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HDAC7 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, WB, E |
|---|---|
| Primary Accession | Q8WUI4 |
| Other Accession | NP_056216.2, NP_001091886.1 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 102927 Da |
| Antigen Region | 846-875 aa |
| Gene ID | 51564 |
|---|---|
| Other Names | Histone deacetylase 7, HD7, Histone deacetylase 7A, HD7a, HDAC7, HDAC7A |
| Target/Specificity | This HDAC7 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 846-875 amino acids from the C-terminal region of human HDAC7. |
| Dilution | 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 purified through a protein A column, followed by peptide affinity purification. |
| 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 | HDAC7 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | HDAC7 |
|---|---|
| Synonyms | HDAC7A |
| Function | Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). 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). Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C (By similarity). During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene (PubMed:12239305). Positively regulates the transcriptional repressor activity of FOXP3 (PubMed:17360565). Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (PubMed:28167758). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758). Also acetylates non-histone proteins, such as ALKBH5 (PubMed:37369679). |
| Cellular Location | Nucleus. Cytoplasm Note=In the nucleus, it associates with distinct subnuclear dot-like structures (PubMed:11262386). Shuttles between the nucleus and the cytoplasm (PubMed:16980613). In muscle cells, it shuttles into the cytoplasm during myocyte differentiation (By similarity). The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation (PubMed:16980613) {ECO:0000250|UniProtKB:Q8C2B3, ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:16980613} |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to mouse HDAC7 gene whose protein promotes repression mediated via the transcriptional corepressor SMRT. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Margariti, A., et al. Circ. Res. 106(7):1202-1211(2010)
Hutt, D.M., et al. Nat. Chem. Biol. 6(1):25-33(2010)
Malik, S., et al. Mol. Cell. Biol. 30(2):399-412(2010)
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
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