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Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. Additionally we are shipping Calpain 7 Antibodies (19) and many more products for this protein.
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The proteolytic activity of CAPN7 is important for the acceleration of EGFR (show EGFR Proteins) degradation via the endosomal sorting pathway.
Data indicate that CAPN 7 promotes endometrial stromal cell (hESC) migration and invasion by increasing the activity of MMP-2 (show MMP2 Proteins) via an increased ratio of MMP-2 (show MMP2 Proteins) to TIMP-2 (show TIMP2 Proteins).
Mutational analysis of calpain-7 reveals the importance of not only the N-terminal microtubule-interacting and trafficking domains but also the C-terminal C2 domain-like domains for proteolytic activity.
The detected enhancement of autolysis of mGFP-fused calpain-7 by coexpression with CHMP1B and observed further activation by additional coexpression of IST1 (show IST1 Proteins) in HEK293T cells.
Results demonstrate that human calpain 7 is proteolytically active, and imply that calpain 7 is activated by ESCRT-III-related protein IST1 (show IST1 Proteins).
calpain-derived Htt (show HTT Proteins) fragmentation has a role in Huntington's disease and aberrant activation of calpains may play a role in HD pathogenesis
Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit possesses a cysteine protease domain, and both subunits possess calcium-binding domains. Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. The function of the protein encoded by this gene is not known. An orthologue has been found in mouse but it seems to diverge from other family members. The mouse orthologue is thought to be calcium independent with protease activity.
, calpain like protease
, homolog of Aspergillus Nidulans PALB
, palB homolog