Anti-histone deacetylase 8 HDAC8 Antibody Picoband® fluoro488 Vervoeging

HDAC8, Histone deacetylase 8, is an enzyme that in humans is encoded by the HDAC8 gene, and is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Sequence analysis predicted that the 377-amino acid HDAC8 protein contains the 9 conserved HDAC blocks that are presumably important for catalytic function. HDAC8 shares 54% sequence similarity with HDAC1 and HDAC2 and 39% similarity with HDAC3, making it a class I HDAC. 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 I of the histone deacetylase/acuc/apha family. It has histone deacetylase activity and represses transcription when tethered to a promoter.

Histone deacetylase 8; HD8;3.5.1.98; HDAC8; HDACL1; CDA07

HDAC8

55869

Q9BY41

Human, Mouse, Rat

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the N-terminus of human HDAC8, different from the related mouse and rat sequences by two amino acids.

Weakly expressed in most tissues. Expressed at higher level in heart, brain, kidney and pancreas and also in liver, lung, placenta, prostate and kidney. .

Flow Cytometry

Transcription

Immunogen affinity purified.

Liquid

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. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. .

1. Buggy, J. J., Sideris, M. L., Mak, P., Lorimer, D. D., McIntosh, B., Clark, J. M.Cloning and characterization of a novel human histone deacetylase, HDAC8.Biochem. J. 350: 199-205, 2000. 2. Hu, E., Chen, Z., Fredrickson, T., Zhu, Y., Kirkpatrick, R., Zhang, G.-F., Johanson, K., Sung, C.-M., Liu, R., Winkler, J.Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor.J. Biol. Chem. 275: 15254-15264, 2000. 3. Vannini, A., Volpari, C., Filocamo, G., Casavola, E. C., Brunetti, M., Renzoni, D., Chakravarty, P., Paolini, C., De Francesco, R., Gallinari, P., Steinkuhler, C., Di Marco, S.Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor.Proc. Nat. Acad. Sci. 101: 15064-15069, 2004.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

41758 MW

No cross reactivity with other proteins.

6

Histone deacetylase 8

Nucleus. Cytoplasm. Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation.

Histone deacetylase 8 (HD8)

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.