Analytical Data
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Gene name
CAPN2
- Application
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Alternative Names
CANPL2; CANPml; mCANP; Calpain-2 Catalytic Subunit; Calcium-activated neutral proteinase 2; Calpain M-type; Calpain large polypeptide L2; Millimolar-calpain; Calpain 2, Large Subunit
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O08529
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Expression Region
Glu33~Thr344
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Molecular Weight
65kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
CAPN2, or calpain-2, is a cysteine protease that plays a crucial role in various cellular processes, including cell signaling, cytoskeletal remodeling, and apoptosis. As a member of the calpain family, CAPN2 is activated in response to calcium ion concentrations, and its dysregulation has been implicated in several pathological conditions, including neurodegenerative diseases, cancer, and cardiovascular disorders. The study of CAPN2 recombinant proteins offers valuable insights into its functional mechanisms and potential therapeutic targets. Researchers have focused on cloning and expressing CAPN2 in various systems to obtain sufficient quantities of the active enzyme for biochemical assays, structural studies, and the development of specific inhibitors. These efforts are essential for understanding the substrate specificity of CAPN2 and its role in mediating protein degradation and cellular responses to stress. Moreover, the production of CAPN2 recombinant protein can facilitate the development of diagnostic tools and novel drugs aimed at modulating calpain activity in disease contexts, making it a significant target in biomedical research.
