|Application ||WB, IHC-P, E|
|Other Accession||O88501, O35646, NP_055104.2|
|Calculated MW||74576 Da|
|Antigen Region||390-419 aa|
|Other Names||Calpain-6, Calpain-like protease X-linked, Calpamodulin, CalpM, CAPN6, CALPM, CANPX|
|Target/Specificity||This CAPN6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 390-419 amino acids from the Central region of human CAPN6.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CAPN6 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues (By similarity).|
|Cellular Location||Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle. Note=During mitose associated with the mitotic spindle. At telophase colocalized to the midbody spindle|
|Tissue Location||Expressed only in placenta.|
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Provided below are standard protocols that you may find useful for product applications.
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.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Secolin, R., et al. Psychiatr. Genet. 20(3):126-129(2010)
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
Rho, S.B., et al. Cancer Lett. 271(2):306-313(2008)
Rojas, F.J., et al. Mol. Hum. Reprod. 5(6):520-526(1999)
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