Anti-Calpain 2 Antibody [JA43-41]

HUABIO

Anti-Calpain 2 Antibody [JA43-41]

7

Flow Cytometry, ImmunoFluorescence, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin

WB,IF-Cell,IHC-P,FC

Research Use Only

Monoclonal

JA43-41

1 mg/ml

Unconjugated

CAPN2

calpain 2

CANP2, CANPL2, CANPml, mCANP, calpain-2 catalytic subunit, CANP 2, M-calpain, calcium-activated neutral proteinase 2, calpain 2, (m/II) large subunit, calpain 2, large [catalytic] subunit, calpain 2, large subunit, calpain M-type, calpain, large polypeptide L2, millimolar-calpain

Rabbit

IgG

Calpain-2 catalytic subunit

Calpain-2 is a heterodimer of a catalytic subunit encoded by CAPN2 gene and a regulatory subunit CAPNS1. The catalytic subunit consists of four domains: protease core 1 domain (PC1), protease core 2 domain (PC2), calpain-type beta-sandwich-like domain (CBSW), and penta EF-hand domain (PEF(L)). The catalytic cleft is formed by PC1 and PC2 upon calcium binding. The catalytic triad consists of residues C105, H262, and N286. Noteworthy, CAPN2 also contains an N-terminal anchor helix, which however is cleaved off upon protease activation. There is no known consensus sequence for calpain-2 proteolysis, but there is evidence for over 130 potential substrates. Proteolytic cleavage by calpain-2 is regulated by presence of Ca2+ ions. It requires supraphysiological (low millimolar) concentration of Ca2+ for activation. Intracellular concentration of Ca2+ (approx. 100 nM) is insufficient for activating calpain-2, so activation occurs upon influx of ions from extracellular space or from endoplasmic reticulum.

Human, Rat

Human,Rat

Mouse

-20°C,2°C to 8°C

41116161