Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. Additionally we are shipping Calpain 6 Antibodies (52) and Calpain 6 Proteins (5) and many more products for this protein.
Showing 4 out of 16 products:
High CAPN6 expression is associated with liver cancer.
CAPN6 promotes atherogenicity in inflamed macrophages by disturbing CWC22 (show CWC22 ELISA Kits)/EJC systems.
syndecan-2 (show SDC2 ELISA Kits) exerts its pro-apoptotic function through modulation of the endothelin-1 (show EDN1 ELISA Kits)/NFkappaB (show NFKB1 ELISA Kits) signaling and through downregulation of calpain-6.
results indicated that calpain 6 supported tumorigenesis by inhibiting apoptosis and facilitating angiogenesis. To our knowledge, this result is the first evidence implicating calpain 6 in tumorigenesis
These results collectively showed that a loss of CAPN6 promotes skeletal muscle differentiation during both development and regeneration, suggesting a novel physiological function of CAPN6 as a suppressor of skeletal muscle differentiation.
CAPN6 acts as a regulator of Rac1 and cell motility through interaction with GEF-H1 (show ARHGEF2 ELISA Kits).
Capn6 promotes cytoskeletal organization and microtubule stability in osteoclasts.
Capn6 is a microtubule-stabilizing protein expressed in embryonic tissues that may be involved in the regulation of microtubule dynamics and cytoskeletal organization.
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 protein encoded by this gene is highly expressed in the placenta. Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains. The protein lacks critical active site residues and thus is suggested to be proteolytically inactive. The protein may play a role in tumor formation by inhibiting apoptosis and promoting angiogenesis.
, calpain-like protease X-linked