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Rabbit Anti-caspase-9 p10/FITC Conjugated antibody
background:
A unique family of cysteine proteases has been described that differs in sequence, structure and substrate specificity from any previously described protease family. This family, Ced-3/caspase-1, is comprised of caspase-1, caspase-2, caspase-3, caspase-4, caspase-6, caspase-7 (also designated Mch3, ICE-LAP3 or CMH-1), caspase-9 and caspase-10. Ced-3/caspase-1 family members function as key components of the apoptotic machinery and act to destroy specific target proteins which are critical to cellular longevity. Poly(ADP-ribose) polymerase plays an integral role in surveying for DNA mutations and double strand breaks. Caspase-3, caspase-7 and caspase-9, but not caspase-1, have been shown to cleave the nuclear protein PARP into an apoptotic fragment. Caspase-6, but not caspase-3, has been shown to cleave the nuclear lamins which are critical to maintaining the integrity of the nuclear envelope and cellular morphology. Caspase-10 has been shown to activate caspase-3 and caspase-7 in response to apoptotic stimuli.
Function:
Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).
Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.
Subunit:
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts (inactive form) with EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1, XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin.
Tissue Specificity:
Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues. Within the heart, specifically expressed in myocytes.
Post-translational modifications:
Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events.
Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation.
Similarity:
Belongs to the peptidase C14A family.
Contains 1 CARD domain.
Database links:
Entrez Gene: 842 Human
Entrez Gene: 12371 Mouse
Entrez Gene: 58918 Rat
Omim: 602234 Human
SwissProt: P55211 Human
SwissProt: Q4FJK5 Mouse
SwissProt: Q920G4 Rat
Unigene: 329502 Human
Unigene: 88829 Mouse
Unigene: 32199 Rat
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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