The antiserum was produced against synthesized peptide derived from human Caspase 9 around the phosphorylation site of Thr125. AA range:91-140

Phospho-Caspase-9 (T125) Polyclonal Antibody detects endogenous levels of Caspase-9 protein only when phosphorylated at T125.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):PEtPR

CASP9

Caspase9

CASP9 ;
MCH6 ;
Caspase-9 ;
CASP-9 ;
Apoptotic protease Mch-6 ;
Apoptotic protease-activating factor 3 ;
APAF-3 ;
ICE-like apoptotic protease 6 ;
ICE-LAP6 ;
[Cleaved into: Caspase-9 subunit p35 ;
Caspase-9 subunit p10]

CASP9 encodes 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 two subunits, large and small, that dimerize to form the active enzyme. Caspase 9 can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. Caspase 9 is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants.

Catalytic activity:Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.,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).,Function:Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.,online information:Caspase-9 entry,PTM: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.,similarity:Belongs to the peptidase C14A family.,similarity:Contains 1 CARD domain.,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 with the inhibitors BIRC2, BIRC4, BIRC5 and BIRC7.,tissue specificity:Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues.,

nucleus,mitochondrion,cytosol,apoptosome,

>>Platinum drug resistance ;
>>p53 signaling pathway ;
>>PI3K-Akt signaling pathway ;
>>Apoptosis ;
>>Apoptosis - multiple species ;
>>VEGF signaling pathway ;
>>Thyroid hormone signaling pathway ;
>>Alzheimer disease ;
>>Parkinson disease ;
>>Amyotrophic lateral sclerosis ;
>>Huntington disease ;
>>Prion disease ;
>>Pathways of neurodegeneration - multiple diseases ;
>>Pathogenic Escherichia coli infection ;
>>Legionellosis ;
>>Toxoplasmosis ;
>>Tuberculosis ;
>>Hepatitis C ;
>>Hepatitis B ;
>>Measles ;
>>Human cytomegalovirus infection ;
>>Influenza A ;
>>Kaposi sarcoma-associated herpesvirus infection ;
>>Herpes simplex virus 1 infection ;
>>Epstein-Barr virus infection ;
>>Human immunodeficiency virus 1 infection ;
>>Pathways in cancer ;
>>Colorectal cancer ;
>>Pancreatic cancer ;
>>Endometrial cancer ;
>>Prostate cancer ;
>>Small cell lung cancer ;
>>Non-small cell lung cancer ;
>>Viral myocarditis ;
>>Lipid and atherosclerosis