Caspase-9 (carboxy-terminal divergent) Polyclonal Antibody

Antigen: mixture of synthetic peptides corresponding to rat caspase-9 amino acids 345-359 and 366-383 . Host: rabbit . Cross Reactivity: (+) human, mouse, and rat caspase-9 . Application(s): WB . CTD is a novel isoform of rat caspase-9 in which the C-terminus of full-length caspase-9 is replaced with an alternative peptide sequence. It is found primarily in the cytoplasm and was not detected in the nucleus. CTD proenzyme is not processed in the cells and lacks apoptotic activity. The CTD-transfected cells are resistant to caspase induction by cytochrome c, suggesting the CTD acts as a dominant-negative variant.

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SPECIFICATIONS

Catalog Number

13915

Applications

WB

Hosts

Rabbit

Form

1 ea

P Type

Antibodies|Intracellular Signaling

Weight

0

Antigen

mixture of synthetic peptides corresponding to rat caspase-9 amino acids 345-359 and 366-383

Storage Temp

-20

Shipping Temp

-20

Additional Info

Caspase-9 and Apaf-1 bind to each other, which leads to caspase activation. Activated caspase-9 cleaves and activates caspase-3, one of the key proteases responsible for the proteolytic cleavage of many proteins in apoptosis. Caspase-9 plays a central role in cell death induced by a wide variety of apoptosis inducers including TNFa, TRAIL, anti-CD95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues. Recently, a novel isoform of rat caspase-9 has been identified in which the C-terminus of full-length caspase-9 is replaced with an alternative peptide sequence. This protein, called Caspase-9 (CTD) (where CTD is carboxyl-terminal divergent) is expressed in multiple tissues, with the relative highest levels observed in ovary and heart. The variant C-terminus of CTD in rat is derived from an alternative exon of the rat caspase-9 gene. CTD was found primarily in the cytoplasm and was not detected in the nucleus. CTD proenzyme is not processed in the cells and lacks apoptotic activity. The CTD-transfected cells are resistant to caspase induction by cytochrome c, suggesting the CTD acts as a dominant-negative variant.