|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Caspase 2, Apoptosis-Related Cysteine Peptidase (CASP2) antibody
|Synonyms||ICH1, NEDD2, CASP-2, ICH-1L, ICH-1L/1S, ICH-1, Nedd2, Caspase-2, xCaspase-2|
Alternatives Western Blotting (WB), Flow Cytometry (FACS)
|4 references available|
|Price||450.00 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Description||Other names: CASP2, ICH1, NEDD2, Caspase-2 subunit p12, ICH-1 protease,Neural precursor cell expressed developmentally down-regulated protein 2|
|Characteristics||Rabbit Monoclonal Antibody|
|Specificity||A synthetic peptide corresponding to N-terminus of human Caspase-2 p15 subunit was used as immunogen. The antibody should recognize both pro-form (~50kDa) and p15 cleaved-form of Caspase-2.|
|Molecular Weight||48 kDA|
Background: Caspase-2 (Nedd2/ICH-1) is part of a family of aspartate-specific cysteine proteases that participate in programmed cell death, or apoptosis. Caspase-2 is localized to the nucleus, and has been shown to play roles in both positive and negative regulation of apoptosis (1). Upon apoptotic stimulation, pro-caspase-9 is cleaved in a series of steps to produce an 18-kDa large subunit and a 12-kDa small fragment (2). Caspase-2 can be a nuclear initiator caspase, as it has been shown to precede the processing and activation of caspase-8, -9, and -3 (3). Caspase-2 might also act as an effector caspase, in apoptotic pathways resulting from UV-induced DNA damage, processing of caspase-2 occurs downstream of caspase-9 and caspase-3 activation (4).
|Application Notes||The suggested dilution is: WB: ~~ 1:500 FC: ~~ 1:10|
|Buffer||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Caspase-2 Antibody can be stored at -20°C for up to 12 months from time of receipt.|
|Research Area||Apoptosis/Necrosis, Signaling, Protein Modifications, Metabolism, Cell Structure|
|Restrictions||For Research Use only|
Wang, Miura, Bergeron et al.: "Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death." in: Cell, Vol. 78, Issue 5, pp. 739-50, 1994 (PubMed).
Li, Bergeron, Cryns et al.: "Activation of caspase-2 in apoptosis." in: The Journal of biological chemistry, Vol. 272, Issue 34, pp. 21010-7, 1997 (PubMed).
Paroni, Henderson, Schneider et al.: "Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3." in: The Journal of biological chemistry, Vol. 276, Issue 24, pp. 21907-15, 2001 (PubMed).
Dirsch, Kirschke, Estermeier et al.: "Apoptosis signaling triggered by the marine alkaloid ascididemin is routed via caspase-2 and JNK to mitochondria." in: Oncogene, Vol. 23, Issue 8, pp. 1586-93, 2004 (PubMed).