HDAC8 Protein, Mouse (sf9, His)

The HDAC8 protein is a histone deacetylase that removes acetyl groups from core histone lysine residues, contributing to epigenetic repression and affecting transcriptional regulation, cell cycle progression, and developmental events. It forms large multiprotein complexes and deacetylates SMC3, regulating the release of cohesin complexes. HDAC8 Protein, Mouse (sf9, His) is the recombinant mouse-derived HDAC8 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of HDAC8 Protein, Mouse (sf9, His) is 377 a.a., with molecular weight of ~46 kDa.

HDAC8 Protein is a histone deacetylase that facilitates the removal of acetyl groups from lysine residues on the N-terminal portion of core histones (H2A, H2B, H3, and H4). This deacetylation process contributes to epigenetic repression, thereby exerting significant influence on transcriptional regulation, cell cycle progression, and developmental events. The activity of HDAC8 is mediated through the formation of large multiprotein complexes. Furthermore, it participates in the deacetylation of cohesin complex protein SMC3, which regulates the release of cohesin complexes from chromatin. HDAC8 may also play a role in smooth muscle cell contractility. Additionally, apart from its deacetylase function, HDAC8 demonstrates protein-lysine deacylase activity by acting as a protein decrotonylase, catalyzing the removal of crotonyl groups ((2E)-butenoyl) from histones.

Mouse

Sf9 insect cells

C-His

Q8VH37 (M1-V377)

70315  [NCBI]

Approximately 46 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.