menu
Your Cart

ITP0125

ITP0125
ITP0125-2
ITP0125
ITP0125-2
ITP0125
  • Catalog: ITP0125
  • Gene/Protein: HDAC4
  • Product Description: Immunotag™ HDAC4 (phospho Ser632) Polyclonal Antibody
490.0000
Price in reward points: 490

Available Options

Immunotag™ HDAC4 (phospho Ser632) Polyclonal Antibody
Antibody Specification
Datasheet
Target Protein HDAC4 (Ser632)
Clonality Polyclonal
Storage/Stability -20°C/1 year
Application WB,ELISA
Recommended Dilution Western Blot: 1/500 - 1/2000. ELISA: 1/20000. Not yet tested in other applications.
Concentration 1 mg/ml
Reactive Species Human,Mouse,Rat
Host Species Rabbit
Immunogen Synthesized phospho-peptide around the phosphorylation site of human HDAC4 (phospho Ser632)
Specificity Phospho-HDAC4 (S632) Polyclonal Antibody detects endogenous levels of HDAC4 protein only when phosphorylated at S632.
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen
Form Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Gene Name HDAC4
Accession No. P56524 Q6NZM9 Q99P99
Alternate Names HDAC4; KIAA0288; Histone deacetylase 4; HD4
Description histone deacetylase 4(HDAC4) Homo sapiens 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 belongs to class II of the histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. This protein does not bind DNA directly, but through transcription factors MEF2C and MEF2D. It seems to interact in a multiprotein complex with RbAp48 and HDAC3. [provided by RefSeq, Jul 2008],
Cell Pathway/ Category Protein_Acetylation
Protein Expression Brain,Testis,
Subcellular Localization histone deacetylase complex,nucleus,nucleoplasm,cytoplasm,cytosol,transcriptional repressor complex,Z disc,neuromuscular junction,A band,actomyosin,protein complex,
Protein Function catalytic activity:Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.,domain:The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.,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 via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D.,PTM:Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632. Phosphorylation at other residues is required for the interaction with 14-3-3.,PTM:Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.,similarity:Belongs to the histone deacetylase family. Type 2 subfamily.,subcellular location:Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-246, Ser-467 and Ser-632 by CaMK4. The nuclear localization probably depends on sumoylation.,subunit:Interacts with HDAC7 (By similarity). Homodimer. Homodimerization via its N-terminal domain. Interacts with MEF2C, AHRR, and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B (By similarity). Interacts with KDM5B.,tissue specificity:Ubiquitous.,
Usage For Research Use Only! Not for diagnostic or therapeutic procedures.
Material Safety Data Sheet
English_US
Danish
Dutch
English_UK
French
German
Spanish
Norwegian
Portuguese
Finnish
Swedish
Polish

Write a review

Note: HTML is not translated!
Bad Good
Captcha

CONNECT WITH US