| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Human rhinovirus 3C protease, HRV3C |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Shipping | |
| Species | |
| Storage |
Scientific Background
Recombinant HRV 3C Protease (human rhinovirus 3C protease), encompassing amino acids 1538-1719 corresponding to the proteolytic domain. This construct contains an N-terminal His-Tag (6xHis) followed by a GST-Tag and a Factor Xa cleavage site. This protein recognizes the sequence Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro, cleaving between the Gln and Gly. This protein was affinity purified.
Product Description
E. coli ExpressionRecombinant HRV 3C Protease 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
| Expression System | E. coli |
|---|---|
| Amino Acids / Region | 1538-1719 |
| Affinity Tag | N-terminal His-GST-tags |
| Molecular Weight | 47 kDa |
| Formulation | 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM EDTA, 1 mM TCEP and 50% glycerol |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Specific Activity
1 Unit of HRV 3C Protease cleaves >95% of 100 µg of target protein at 4°C for 16 hours.
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 1538-1719. 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.
- Timmer JC, Salvesen GS. Methods Mol Biol. 2011;753:243-55.