Abcam, ab114576, Recombinant Human Calpain 3 protein

Size: 10µg
Recombinant Human Calpain 3 protein is a Human Full Length protein, in the 1 to 309 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:WB, SDS-PAGE, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:P20807,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.3% Glutathione

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Calpain 3 also known as p94 or CAPN3 is a calcium-dependent cysteine protease. Its molecular mass is approximately 94 kDa. Calpain 3 is expressed mainly in skeletal muscle tissue. It has a unique structure compared to other calpains possessing specific insertion sequences that are not present in other members of the calpain family. This protein is involved in muscle function through its proteolytic activity where it cleaves target proteins by recognizing specific amino acid sequences.
Biological function summary
Calpain 3 plays an active role in skeletal muscle remodeling and growth. It is a member of the calpain family and works independently not as part of a larger enzyme complex. The protein regulates cytoskeletal remodeling by targeting structural proteins influencing cell motility and muscle integrity. Modifications in Calpain 3 activity can affect muscle elasticity and repair mechanisms which are essential for normal muscle function.
Pathways
Calpain 3 significantly impacts muscle development and maintenance pathways. Its actions in these pathways allow for proper muscle adaptation to stress and changes in physical demands. The protease interacts with titin a large muscle protein and modulates its dynamics influencing how muscle contraction and relaxation occur. Alterations in the signaling pathways involving Calpain 3 and titin can directly affect muscle performance and structural integrity.
Calpain 3 has been directly linked to limb-girdle muscular dystrophy type 2A (LGMD2A). This disorder involves mutations in the CAPN3 gene leading to dysfunctional protein activity. The disease symptoms manifest as progressive weakening of the skeletal muscles. Research also highlights the interaction between Calpain 3 and titin as disruptions to their interaction contribute to the degenerative muscle changes observed in LGMD2A. Scientists continue examining these molecular connections to develop new therapeutic strategies for managing and treating muscle-related disorders.