protein

CAPN1 Protein, Human (His)

HY-P72113

5 μg;10 μg;50 μg;100 μg

65;110;300;510 USD

CAPN1 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

65;110;300;510 USD

CAPN1 (Calpain-1) is a calcium-regulated non-lysosomal thiol protease that plays a critical role in the limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This protease catalyzes specific cleavage events, including CTBP1 cleavage at "Asn-375," "Gly-387," and "His-409," and activation of caspase-7 (CASP7). CAPN1 Protein, Human (His) is the recombinant human-derived CAPN1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of CAPN1 Protein, Human (His) is 714 a.a., with molecular weight of ~85.9 kDa.

Human

CAPN1, a calcium-regulated non-lysosomal thiol-protease, plays a crucial role in limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Operating in a calcium-dependent manner, CAPN1 catalyzes the targeted cleavage of various proteins, such as CTBP1 at specific sites, including 'Asn-375', 'Gly-387', and 'His-409'. Additionally, CAPN1 is involved in the activation of caspase-7 (CASP7) through proteolytic cleavage. These activities highlight its significance in regulating cellular processes associated with cytoskeletal dynamics and apoptosis, emphasizing its role as a calcium-dependent protease with implications for signal transduction pathways and cellular remodeling.

Ca2 activated neutral protease; Calcium activated neutral proteinase; CANP1; CANPL 1; CANPL1; CAPN 1; CAPN1; Cell proliferation inducing protein 30; Cell proliferation-inducing gene 30 protein; Micromolar Calpain; Micromolar-calpain; Mu Calpain; muCANP; muCL

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.