| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | HSP70, Heat Shock Protein 70, DnaK, HSP70i |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Shipping | |
| Species | |
| Storage | |
| UniProt # |
Scientific Background
In cooperation with other chaperones, Hsp70 stabilizes preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.
Product Description
E. coli ExpressionRecombinant HSP70 Human protein is produced using a validated E. coli 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 | P08107 |
|---|---|
| Expression System | E. coli |
| Amino Acids / Region | 2-641 |
| Affinity Tag | C-terminal His-tag |
| Molecular Weight | 71 kDa |
| Formulation | 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 3 mM DTT, 20% glycerol, and 200… |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Safety & Handling
Avoid freeze/thaw cycles.
This protein was produced in E. coli. 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 2-641. 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.
- Lee K.J. et al., Exp. Mol. Med. 40 (6), 658-668 (2008).
- Birtas-Atesoglu E. et al., Clin. Exp. Rheumatol. 26, S96-S98 (2008).
