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Products Polyclonal Anti-HDAC8
| Catalogue number: | PA1591 |
| Price: | $200.00 |
| Reactivities: | Human, Mouse, Rat |
| Applications: | Immunohistochemistry, Western Blot |
| Size: | 100ug/vial |
| Gene: | HDAC8 |
| Swiss prot: | Q9BY41 |
| Form: | Lyophilized |
| Format: | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
| Storage temp: | At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing. |
| Scientific background: | 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. |
| References: | 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. |
| Additional info: | A synthetic peptide mapping at the N-terminal of human HDAC8,, different from the related mouse and rat sequences by two amino acids. |
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