protein

CAPN2 Protein, Human (His)

HY-P72115

5 μg;10 μg;50 μg

120;200;560 USD

CAPN2 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg

120;200;560 USD

CAPN2 (Calpain-2) is a calcium-regulated, non-lysosomal thiol protease known for catalyzing the limited proteolysis of substrates critical for cytoskeletal remodeling and signaling. Notably, CAPN2 proteolytically cleaves MYOC at “Arg-226,” suggesting its involvement in regulating the function of this protein. CAPN2 Protein, Human (His) is the recombinant human-derived CAPN2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of CAPN2 Protein, Human (His) is 681 a.a., with molecular weight of ~82.1 kDa.

Human

CAPN2, a calcium-regulated non-lysosomal thiol-protease, serves as a pivotal enzyme in the limited proteolysis of substrates implicated in cytoskeletal remodeling and signal transduction. Operating in a calcium-dependent manner, CAPN2 catalyzes targeted proteolysis, as evidenced by its cleavage of MYOC at the specific site 'Arg-226.' Furthermore, CAPN2 is involved in the regulation of neuronal stimulation-induced proteolytic cleavage of CPEB3, leading to the abolishment of CPEB3's translational repressor activity. This event subsequently facilitates the translation of CPEB3 target mRNAs, highlighting the multifaceted role of CAPN2 in orchestrating cellular processes associated with cytoskeletal dynamics, signal transduction, and neuronal function.

Calcium-activated neutral proteinase 2; Calpain M-type; Millimolar-calpain; CAPN2; CANPL2

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.