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Key Documents

SRP0311

Sigma-Aldrich

HDAC6 H611A human

recombinant, expressed in baculovirus infected Sf9 cells, ≥79% (SDS-PAGE)

Synonyme(s) :

HD6, JM21, histone deacetylase 6

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About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in baculovirus infected Sf9 cells

Pureté

≥79% (SDS-PAGE)

Forme

aqueous solution

Poids mol.

161 kDa

Conditionnement

pkg of 50 μg

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... HDAC6(10013)

Description générale

HDAC6 (histone deacetylase 6) belongs to the HDAC family of proteins. HDACs are responsible for deacetylation of nuclear histone and nonhistone proteins, including transcription factors. The mutation H611A results in catalytically inactive HDAC6.
Human HDAC6 with H611A mutation (GenBank Accession No. NM_006044), full length with N-terminal GST tag, MW= 161kDa, expressed in a Baculovirus expression system.

Actions biochimiques/physiologiques

HDAC6 (histone deacetylase 6) is involved in the control of microtubules, growth factor-mediated chemotaxis, stress response in presence of misfolded protein and tumor invasion. It also participates in EGF (epidermal growth factor)-mediated β-catenin nuclear presence and activation of c-myc. In mouse model, HDAC6 is implicated in oncogene-induced tumorigenesis. HDAC6 is the main deacetylase for α-tubulin and thus, is involved in cell motility. It is also involved in the formation of SGs (stress granules) and SG proteins. Mutations in the 3′-UTR of the HDAC6 gene suppresses hsa-miR-433-mediated post-transcriptional regulation. This results in overexpression of HDAC6, thereby causing X-linked chondrodysplasia.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes.
Hook SS, et al.
Proceedings of the National Academy of Sciences of the USA, 99, 13425-13425 (2002)
Loss of a-Tubulin Acetylation Is Associated with TGF-?-induced Epithelial-Mesenchymal Transition.
Gu S, et al.
The Journal of Biological Chemistry, 291, 5396-5396 (2016)
Li S. et al.
Neurology, 41, 112-116 (2010)
Jiaqi Liu et al.
Journal of translational medicine, 14, 7-7 (2016-01-10)
Histone deacetylase (HDAC) inhibitors are widely used in clinical investigation as novel drug targets. For example, panobinostat and vorinostat have been used to treat patients with melanoma. However, HDAC inhibitors are small-molecule compounds without a specific target, and their mechanism
Qun Wang et al.
Oncotarget, 7(9), 10064-10072 (2016-02-06)
Histone deacetylase inhibitors (HDIs) represent a new class of anticancer drugs. Suberoylanilide hydroxamic acid (SAHA), the first HDI approved for the treatment of cutaneous T cell lymphoma (CTCL), is currently being tested in clinical trials for other cancers. However, SAHA

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