Reactive species
Human;Rat;Mouse;
Antibody type
Polyclonal Antibody
Gene Name
CASP2 ICH1 NEDD2
Immunogen
Synthesized peptide derived from human Caspase 2 (p12, Cleaved-Ala348)
Specificity
This antibody detects endogenous levels of Human Caspase 2 (p12, Cleaved-Ala348, protein was cleaved amino acid sequence between 347-348)
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
WB 1:1000-2000 ELISA 1:5000-20000
Purification process
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
Other name
Caspase-2 (CASP-2;EC 3.4.22.55;Neural precursor cell expressed developmentally down-regulated protein 2;NEDD-2;Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
Background
alternative products:Isoforms differ in the N- and C-termini,catalytic activity:Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.,function:Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival.,PTM:The mature protease can process its own propeptide, but not that of other caspases.,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 p18 subunit and a p12 subunit. Interacts with LRDD.,tissue specificity:Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle.,
Function
proteolysis, apoptosis, anti-apoptosis, induction of apoptosis, cell death, induction of apoptosis by extracellular signals, regulation of cell death, positive regulation of cell death, programmed cell death, induction of programmed cell death, death, protein processing, regulation of apoptosis, positive regulation of apoptosis, negative regulation of apoptosis, regulation of programmed cell death, positive regulation of programmed cell death, negative regulation of programmed cell death, protein maturation, protein maturation by peptide bond cleavage, negative regulation of cell death,