|Other Names||Inactive caspase-12, CASP-12, CASP12|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Has no protease activity. May reduce cytokine release in response to bacterial lipopolysaccharide during infections. Reduces activation of NF-kappa-B in response to TNF.|
|Tissue Location||Detected in heart, kidney, liver, lung, pancreas, small intestine, spleen, stomach, thymus and testis|
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Caspases are cysteine proteases that cleave C-terminalaspartic acid residues on their substrate molecules. This gene ismost highly related to members of the ICE subfamily of caspasesthat process inflammatory cytokines. In rodents, the homolog ofthis gene mediates apoptosis in response to endoplasmic reticulumstress. However, in humans this gene contains a polymorphism forthe presence or absence of a premature stop codon. The majority ofhuman individuals have the premature stop codon and produce atruncated non-functional protein. The read-through codon occursprimarily in individuals of African descent and carriers haveendotoxin hypo-responsiveness and an increased susceptibility tosevere sepsis. Several alternatively spliced transcript variantshave been noted for this gene.
Lee, H.J., et al. Arch. Biochem. Biophys. 502(1):68-73(2010)Plantinga, T.S., et al. J. Acquir. Immune Defic. Syndr. 55(1):87-94(2010)McCall, M.B., et al. Eur. Cytokine Netw. 21(2):77-83(2010)Kachapati, K., et al. Hum. Mutat. 27 (9), 975 (2006) :Xue, Y., et al. Am. J. Hum. Genet. 78(4):659-670(2006)
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