Human HDAC6 with H216A mutation (GenBank Accession No. NM_006044), full length with N-terminal GST-tag, MW= 161 kDa, expressed in a baculovirus expression system.
Host cell line: Sf9 cells
Specific activity: >=380 pmol/min/ug
Immunogen Region
full length
Tag
N-terminal GST-tag
Formulation
50 mM Tris-HCl, pH 7.5, 500 mM NaCl, 50 mM KCl, 2 mM EDTA, 10% glycerol, and 2 mM DTT
Mutation
H216A
Species
Human
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling
Purification
Protein was purified by affinity chromatography and gel filtration.
Notes
25 mM Tris/HCl, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2, and 0.1 mg/ml BSA, 20 uM BPS HDAC substrate 3 (Catalog #50037), and HDAC6 H216A (1.6 - 100 ng). Incubation condition: 30 min at 37°C followed byHDAC developer (Catalog #50030) for 15 min at room temperature. Fluorescence intensity is measured at ex360/em460.
Avoid freeze/thaw cycles.
GenBank
NM_006044
Mw(kda)
161 kDa
Synonyms
histone deacetylase 6, HDAC6
Uniprot
Q9UBN7
Shipping Temperature
-80°C (dry ice)
Format
Aqueous buffer solution
Storage
At least 6 months at -80°C.
Reference
1. Li S. et al., Neurology. 41(2), 112-6 (2010). 2. Strausberg, R.L. et al., Proc. Natl. Acad. Sci. U.S.A. 99 (26), 16899-16903 (2002).Application References: 1. Meyners, C., et al. Anal Biochem. 2014 Sep 1;460:39-46. doi: 10.1016/j.ab.2014.05.014. Kinetic method for the large-scale analysis of the binding mechanism of histone deacetylase inhibitors (2014) 2. Blackburn, C., et al. J Med Chem. 2013 Sep 26;56(18):7201-11. doi: 10.1021/jm400385r. Potent histone deacetylase inhibitors derived from 4-(aminomethyl)-N-hydroxybenzamide with high selectivity for the HDAC6 isoform (2013) Pavlik, C.M., et al. J Nat Prod. 2013 Nov 22;76(11):2026-33. doi: 10.1021/np400198r. Santacruzamate A, a potent and selective histone deacetylase inhibitor from the Panamanian marine cyanobacterium cf. Symploca sp (2013) 4. Baud, MGJ, et al. Beilstein J Org Chem. 2013;9:81-8. doi: 10.3762/bjoc.9.11. Thioester derivatives of the natural product psammaplin A as potent histone deacetylase inhibitors (2013)