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>   首页   >   产品   >   一抗   >   心血管   >   HDAC7 Antibody (C-term)   

HDAC7 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - HDAC7 Antibody (C-term) AP1107a
    Western blot analysis of hHDAC7-A935 (Cat. #AP1107a) in CEM cell line lysates (35ug/lane). HDAC7 (arrow) was detected using the purified Pab.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q8WUI4
Other Accession NP_056216
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Additional info
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 920-952 amino acids from the C-terminal region of human HDAC7.
Dilution WB~~1:1000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
StorageMaintain 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.
PrecautionsHDAC7 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
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). 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. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. 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.
Cellular Location Nucleus. Cytoplasm. Note=In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. Treatment with EDN1 results in shuttling from the nucleus to the perinuclear region. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation
Research Areas

BACKGROUND

Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins (1). Eight members of HDAC family have been identified in the past several years (2,3). These HDAC family members are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about two-fold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns (3). These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

REFERENCES

Meinke PT and Liberator P. Curr Med Chem, 8(2): 211- 235 (2001).
Nakayama T and Takami Y. J Biochem (Tokyo) 129 (4): 491-499 (2001).
Cress, W.D. and Seto, E. J. Cell. Physiol. 184, 1-16 (2000).

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