| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | histone deacetylase 1, HDAC-1 |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Shipping | |
| Species | |
| Storage | |
| UniProt # |
Scientific Background
Human HDAC1, GenBank Accession No. NM_004964, full length with C-terminal FLAG and C-terminal His-tag, MW= 56 kDa, expressed in baculovirus expression system.
Product Description
Insect Cells (Sf9) ExpressionRecombinant HDAC1 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 | Q13547 |
|---|---|
| Expression System | Insect Cells (Sf9) |
| Amino Acids / Region | full length |
| Affinity Tag | C-terminal FLAG-tag, C-terminal His-tag |
| Molecular Weight | 56 kDa |
| Formulation | 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 80 ng/µl FLAG peptide, and 20% … |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Specific Activity
≥460 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.
- Rikimaru,T. et al., Oncology 72 (1-2), 69-74 (2007).
- Ishihama, K. et al., J Clin Pathol 60(11), 1205-10 (2007). Application References:
- Identification of histone deacetylase inhibitors with benzoylhydrazide scaffold that selectively inhibit class I histone deacetylases (2015)
- A chimeric SERM-histone deacetylase inhibitor approach to breast cancer therapy (2014)
- CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis (2014)
- Design, synthesis and evaluation of novel HDAC inhibitors as potential antitumor agents (2014)
- Design, synthesis, 3D pharmacophore, QSAR, and docking studies of carboxylic acid derivatives as Histone Deacetylase inhibitors and cytotoxic agents (2014)
- Discovery of a small molecule agonist of phosphatidylinositol 3-kinase p110α that reactivates latent HIV-1 (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)
- Selective HDAC Inhibition for the Disruption of Latent HIV-1 Infection (2014)
- The effect of various zinc binding groups on inhibition of histone deacetylases 1-11 (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)
- Class I HDAC imaging using [ (3)H]CI-994 autoradiography (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)
- FDG-PET imaging reveals local brain glucose utilization is altered by class I histone deacetylase inhibitors (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)
- Imaging epigenetic regulation by histone deacetylases in the brain using PET/MRI with ¹¸F-FAHA (2013)
- Marek, M., et al. PLoS Pathog. 2013;9(9):e1003645. doi: 10.1371/journal.ppat.1003645. Structural basis for the inhibition of histone deacetylase 8 (HDAC8), a key epigenetic player in the blood fluke Schistosoma mansoni (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)
