anti-Caspase-2, mAb (10C6)

AdipoGen Life Sciences

anti-Caspase-2, mAb (10C6)

10

Recognizes an epitope in the p19 subunit of human, mouse, rat, monkey and dog caspase-2.

Flow Cytometry, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry

Research Use Only

Monoclonal

10C6

1 mg/ml

>95%

CASP2

caspase 2

CASP-2; caspase 2 apoptosis-related cysteine peptidase; caspase-2; ICH1; NEDD2; NEDD-2; neural precursor cell expressed developmentally down-regulated protein 2; PPP1R57; protease ICH-1; protein phosphatase 1, regulatory subunit 57

Rat

IgG2a

Caspase-2 is a Class I caspase with a long prodomain necessary for nuclear localization. Upon activation of the apoptotic pathway, the procaspase is cleaved into smaller fragments. Caspase-2 is the nuclear apoptotic respondent to cellular genotoxic stress or mitotic catastrophe and is involved in the activation cascade of caspases responsible for apoptosis execution. Activation occurs upon recruitment to a complex containing a p53-induced death domain protein, PIDD. This suggests caspase-2 can be a nuclear initiator caspase with a requirement for caspase-9 and caspase-3 activation in downstream apoptotic events. In apoptotic pathways resulting from UV-induced DNA damage, processing of caspase-2 occurs downstream of mitochondrial dysfunction and of caspase-9 and caspase-3 activation, extending a possible role for caspase-2 as a parallel effector caspase. - Monoclonal Antibody. Recognizes an epitope in the p19 subunit of human, mouse, rat, monkey and dog caspase-2. Isotype: Rat IgG2akappa. Clone: 10C6. Applications: ELISA, FACS, ICC, IHC. Liquid. In PBS containing 0.02% sodium azide. Caspase-2 is a Class I caspase with a long prodomain necessary for nuclear localization. Upon activation of the apoptotic pathway, the procaspase is cleaved into smaller fragments. Caspase-2 is the nuclear apoptotic respondent to cellular genotoxic stress or mitotic catastrophe and is involved in the activation cascade of caspases responsible for apoptosis execution. Activation occurs upon recruitment to a complex containing a p53-induced death domain protein, PIDD. This suggests caspase-2 can be a nuclear initiator caspase with a requirement for caspase-9 and caspase-3 activation in downstream apoptotic events. In apoptotic pathways resulting from UV-induced DNA damage, processing of caspase-2 occurs downstream of mitochondrial dysfunction and of caspase-9 and caspase-3 activation, extending a possible role for caspase-2 as a parallel effector caspase.

Canine, Human, Monkey, Mouse, Rat

2°C to 8°C,-20°C

12352203