitor of its deacetylase activity, maintaining higher acetylation of substrates such as p53 and thereby sustaining p53-dependent transcriptional programs and apoptotic competence under basal and genotoxic stress conditions. The interaction between DBC1 and SIRT1 is dynamic and responds to cellular energetic status: elevations in cAMP and activation of PKA and AMPK pathways induce dissociation of the DBC1–SIRT1 complex without changing NAD⁺ levels, which leads to increased SIRT1 activity and connects metabolic signaling to shifts in deacetylase output. DBC1 also interacts with the nuclear receptor Rev-erbα and stabilizes this core clock and metabolic regulator by limiting its ubiquitination and proteasomal degradation, enhancing Rev-erbα-mediated transcriptional repression of clock and metabolic genes and placing DBC1 within the circuitry that shapes circadian and metabolic transcription. Through additional binding to HDAC3, ERα, BRCA1, and components of NF‑κB and alternative NF‑κB pathways, DBC1 modulates hormone-dependent gene expression, DNA-damage responses, and B cell activation, acting as a context-dependent regulator that can either restrain or facilitate transcriptional programs linked to proliferation, apoptosis, and inflammation. Altered DBC1 expression or post-translational modification, including ATM/ATR‑dependent phosphorylation in response to DNA damage, associates with defects in SIRT1 control, p53 stability, and checkpoint signaling, and DBC1 is described as a tumor-suppressive factor in several settings through its role in p53 regulation and repression of oncogenic transcriptional drivers, while also participating in inflammatory and autoimmune pathogenesis through effects on NF‑κB-related networks.

References
https://pubmed.ncbi.nlm.nih.gov/23398316/ https://pubmed.ncbi.nlm.nih.gov/18235502/

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%