Analytical Data
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Gene name
CAPN3
- Application
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Alternative Names
CANPL3; p94; LGMD2; LGMD2A; nCL1; Calcium-activated neutral proteinase 3; Muscle-specific calcium-activated neutral protease 3; New calpain 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P20807
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Expression Region
Ile602~Ala821
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Molecular Weight
32kDa
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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
CAPN3, or calpain-3, is a member of the calpain family of calcium-dependent cysteine proteases and plays a crucial role in muscle development and function. Mutations in the CAPN3 gene are linked to limb-girdle muscular dystrophy type 2A (LGMD2A), a genetic disorder characterized by progressive muscle weakness and atrophy. Research into recombinant CAPN3 is pivotal for understanding its biological functions, elucidating the pathogenesis of LGMD2A, and exploring potential therapeutic strategies. The study of CAPN3 includes the recombinant expression of its protein, which allows for detailed investigations into its enzymatic activity, substrate specificity, and involvement in muscle regeneration. Additionally, the recombinant protein can serve as a valuable tool for developing gene therapies, enabling the possibility of correcting the underlying defect in patients with CAPN3-related disorders. Investigating the structural and functional characteristics of CAPN3 through recombinant techniques not only enhances our understanding of the molecular mechanisms underlying muscle diseases but also opens avenues for innovative treatments aimed at restoring muscle function and improving the quality of life for affected individuals. Thus, the research on CAPN3 recombinant protein represents a significant step forward in the field of muscle biology and gene therapy.
