Analytical Data
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Gene name
CAPN1
- Application
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Alternative Names
Calcium-activated neutral proteinase 1 ;CANP 1;Calpain mu-type;Calpain-1 large subunit;Micromolar-calpain ;muCANP
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Species
Mouse
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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
O35350
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Expression Region
1-713aa
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Molecular Weight
86.1 kDa
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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
CAPN1, or calpain-1, is a calcium-dependent cysteine protease that plays a crucial role in various cellular processes, including cell signaling, apoptosis, and cytoskeletal remodeling. Dysregulation of CAPN1 has been implicated in several pathological conditions, including neurodegenerative diseases, cardiovascular disorders, and cancer. The study of CAPN1 and its functions has garnered increasing interest due to its potential as a therapeutic target. Recombinant CAPN1 protein production allows for detailed biochemical studies and structural analyses, facilitating the understanding of its enzymatic mechanisms and interactions with substrates. By utilizing techniques such as molecular cloning and expression systems, researchers can generate large quantities of this enzyme, enabling in vitro assays to explore its role in cellular pathways and disease mechanisms. Furthermore, recombinant CAPN1 can be employed in drug screening assays to identify small molecules that modulate its activity, thereby offering insights into novel treatment strategies for related diseases. Overall, the study of CAPN1 through recombinant protein techniques is pivotal, not only for elucidating its biological functions but also for advancing therapeutic interventions targeting calpain-related pathways.
