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Caspase 3, Apoptosis-Related Cysteine Peptidase (CASP3) (Pro-form) antibody
Alternatives Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunoprecipitation (IP), Flow Cytometry (FACS)
|3 references available|
|Price||450.00 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Description||Other names: CASP3, CPP32, Caspase-3 subunit p12, Yama protein,SREBP cleavage activity 1|
|Characteristics||Rabbit Monoclonal Antibody|
|Specificity||A synthetic peptide correscponding to N-terminal residues of Human Pro-Caspase-3 was used as immunogen. The antibody only recognizes the pro-form of Caspase-3. It does not react with the cleaved forms (active enzyme) of Caspase-3.|
|Molecular Weight||35 kDA|
Background: Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. Caspase-3 (apopain, SCA-1, Yama and CPP32) is a member of the apoptosis execution functional group of caspases, and is either partially or totally responsible for the proteolytic cleavage of many key proteins during apoptosis, such as poly (ADP-ribose) polymerase (PARP) (1,2,3). Caspase-3 is a cytosolic protein found in cells as an inactive 32 kDa proenzyme. It is activated by proteolytic cleavage into two active subunits only when cells undergo apoptosis (3).
|Synonyms||CC3, Lice, Yama, CPP32, Apopain, Caspase-3, A830040C14Rik, Cas3, Casp3, DECAY, Drosophila executioner caspase related to Apopain/Yama, caspase 3, DmelCG14902, CG14902, DRICE, ICE, DmelCG7788, CG7788, casp3, xcpp32, CASP3|
|Application Notes||The suggested dilution is: WB: ~~ 1:1000 IP: ~~ 1:10 FC: ~~ 1:50 ICC: ~~ 1:100 IHC: ~~ 1:500|
|Buffer||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Caspase-3 Antibody (Pro) can be stored at -20°C for up to 12 months from time of receipt.|
|Research Area||Apoptosis/Necrosis, Signaling, Phospho-specific antibodies, Protein Modifications, Metabolism, Cell Structure|
|Restrictions||For Research Use only|
Nicholson, Ali, Thornberry et al.: "Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis." in: Nature, Vol. 376, Issue 6535, pp. 37-43, 1995 (PubMed).
Tewari, Quan, ORourke et al.: "Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase." in: Cell, Vol. 81, Issue 5, pp. 801-9, 1995 (PubMed).
Fernandes-Alnemri, Litwack, Alnemri: "CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme." in: The Journal of biological chemistry, Vol. 269, Issue 49, pp. 30761-4, 1995 (PubMed).