Recombinant Proteins

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CAPNS1 Human

Calpain, Small Subunit 1 Human Recombinant

CAPNS1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (84-268) and having a molecular mass of 23.8 kDa.
CAPNS1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3167
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

Calpain is a family of calcium-dependent, non-lysosomal cysteine proteases that are ubiquitously expressed in mammals and many other organisms . These proteolytic enzymes belong to the C2 family of protease clan CA in the MEROPS database . The calpain system includes the calpain proteases, the small regulatory subunit CAPNS1 (also known as CAPN4), and the endogenous calpain-specific inhibitor, calpastatin . The two main isoforms, μ-calpain and m-calpain, differ primarily in their calcium requirements for activation .

Biological Properties

Calpains are intracellular proteases that require calcium ions for activation . They are expressed ubiquitously across various tissues, including the brain, lens of the eye, and skeletal muscle . The expression patterns and tissue distribution of calpains are diverse, reflecting their involvement in numerous cellular processes . Calpains are typically present as inactive enzyme precursors and are activated through autolysis when intracellular calcium levels exceed a certain threshold .

Biological Functions

Calpains play essential roles in various biological processes, including signal transduction, cell proliferation, cell cycle progression, differentiation, apoptosis, membrane fusion, and platelet activation . They are involved in immune responses and pathogen recognition by modulating the structure and function of their substrates through limited proteolytic activity . Calpains have also been implicated in apoptotic cell death and are essential components of necrosis .

Modes of Action

Calpains act by proteolytic processing, recognizing bonds between domains rather than specific amino acid residues or sequences . This limited proteolysis results in large fragments retaining intact domains . Calpains interact with various molecules and cells, including integrins, cytoskeletal proteins, and signaling molecules . They are involved in downstream signaling cascades that regulate cell migration, cytoskeletal remodeling, cell differentiation, and apoptosis .

Regulatory Mechanisms

The activity of calpains is tightly regulated by several mechanisms, including calcium and phospholipid binding, phosphorylation, autolysis, and subcellular localization . Calpains are also regulated by the specific endogenous inhibitor calpastatin . Transcriptional regulation and post-translational modifications further control the expression and activity of calpains . Abnormal activation of calpains due to elevated calcium levels can lead to various pathological conditions .

Applications

Calpains have significant applications in biomedical research, diagnostic tools, and therapeutic strategies . They are involved in the pathogenesis of cardiometabolic disorders, and calpain inhibitors are being explored as potential therapeutic agents . Calpains also play a role in autophagic flux and are being studied for their potential in treating neurodegenerative diseases .

Role in the Life Cycle

Calpains are active participants throughout the life cycle, from development to aging and disease . They are involved in processes such as cell mobility, cell cycle progression, long-term potentiation in neurons, and cell fusion in myoblasts . Calpains play essential roles in development and participate in various signal transduction pathways that regulate important cellular processes of life and death .

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