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Scientific Background
RIPK2 (receptor-interacting protein kinase 2) is a serine-threonine kinase that has been shown to mediate the activation of pro-inflammatory signals by NODs (Nucleotide-binding oligomerization domain-containing proteins), suggesting RIPK2 may be a promising therapeutic target in autoimmune and inflammatory diseases. This protein is expressed in several tissues, such as the spleen, placenta, testis and heart. It can interact with TNFR (tumor necrosis factor receptor) and thus participate in NOD and TLR (Toll-like receptor) pathways. Inhibition of RIPK2 may result in therapeutic benefits, and most of the inhibitors developed so far involve binding to the ATP site.
Product Description
Insect Cells (Sf9) ExpressionRecombinant RIPK2 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 | O43353 |
|---|---|
| Expression System | Insect Cells (Sf9) |
| Amino Acids / Region | 1-299 |
| Molecular Weight | 61 kDa |
| Purity | ≥90% |
| Formulation | 45 mM Tris-HCl, pH 8.0, 500 mM NaCl, 2.5 mM KCl, 0.02% Tween-20, 3 mM DTT and 10… |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Specific Activity
≥15 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 1-299. 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.
≥90% as determined by SDS-PAGE. 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.
- Inohara, N. et al: RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis. J. Biol. Chem. 273: 12296-12300, 1998. Note: Erratum: J. Biol. Chem 273: 18675 only, 1998.
- Thome, M. et al: Identification of CARDIAK, a RIP-like kinase that associates with caspase-1. Curr. Biol. 8: 885-888, 1998.