Histone deacetylase 8, HD8, Hdac8.
Greater than 90.0% as determined by SDS-PAGE.
HDAC8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 383 amino acids (1-377 a.a.) and having a molecular mass of 42.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
HDAC8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Histone deacetylase 8 (HDAC8) is a class 1 member of the histone deacetylase/acuc/apha family. This enzyme plays a crucial role in skull development and the regulation of the ERR-alpha/PGC1-alpha transcriptional complex, which is involved in metabolic processes. Histones, proteins that interact with DNA, are essential for controlling gene expression, cell cycle progression, and developmental processes. The acetylation and deacetylation of histones modify the structure of chromosomes, influencing how easily transcription factors can access and regulate DNA.
Recombinant HDAC8 Mouse, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 383 amino acids (with amino acids 1-377 being specifically identified) and has a molecular weight of 42.5 kDa. Under reducing conditions on SDS-PAGE, it migrates between 40-57 kDa. This HDAC8 protein is expressed with a 6 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
The HDAC8 protein solution is supplied at a concentration of 0.25 mg/ml. It is prepared in a buffer consisting of Phosphate Buffered Saline at a pH of 7.4 and contains 10% glycerol.
Analysis by SDS-PAGE indicates that the purity of this product is greater than 90%.
Histone deacetylase 8, HD8, Hdac8.
MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY DCPATEGIFD YAAAIGGGTI TAAQCLIDGK CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY YHICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVVHHH HHH.
Histone deacetylase 8 (HDAC8) is an enzyme that plays a crucial role in the regulation of gene expression through the modification of chromatin structure. This enzyme is part of the histone deacetylase family, which is involved in the removal of acetyl groups from lysine residues on histone proteins. The mouse recombinant version of HDAC8 is a valuable tool for research, providing insights into its function and potential therapeutic applications.
HDAC8 belongs to class I of the histone deacetylase family. The recombinant mouse HDAC8 is produced in Sf9 Baculovirus cells and consists of a single, glycosylated polypeptide chain containing 383 amino acids, with a molecular mass of approximately 42.5 kDa . This enzyme is known for its histone deacetylase activity, which involves the removal of acetyl groups from histone proteins, leading to a more condensed chromatin structure and repression of gene transcription .
Histone deacetylation by HDAC8 plays a critical role in various cellular processes, including transcriptional regulation, cell cycle progression, and developmental events . By altering the acetylation status of histones, HDAC8 affects the accessibility of transcription factors to DNA, thereby influencing gene expression. This enzyme is also involved in skull morphogenesis and the metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex .
HDAC8 has been implicated in several disease states, particularly in cancer. Overexpression and deregulation of HDAC8 are associated with cancer cell proliferation, metastasis, immune evasion, and drug resistance . Additionally, HDAC8 is linked to the pathogenesis of neuroblastoma, acute myeloid leukemia, and other cancers . Beyond cancer, HDAC8 is also involved in non-cancer diseases such as Cornelia de Lange Syndrome (CdLS), cardiovascular diseases, pulmonary diseases, and myopathy .
Given its significant role in various diseases, HDAC8 is considered an attractive therapeutic target. Researchers have developed several HDAC8 selective inhibitors (HDAC8is) that have shown promising anti-cancer effects . These inhibitors work by specifically targeting HDAC8, thereby reversing the pathological phenotypes associated with its overexpression and deregulation.