Analytical Data
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Gene name
CAPNS2
- Application
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Alternative Names
CAPNS2Calpain small subunit 2; CSS2; Calcium-dependent protease small subunit 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96L46
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Expression Region
1-248aa
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AA Sequence
MFLAKALLEGADRGLGEALGGLFGGGGQRREGGGRNIGGIVGGIVNFISEAAAAQYTPEPPPTQQHFTSVEASESEEVRRFRQQFTQLAGPDMEVGATDLMNILNKVLSKHKDLKTDGFSLDTCRSIVSVMDSDTTGKLGFEEFKYLWNNIKKWQCVYKQYDRDHSGSLGSSQLRGALQAAGFQLNEQLYQMIVRRYANEDGDMDFNNFISCLVRLDAMFRAFKSLDRDRDGLIQVSIKEWLQLTMYS
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Molecular Weight
53.02 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
CAPNS2 (Calpain 2, the large subunit of calpain) is a crucial protein involved in various cellular processes, including cytoskeletal remodeling, apoptosis, and cell signaling. As a member of the calpain family, CAPNS2 functions as a calcium-dependent cysteine protease that plays a pivotal role in cellular responses to stress and injury. Dysregulation of CAPNS2 has been linked to several pathological conditions, including neurodegenerative diseases, cardiac disorders, and cancer. Research has shown that CAPNS2 is essential for proper muscle development and function, as well as for the maintenance of neuronal integrity. Its activity is regulated by intracellular calcium levels, which makes it an intriguing target for therapeutic interventions aimed at modulating its function. Given its significant biological roles, there is a growing interest in the structural and functional characterization of CAPNS2, particularly through the production of recombinant proteins. The generation of CAPNS2 recombinant proteins allows for detailed studies of its enzymatic activity, interactions with substrates, and effects on cellular pathways. Understanding the mechanisms by which CAPNS2 exerts its effects can shed light on its potential as a drug target and contribute to the development of novel therapeutic strategies for diseases associated with calpain dysregulation. Thus, the study of CAPNS2 not only advances our knowledge of proteolytic regulation in cells but also opens new avenues for addressing major health challenges associated with its dysfunction.
