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To Purchase # 12742S

12742S 1 Kit (7 x 40 µl) $489.00
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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Caspase-3 (8G10) Rabbit mAb 9665 x 40 µl
H M R Mk 17, 19, 35 Rabbit IgG
Caspase-6 Antibody 9762 x 40 µl
H M R 15, 35 Rabbit 
Caspase-7 (D2Q3L) Rabbit mAb 12827 x 40 µl
H M R 20, 35 Rabbit IgG
Caspase-8 (1C12) Mouse mAb 9746 x 40 µl
H 18, 43, 57 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
Lamin A/C (4C11) Mouse mAb 4777 x 40 µl
H M R Mk 74 (Lamin A), 63 (Lamin C) Mouse IgG2a
PARP Antibody 9542 x 40 µl
H M R Mk 89, 116 Rabbit 
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 Procaspase Antibody Sampler Kit provides an economical means to evaluate the abundance and activation of caspases. The kit contains enough primary antibody to perform at least four western blots per primary antibody.


Specificity / Sensitivity

Each antibody in the Procaspase Antibody Sampler Kit detects endogenous levels of its respective target. Caspase-3 (8G10) Rabbit mAb detects full-length (35 kDa) and the large fragment (17/19 kDa) of caspase-3 resulting from cleavage at Asp175. Caspase-6 Antibody detects both full length caspase-6 (35 kDa) and the small subunit (15 kDa) of caspase-6 resulting from cleavage at Asp193. Caspase-7 (D2Q3L) Rabbit mAb detects both the full-length (35 kDa) and the large subunit (20 kDa) of caspase-7 resulting from cleavage at Asp198. Caspase-8 (1C12) Mouse mAb detects full length (57 kDa), the cleaved intermediate p43/p41, and the p18 fragment of caspase-8. Caspase-9 (C9) Antibody detects full-length caspase-9, as well as the large fragments resulting from cleavage at Asp315 and Asp330. PARP Antibody detects full length PARP1 (116 kDa), as well as the large fragment (89 kDa) of PARP1 resulting from caspase cleavage at Asp214. Lamin A/C (4C11) Mouse mAb detects full-length lamin A and lamin C proteins, as well as the larger fragments of lamin A (50 kDa) and lamin C (41 kDa) resulting from caspase cleavage. Caspase-9 (C9) Antibody detects the pro form of caspase-9 as well as cleaved fragments.


Source / Purification

Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues adjacent to (Asp175) in human caspase-3 protein, residues surrounding Pro158 of human caspase-7 protein, the carboxy-terminal sequence of the p18 fragment of human caspase-8 protein, recombinant human caspase-9 protein or human lamin A protein.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the cleavage site of caspase-6 or the caspase cleavage site in PARP. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.

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 the 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 like PARP, α-fodrin, DFF and lamin A, and induce apoptosis (1,2).

Caspase-8 (FLICE, Mch5, MACH) and Caspase-9 (ICE-LAP6, Mch6) are initiator caspases. CD95 receptor (Fas/APO-1) and tumor necrosis factor receptor 1 (TNFR1) activate caspase-8, leading to the release of the caspase-8 active fragments, p18 and p10 (3-6). Cytochrome c released from the mitochondria associates with procaspase-9 (47 kDa)/Apaf 1. Apaf-1 mediated activation of caspase-9 involves intrinsic proteolytic processing resulting in cleavage at Asp315 and producing a p35 subunit. Another cleavage occurs at Asp330 producing a p37 subunit that can serve to amplify the apoptotic response (7-11).

Caspase-3 (CPP-32, Apoptain, Yama, SCA-1), Caspase-6 (Mch2), and Caspase-7 (CMH-1, Mch3, ICE-LAP3) are effector caspases (12-16). Activation of caspase-3 requires proteolytic processing of its inactive zymogen/proform into activated p17 and p12 subunits (17). Procaspase-7 is activated through proteolytic processing by upstream caspases at Asp23, Asp198, and Asp206 to produce the mature subunits (14,16). Procaspase-6 is cleaved by caspase-3 at Asp23, Asp179 and Asp193 to form active large (p18) and small (p11) subunits (7).

PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (18). This protein can be cleaved by many ICE-like caspases in vitro (2,19) and is one of the main cleavage targets of caspase-3 in vivo (17,20). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (17,19). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (21).

Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (22-24). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into large (41-50 kDa) and small (28 kDa) fragments (24,25). The cleavage of lamins results in nuclear disregulation and cell death (26,27).


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.  Fernandes-Alnemri, T. et al. (1995) Cancer Res. 55, 6045-6052.

4.  Gruenbaum, Y. et al. (2000) J Struct Biol 129, 313-23.

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

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

7.  Duan, H. et al. (1996) J. Biol. Chem. 271, 1621-1625.

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

9.  Goldberg, M. et al. (1999) Crit Rev Eukaryot Gene Expr 9, 285-93.

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

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

12.  Lippke, J. A. et al. (1996) J. Biol. Chem. 271, 1825-1828.

13.  Yabuki, M. et al. (1999) Physiol Chem Phys Med NMR 31, 77-84.

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

15.  Rao, L. et al. (1996) J Cell Biol 135, 1441-55.

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

17.  Orth, K. et al. (1996) J Biol Chem 271, 16443-6.

18.  Oberhammer, F.A. et al. (1994) J Cell Biol 126, 827-37.

19.  Duan, H. et al. (1996) J Biol Chem 271, 16720-4.

20.  Srinivasula, S.M. et al. (1996) J Biol Chem 271, 27099-106.

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

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

23.  Faleiro, L. et al. (1997) EMBO J 16, 2271-81.

24.  Satoh, M.S. and Lindahl, T. (1992) Nature 356, 356-8.

25.  Lazebnik, Y.A. et al. (1994) Nature 371, 346-7.

26.  Tewari, M. et al. (1995) Cell 81, 801-9.

27.  Oliver, F.J. et al. (1998) J Biol Chem 273, 33533-9.


Entrez-Gene Id 836, 839, 840, 841, 842, 4000, 142
Swiss-Prot Acc. P42574, P55212, P55210, Q14790, P55211, P02545, P09874


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U.S. Patent No. 5,675,063.