Caspase-9 Mouse anti-Human, Unlabeled, Clone: 2-22, BD

Description

• The caspase family of cysteine proteases plays a key role in apoptosis and inflammation
• Caspases are synthesized as inactive proenzymes containing three domains, that are processed into large and small subunits that associate to form the active enzyme
• Processing can occur in apoptotic cells by either transactivation, self-proteolysis or cleavage by another protease
• While caspases share a common structure, there are some differences, such as the preferred substrate specificity
• These sequence differences in specificity, as well as the size of the NH2 -terminal prodomain, can be used to catagorize the caspases into functional groups including apoptotic initiators (long prodomains), apoptotic executioners (short prodomains), and cytokine processors
• Caspase-9 is a member of the apoptotic initiator group of caspases which include caspases-2, -8, and -10
• Activation of caspase-9 occurs in the presence of cytochrome c, following an interaction between caspase-9 and APAF-1
• Activation may also be triggered directly by the cytotoxic T-cell protease, granzyme B
• Active caspase-9 cleaves and thus activates caspase-3, and is also a relevant target of active caspase-3
• Caspase-9 can also cleave the nuclear protein PARP
• Northern blot analysis suggests that high expression of caspase-9 is found in the heart, testis, and ovary
• The antibody recognizes the 47kDa proform and 37kDa cleaved form of human caspase-9
• The N-terminal fragment (amino acids 1-134) of human caspase-9 was used as an immunogen
• Host Species: Mouse Clone: 2-22 Isotype: IgG1 κ Species Reactivity: Human Immunogen: Human caspase-9 N-terminal fragment aa 1-134 Western Blotting