HDAC6 is a member of the class II mammalian histone deacetylases. Human HDAC6 is composed of 1215 amino acid residues. It possesses two separate putative catalytic domains. Both catalytic domains are fully functional HDACs and contribute independently to the overall activity of HDAC6 protein. A very potent NES is present at the amino-terminus of HDAC6, which was found to play an important role in regulating the shuttling of HDAC6 protein between cytoplasm and nucleus. The shuttling process may be a critical regulatory mechanism of HDAC6 function. The expression of HDAC6 is tightly linked to the state of cell differentiation. HDAC6 may participate in coordinating expression of a group of genes involved in the remodelling of chromatin during cell differentiation.
产品应用
应用
已检合格种属
预测种属
推荐稀释比例
WB
Human
1:500-2000
IHC-P
Human
1:100-500
IHC-F
Human
1:100-500
IF
Human
1:100-500
ICC/IF
Human
1:50-200
交叉反应
交叉反应: Human
相关产品
暂无相关产品
靶标
基因名
HDAC6
蛋白名
Histone deacetylase 6
亚基
Interacts with CBFA2T3, HDAC11 and SIRT2. Interacts with F-actin. Interacts with BBIP10. Under proteasome impairment conditions, interacts with UBD via its histone deacetylase 1 and UBP-type zinc-finger regions. Interacts with CYLD. Interacts with ZMYND15 (By similarity). Interacts with DDIT3/CHOP.
亚细胞定位
Nucleus. Cytoplasm. Note=It is mainly cytoplasmic, where it is associated with microtubules.
翻译后修饰
Phosphorylated by AURKA.
Ubiquitinated. Its polyubiquitination however does not lead to its degradation.
Sumoylated in vitro.
相似性
Belongs to the histone deacetylase family. HD type 2 subfamily. Contains 1 UBP-type zinc finger.
功能
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. Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin.
In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.