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HDAC2 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IF, IHC-P, E |
|---|---|
| Primary Accession | Q92769 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 55364 Da |
| Antigen Region | 456-488 aa |
| Gene ID | 3066 |
|---|---|
| Other Names | Histone deacetylase 2, HD2, HDAC2 |
| Target/Specificity | This HDAC2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 456-488 amino acids from the C-terminal region of human HDAC2. |
| Dilution | IF~~1:10~50 WB~~1:1000 IHC-P~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation 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 (C-term) 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} |
|---|---|
| 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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Provided below are standard protocols that you may find useful for product applications.
Background
Histone deacetylase 2 (HDAC2), or transcriptional regulator homolog RPD3 L1, is highly homologous to the yeast transcription factor RPD3 (reduced potassium dependency 3) gene. As in yeast, human HDA2 is likely to be involved in regulating chromatin structure during transcription. It has been implicated to associate with YY1, a mammalian zinc-finger transcription factor, which negatively regulates transcription by tethering RPD3 to DNA as a cofactor. This process is highly conserved from yeast to human.
References
Choi, Y.B., et al., J. Biol. Chem. 279(49):50930-50941 (2004).
Zhu, P., et al., Cancer Cell 5(5):455-463 (2004).
Longworth, M.S., et al., J. Virol. 78(7):3533-3541 (2004).
Lu, Y., et al., J. Biol. Chem. 278(48):47792-47802 (2003).
Verdin, E., et al., Trends Genet. 19(5):286-293 (2003).
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