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PDP - Template Name: Antibody Sampler Kit
PDP - Template ID: *******4a3ef3a
  1. Products /
  2. Primary Antibodies /
  3. Initiator Caspases Antibody Sampler Kit

Initiator Caspases Antibody Sampler Kit #12675

    Product Information

    Kit Usage Information

    Protocols

    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 two western blots with each primary antibody.

    Specificity / Sensitivity

    Each antibody in the Initiator Caspases Antibody Sampler Kit recognizes its respective target at endogenous levels. Caspase-3 (D3R6Y) Rabbit mAb detects full-length caspase-3 (35 kDa) as well as the large subunit (p20) of caspase-3 resulting from cleavage during apoptosis. 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) (E5Z7N) Rabbit mAb recognizes caspase-9 protein 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 protein specific to either the p20 subunit of human caspase-3 protein, or human caspase-9 protein. Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to 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.

    Background

    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. Cohen, G.M. (1997) Biochem J 326 ( Pt 1), 1-16.
    3. Nagata, S. (1997) Cell 88, 355-65.
    4. Chinnaiyan, A.M. et al. (1995) Cell 81, 505-12.
    5. Boldin, M.P. et al. (1995) J Biol Chem 270, 7795-8.
    6. Hsu, H. et al. (1995) Cell 81, 495-504.
    7. Muzio, M. et al. (1996) Cell 85, 817-27.
    8. Boldin, M.P. et al. (1996) Cell 85, 803-15.
    9. Vincenz, C. and Dixit, V.M. (1997) J Biol Chem 272, 6578-83.
    10. Fernandes-Alnemri, T. et al. (1996) Proc Natl Acad Sci U S A 93, 7464-9.
    11. Kischkel, F.C. et al. (2001) J Biol Chem 276, 46639-46.
    12. Wang, J. et al. (2001) Proc Natl Acad Sci U S A 98, 13884-8.
    13. Hsu, H. et al. (1996) Cell 84, 299-308.
    14. Liu, X. et al. (1996) Cell 86, 147-57.
    15. Li, P. et al. (1997) Cell 91, 479-89.
    16. Zou, H. et al. (1999) J Biol Chem 274, 11549-56.
    17. Srinivasula, S.M. et al. (1998) Mol Cell 1, 949-57.
    18. Li, H. et al. (1997) J Biol Chem 272, 21010-7.
    19. Tinel, A. and Tschopp, J. (2004) Science 304, 843-6.
    20. Dirsch, V.M. et al. (2004) Oncogene 23, 1586-93.
    21. Castedo, M. et al. (2004) Oncogene 23, 4362-70.
    22. Paroni, G. et al. (2001) J Biol Chem 276, 21907-15.
    23. Fernandes-Alnemri, T. et al. (1994) J Biol Chem 269, 30761-4.
    24. Nicholson, D.W. et al. (1995) Nature 376, 37-43.

    Limited Uses

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    Products are labeled with For Research Use Only or a similar labeling statement and have not been approved, cleared, or licensed by the FDA or other regulatory foreign or domestic entity, for any purpose. Customer shall not use any Product for any diagnostic or therapeutic purpose, or otherwise in any manner that conflicts with its labeling statement. Products sold or licensed by CST are provided for Customer as the end-user and solely for research and development uses. Any use of Product for diagnostic, prophylactic or therapeutic purposes, or any purchase of Product for resale (alone or as a component) or other commercial purpose, requires a separate license from CST. Customer shall (a) not sell, license, loan, donate or otherwise transfer or make available any Product to any third party, whether alone or in combination with other materials, or use the Products to manufacture any commercial products, (b) not copy, modify, reverse engineer, decompile, disassemble or otherwise attempt to discover the underlying structure or technology of the Products, or use the Products for the purpose of developing any products or services that would compete with CST products or services, (c) not alter or remove from the Products any trademarks, trade names, logos, patent or copyright notices or markings, (d) use the Products solely in accordance with CST Product Terms of Sale and any applicable documentation, and (e) comply with any license, terms of service or similar agreement with respect to any third party products or services used by Customer in connection with the Products.

    For Research Use Only. Not For Use In Diagnostic Procedures.
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