DBC 1 Antibody (YA956)(PBS only)
(Synonyms: DBC1; DBC-1; NET35; p30DBC; p30 DBC; KIAA1967)DBC 1 Antibody (YA956) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to DBC 1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-F, IHC-P, ICC/IF, IP
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Reactivity :
Human
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
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Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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IHC-F
IHC-F: Immunohistochemistry-Frozen
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IP
IP: Immunoprecipitation
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|---|---|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:50-1:100 | 1:50-1:200 | 1:20 |
Product Details
DBC 1 Antibody (YA956) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to DBC 1.
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Host Rabbit
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 130 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 103 kDa
A synthetic peptide of human DBC-1
Affinity Purified
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
DBC 1 core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis. Inhibits SUV39H1 methyltransferase activity. Mediates ligand-dependent transcriptional activation by nuclear hormone receptors. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress. Regulates the circadian expression of the core clock components NR1D1 and BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation. Represses the ligand-dependent transcriptional activation function of ESR2. Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1. Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization. Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway. Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3. Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2. Represses the transcriptional activator activity of BRCA1. Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15].
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Subcellular Localization
Nucleus; Cytoplasm; Cytoplasm, cytoskeleton, spindle
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Expression
Tissue_specificity:It is expressed in gastric cancer tissues, and its expression level gradually increases with the progression of cancer (protein level) . It is widely expressed in normal tissues. It is expressed in 84% to 100% of breast cancer, lung cancer, and colon cancer tumor tissues. -
Isoforms & Post-Translational Modification
Q8N163 has 2 isomers: Q8N163-1: 102902 Da (predicted); Q8N163-2: 103143 Da (predicted).
ATM/ATR-mediated phosphorylation at Thr-454 upon DNA damage promotes binding to SIRT1. Phosphorylation at Thr-454 promotes its sumoylation by switching the binding partner of CCAR2 from SENP1 to PIAS3;Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity;Genotoxic stress induces its sumoylation and sumoylation promotes the SIRT1-CCAR2 interaction which in turn inhibits SIRT1-mediated deacetylation of p53/TP53. Sumoylation leads to transcriptional activation of p53/TP53 by sequestering SIRT1 from p53/TP53. Desumoylated by SENP1 -
Subunit
Component of the DBIRD complex (PubMed:22446626). Interacts with ZNF326/ZIRD; the interaction is direct (PubMed:22446626).
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SwissProt ID
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Synonyms
DBC1; DBC-1; NET35; p30DBC; p30 DBC; KIAA1967
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Research Field
Epigenetics and Nuclear Signaling
Documentation
References
[1]. Close P, et al. DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation. Nature. 2012 Mar 25;484(7394):386-9. [Content Brief]
[2]. Kim JE, et al. DBC1 is a negative regulator of SIRT1. Nature. 2008 Jan 31;451(7178):583-6. [Content Brief]
[3]. Zhao W, et al. Negative regulation of the deacetylase SIRT1 by DBC1. Nature. 2008 Jan 31;451(7178):587-90. [Content Brief]
[4]. Kim W, et al. Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of breast cancer cells through impaired responses to UV-induced DNA damage. Cancer Lett. 2013 Jun 10;333(2):180-6. [Content Brief]
[5]. Li Z, et al. Inhibition of SUV39H1 methyltransferase activity by DBC1. J Biol Chem. 2009 Apr 17;284(16):10361-6. [Content Brief]
[6]. Garapaty S, et al. Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation. J Biol Chem. 2009 Mar 20;284(12):7542-52. [Content Brief]
[7]. Chini CC, et al. DBC1 (Deleted in Breast Cancer 1) modulates the stability and function of the nuclear receptor Rev-erbα. Biochem J. 2013 May 1;451(3):453-61. [Content Brief]
[8]. Koyama S, et al. Repression of estrogen receptor beta function by putative tumor suppressor DBC1. Biochem Biophys Res Commun. 2010 Feb 12;392(3):357-62. [Content Brief]
[9]. Nin V, et al. Deleted in breast cancer 1 (DBC1) protein regulates hepatic gluconeogenesis. J Biol Chem. 2014 Feb 28;289(9):5518-27. [Content Brief]
[10]. Chini CC, et al. HDAC3 is negatively regulated by the nuclear protein DBC1. J Biol Chem. 2010 Dec 24;285(52):40830-7. [Content Brief]
[11]. Pangon L, et al. MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm. Int J Cancer. 2015 Jan 1;136(1):55-64. [Content Brief]
[12]. Sakurabashi A, et al. CCAR2 negatively regulates nuclear receptor LXRα by competing with SIRT1 deacetylase. J Steroid Biochem Mol Biol. 2015 May;149:80-8. [Content Brief]
[13]. Qin B, et al. DBC1 functions as a tumor suppressor by regulating p53 stability. Cell Rep. 2015 Mar 3;10(8):1324-34. [Content Brief]
[14]. Hiraike H, et al. Identification of DBC1 as a transcriptional repressor for BRCA1. Br J Cancer. 2010 Mar 16;102(6):1061-7. [Content Brief]
[15]. Magni M, et al. Chk2 and REGγ-dependent DBC1 regulation in DNA damage induced apoptosis. Nucleic Acids Res. 2014 Dec 1;42(21):13150-60. [Content Brief]
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