CASP1 is a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. CASP1 was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This protein has been shown to induce cell apoptosis and may function in various developmental stages.
Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
Target:
The synthetic peptide sequence used to generate the antibody AP6703c was selected from the Center region of human CASP1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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