HDAC2 Antibody (Center)
Purified Mouse Monoclonal Antibody (Mab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | Q92769 |
Reactivity | Human, Mouse |
Host | Mouse |
Clonality | Monoclonal |
Calculated MW | H=55 KDa |
Isotype | IgG1 |
Antigen Source | HUMAN |
Gene ID | 3066 |
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Antigen Region | 202-488 aa |
Other Names | Histone deacetylase 2, HD2, HDAC2 |
Dilution | WB~~1:1000 |
Target/Specificity | This HDAC2 antibody is generated from a mouse immunized with a recombinant protein between 202-488 amino acids from the Central region of human HDAC2. |
Format | Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | HDAC2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | HDAC2 {ECO:0000303|PubMed:10545197, ECO:0000312|HGNC:HGNC:4853} |
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Function | Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR (PubMed:12724404). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Component of the SIN3B complex that represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). Also deacetylates non-histone targets: deacetylates TSHZ3, thereby regulating its transcriptional repressor activity (PubMed:19343227). May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation (By similarity). Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A (PubMed:21965678). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2- hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation and de-2- hydroxyisobutyrylation, respectively (PubMed:28497810, PubMed:29192674). |
Cellular Location | Nucleus. Cytoplasm |
Tissue Location | Widely expressed; lower levels in brain and lung. |
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Background
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.
References
Yang W.-M.,et al.Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mungall A.J.,et al.Nature 425:805-811(2003).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Schmidt D.R.,et al.Biochemistry 38:14711-14717(1999).
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