| Field | Specification |
|---|---|
| Activity | |
| Alternative Names | Calcium-activated neutral proteinase 2 ;CANP 2;Calpain M-type;Calpain-2 large subunit;Millimolar-calpain ;M-calpain |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Function | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Species | |
| Storage | |
| UniProt # |
Scientific Background
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal rodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' .
Product Description
E. coli ExpressionRecombinant Pig Calpain-2 catalytic subunit (CAPN2) is a recombinant protein expressed in E. coli and purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. Supplied as Liquid or Lyophilized powder, n-terminal 6xhis-sumo-tagged. For research use only.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Specifications
| Molecular Weight | 53.8 kDa |
|---|---|
| Expression Region | 1-324aa |
| Expression System | E. coli |
| Tag | N-terminal 6xHis-SUMO-tagged |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Form | Liquid or Lyophilized powder |
| Storage Buffer | If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Endotoxin Level | Not test |
| UniProt Accession | P43367 |
| Storage | The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃. |
Safety & Handling
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This recombinant protein is expressed in E. coli, a widely used system for producing soluble, biologically active proteins at scale. The E. coli expression platform enables efficient folding and high yields, suitable for functional and binding assays.
This protein is supplied as N-terminal 6xHis-SUMO-tagged and has been purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. High purity minimizes interference in downstream assays, particularly in cell-based bioactivity studies and ELISA development.
Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1–1.0 mg/mL. For long-term storage, add 5–50% glycerol and store in aliquots at -20°C or -80°C to avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
Biological activity data are available in the product datasheet. Please contact our support team for activity specifications relevant to your specific application.
This recombinant protein is suitable for a range of in vitro research applications including binding assays, protein–protein interaction studies, cell proliferation/bioactivity assays, ELISA standard curve calibration, and assay development. Confirm suitability for your specific assay conditions with the product datasheet.
We offer flexible ordering options including bulk quantities, custom formulations, and endotoxin removal services for many of our recombinant proteins. Lead times and minimum order quantities vary by product. For custom conjugation, specialized buffer formulations, or volume pricing, please contact our support team. All customization requests are handled in partnership with our manufacturing suppliers and are subject to feasibility review.
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