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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Cleaved Caspase-9 (Asp330) (D2D4) Rabbit mAb 7237 x 40 µl
H 37 Rabbit IgG
Caspase-3 (8G10) Rabbit mAb 9665 x 40 µl
H M R Mk 17, 19, 35 Rabbit IgG
Caspase-2 (C2) Mouse mAb 2224 x 40 µl
H 12, 14, 48 Mouse IgG1
Caspase-9 (C9) Mouse mAb 9508 x 40 µl
H M R Hm Mk 47 /37/35 (H). 51 /39/37 (R,M). Mouse IgG1
Caspase-8 (1C12) Mouse mAb 9746 x 40 µl
H 18, 43, 57 Mouse IgG1
Anti-rabbit IgG, HRP-linked Antibody 7074 x 100 µl
All Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 x 100 µl
All Horse 

Product Description

The Initiator Caspases Antibody Sampler Kit provides an economical means of evaluating initiator (apical) caspase proteins. The kit contains enough primary antibody to perform four western blots with each primary antibody.


Specificity / Sensitivity

Each antibody in the Initiator Caspases Antibody Sampler Kit recognizes endogenous levels of its respective target. Caspase-3 (8G10) Rabbit mAb recognizes full-length (35 kDa) and the large fragment (17/19 kDa) of caspase-3 resulting from cleavage at aspartic acid 175. Caspase-8 (1C12) Mouse mAb recognizes full length (57 kDa), the cleaved intermediate p43/p41, and the p18 fragment of caspase-8. Caspase-9 (C9) Antibody recognizes full-length caspase-9, as well as the large fragments resulting from cleavage at Asp315 and Asp330. Cleaved Caspase-9 (Asp330) (D2D4) Rabbit mAb recognizes caspase-9 only when cleaved at Asp330. Caspase-2 (C2) Mouse mAb recognizes procaspase-2, as well as its 14 and 12 kDa cleaved fragments.


Source / Purification

Monoclonal antibodies are produced by immunizing animals with a recombinant human caspase-9 protein or with a synthetic peptide corresponding to amino-terminal residues adjacent to (Asp175) in human caspase-3, residues surrounding Asp330 of human caspase-9, the carboxy-terminal sequence of the p18 fragment of human caspase-8, or the carboxy-terminal portion of human caspase-2.

Apoptosis is a regulated physiological process leading to cell death. Caspases, a family of cysteine acid proteases, are central regulators of apoptosis. Initiator caspases (including 2, 8, 9, 10 and 12) are closely coupled to proapoptotic signals, which include FasL, TNF-α, and DNA damage. Once activated, these caspases cleave and activate downstream effector caspases (including 3, 6 and 7), which in turn cleave cytoskeletal and nuclear proteins such as PARP, α-fodrin, DFF and lamin A; inducing apoptosis (1,2).

Formation of a death-inducing signaling complex (DISC) around the receptors for death factors, including FasL and TNF-α, is essential for receptor-mediated apoptosis (3). Upon ligand activation, Fas and TNF-R1 associate with death domain (DD) containing adaptor proteins FADD (Fas associated death domain) (4,5) and TRADD (TNF-R1 associated death domain) (6). In addition to a carboxy-terminal DD, FADD contains an amino-terminal death effector domain (DED) that binds to DEDs and activates initiator caspase 8 (FLICE, Mch5, MACH) and caspase 10 (FLICE2, Mch4) (7-12). TRADD does not contain a DED and therefore must associate with FADD in response to TNF-R1 driven apoptosis (13).

Caspase-9 (ICE-LAP6, Mch6) is activated through the mitochondrial-mediated pathway. Cytochrome c released from mitochondria associates with procaspase-9 (47 kDa)/Apaf-1. Apaf-1 mediated activation of caspase-9 involves proteolytic processing resulting in cleavage at Asp315 and producing a p35 subunit. Another cleavage occurs at Asp330 producing a p37 subunit that can amplify the apoptotic response (14-17).

Caspase-2 (Nedd2/ICH-1) is the nuclear apoptotic respondent to cellular genotoxic stress or mitotic catastrophe. The procaspase is cleaved at Asp316, producing a 14 kDa fragment and a 32 kDa prodomain/large subunit. Subsequent processing at Asp152 and Asp330 produces an 18 kDa large subunit and a 12 kDa small fragment (18). Activation occurs upon recruitment to a complex containing a p53-induced death domain protein, PIDD (19). This suggests that caspase-2 can be a nuclear initiator caspase with a requirement for caspase-9 and caspase-3 activation in downstream apoptotic events (20,22). 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 (22).

Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis and caspase-3 cleavage is a key indicator of initiator caspase activation. Caspase-3 is either partially or totally responsible for the proteolytic cleavage of many key proteins including the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (23). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments (24).


1.  Budihardjo, I. et al. (1999) Annu Rev Cell Dev Biol 15, 269-90.

2.  Fernandes-Alnemri, T. et al. (1994) J. Biol. Chem. 269, 30761-30764.

3.  Cohen, G.M. (1997) Biochem J 326 ( Pt 1), 1-16.

4.  Li, P. et al. (1997) Cell 91, 479-489.

5.  Nicholson, D. W. et al. (1995) Nature 376, 37-43.

6.  Nagata, S. (1997) Cell 88, 355-65.

7.  Muzio, M. et al. (1996) Cell 85, 817-27.

8.  Liu, X. et al. (1996) Cell 86, 147-157.

9.  Chinnaiyan, A.M. et al. (1995) Cell 81, 505-12.

10.  Boldin, M.P. et al. (1996) Cell 85, 803-15.

11.  Boldin, M.P. et al. (1995) J Biol Chem 270, 7795-8.

12.  Fernandes-Alnemri, T. et al. (1996) Proc Natl Acad Sci U S A 93, 7464-9.

13.  Hsu, H. et al. (1995) Cell 81, 495-504.

14.  Vincenz, C. and Dixit, V.M. (1997) J Biol Chem 272, 6578-83.

15.  Zou, H. et al. (1999) J Biol Chem 274, 11549-56.

16.  Kischkel, F.C. et al. (2001) J Biol Chem 276, 46639-46.

17.  Srinivasula, S.M. et al. (1998) Mol Cell 1, 949-57.

18.  Wang, J. et al. (2001) Proc Natl Acad Sci U S A 98, 13884-8.

19.  Hsu, H. et al. (1996) Cell 84, 299-308.

20.  Li, H. et al. (1997) J Biol Chem 272, 21010-7.

21.  Tinel, A. and Tschopp, J. (2004) Science 304, 843-6.

22.  Dirsch, V.M. et al. (2004) Oncogene 23, 1586-93.

23.  Castedo, M. et al. (2004) Oncogene 23, 4362-70.

24.  Paroni, G. et al. (2001) J Biol Chem 276, 21907-15.


Entrez-Gene Id 835, 836, 841, 842
Swiss-Prot Acc. P42575, P42574, Q14790, P55211


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.