| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | histone deacetylase 6, HDAC-6 |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Shipping | |
| Species | |
| Storage | |
| UniProt # |
Scientific Background
Human HDAC6, GenBank Accession No. BC069243, full length with N-terminal GST-tag, MW= 159 kDa, expressed in baculovirus expression system.
Product Description
Insect Cells (Sf9) ExpressionRecombinant HDAC6 Human protein is produced using a validated Insect Cells (Sf9) expression system and supplied in aqueous buffer solution. Suitable for enzyme kinetics, inhibitor screening, binding assays, structural studies, and related biochemical research applications.
Protein Specifications
| UniProt ID | Q9UBN7 |
|---|---|
| Expression System | Insect Cells (Sf9) |
| Amino Acids / Region | full length |
| Affinity Tag | N-terminal GST-tag |
| Molecular Weight | 159 kDa |
| Formulation | 50 mM Tris-HCl, pH 7.5, 500 mM NaCl, 50 mM KCl, 2 mM EDTA, 10% glycerol, and 2 m… |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Specific Activity
≥450 pmol/min/µg.
Safety & Handling
Avoid freeze/thaw cycles.
This protein was produced in Insect Cells (Sf9). Expression system selection determines post-translational processing, disulfide bond formation, and co-factor incorporation — all of which affect enzymatic activity. Insect cell (Sf9) systems are preferred for kinases and multi-subunit enzymes that require phosphorylation or chaperone assistance; E. coli is used for structurally simpler proteins.
This protein spans amino acids full length. Confirm the region includes your domain of interest — the active site, binding pocket, or substrate recognition sequence — before placing your order. Refer to the UniProt database for domain annotation.
Purity is assessed by SDS-PAGE; see the Certificate of Analysis. A gel image is provided with each lot. BPS Bioscience performs rigorous QC on each lot, including purity assessment and functional activity testing where applicable. Contact technical support if purity ≥99% is required for biophysical measurements.
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Refer to the product datasheet for validated protocols and recommended assay conditions. Contact BioHippo technical support for application-specific guidance.
At least 6 months at -80°C. Avoid repeated freeze-thaw cycles — prepare single-use working aliquots. Add BSA or glycerol to aliquots if storing diluted enzyme is necessary. Typical stability is at least 6 months at −80°C.
BioHippo offers flexible sourcing for qualified research institutions and partners.
- Bulk quantities: Large-scale orders for HTS campaigns or structural studies.
- Custom constructs: Alternative tag positions, truncation variants, or point mutants may be available upon request.
- Biotinylated variants: Avi-Tag site-specific biotinylation is available for SPR/BLI surface capture applications.
- Extended QC data: Activity assay data, SEC-HPLC profiles, or additional purity methods available on request.
Contact BioHippo customer support for custom requirements.
- Li S. et al., Neurology. 41(2), 112-6 (2010).
- Strausberg, R.L. et al., Proc. Natl. Acad. Sci. U.S.A. 99 (26), 16899-16903 (2002). Application References:
- Jang, S., et al. Cancer Gene Ther. 2015 Aug;22(8):410-6. doi: 10.1038/cgt.2015.37. Novel analogs targeting histone deacetylase suppress aggressive thyroid cancer cell growth and induce re-differentiation (2015)
- Design, synthesis, 3D pharmacophore, QSAR, and docking studies of carboxylic acid derivatives as Histone Deacetylase inhibitors and cytotoxic agents (2014)
- Wang, C., et al. J Med Chem. 2014 Oct 9;57(19):7999-8009. doi: 10.1021/jm500872p. In Vivo Imaging of Histone Deacetylases (HDACs) in the Central Nervous System and Major Peripheral Organs (2014)
- 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)
- Meyners, C., et al. Mol Recognit. 2014 Mar;27(3):160-72. Thermodynamics of ligand binding to histone deacetylase like amidohydrolase from Bordetella/Alcaligenes (2014)
- A selective HDAC 1/2 inhibitor modulates chromatin and gene expression in brain and alters mouse behavior in two mood-related tests (2013)
- Fass, D.M., et al. Neuropharmacology. 2013 Jan; 64: 81–96. Crebinostat: a novel cognitive enhancer that inhibits histone deacetylase activity and modulates chromatin-mediated neuroplasticity (2013)
- Baud, MGJ, et al. ChemMedChem. 2013 Jan;8(1):149-56. doi: 10.1002/cmdc.201200450. Highly ligand efficient and selective N-2-(Thioethyl)picolinamide histone deacetylase inhibitors inspired by the natural product psammaplin A (2013)
- 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)
- 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)
