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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-MAPKAPK-2 (Thr334) (27B7) Rabbit mAb 3007 40 µl
H M R Mk 49 Rabbit IgG
Phospho-HSP27 (Ser82) (D1H2) XP® Rabbit mAb 9709 40 µl
H M 27 Rabbit IgG
Phospho-SAPK/JNK (Thr183/Tyr185) (81E11) Rabbit mAb 4668 40 µl
H M R Dm Sc 46, 54 Rabbit IgG
Phospho-c-Jun (Ser73) (D47G9) XP® Rabbit mAb 3270 40 µl
H M R Mk Pg 48 Rabbit IgG
Phospho-p53 (Ser15) (16G8) Mouse mAb 9286 40 µl
H 53 Mouse IgG1
Cleaved Caspase-3 (Asp175) (5A1E) Rabbit mAb 9664 40 µl
H M R Mk 17, 19 Rabbit IgG
Cleaved PARP (Asp214) (D64E10) XP® Rabbit mAb 5625 40 µl
H Mk 89 Rabbit IgG
Phospho-p38 MAPK (Thr180/Tyr182) (D3F9) XP® Rabbit mAb 4511 40 µl
H M R Mk Mi Pg Sc 43 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
All Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 100 µl
All Horse 

Product Description

The Stress and Apoptosis Antibody Sampler Kit provides an economical means of evaluating stress and apoptotic responses of each protein. The kit contains enough primary and secondary antibody to perform four western blot experiments per primary antibody.


Specificity / Sensitivity

Each antibody in the Stress and Apoptosis Antibody Sampler Kit detects endogenous levels of target protein. Antibodies do not cross-react with any isoforms or phosphorylation sites of the target protein.


Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide correspond- ing to amino-terminal residues adjacent to Asp175 of human Caspase-3 or residues surrounding Asp214 of human PARP. Phospho-specific monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser82 of human HSP27, Ser73 of human c-Jun, Thr334 of human MAP- KAPK-2, Ser15 of human p53, Thr180/Tyr182 of human p38 MAPK, or Thr183/Tyr185 of human SAPK/JNK.

Cells respond to environmental or intracellular stresses through various mechanisms ranging from initiation of prosurvival strategies to activation of cell death pathways that remove damaged cells from the organism. Many of the proteins and cellular processes involved in normal signaling and survival pathways also play dual roles in cell death-promoting mechanisms. Apoptosis is a regulated cellular suicide mechanism characterized by nuclear condensation, cell shrinkage, membrane blebbing, and DNA fragmentation. Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). PARP appears to be involved in DNA repair in response to environmental stress (2). This protein can be cleaved by many ICE-like caspases in vitro (3,4) and is one of the main cleavage targets of caspase-3 in vivo (5,6). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (7). The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (8). DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to a reduced interaction between p53 and its negative regulator, the oncoprotein MDM2 (9). MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation (10,11). Stress-activated protein kinases (SAPK)/Jun amino-terminal kinases (JNK) are members of the MAPK family that are activated by a variety of environmental stresses, inflammatory cytokines, growth factors, and GPCR agonists. Stress signals are delivered to this cascade by small GTPases of the Rho family (Rac, Rho, cdc42) (12). SAPK/JNK, when active as a dimer, can translocate to the nucleus and regulate transcription through its effects on c-Jun, ATF-2, and other transcription factors (12,13). c-Jun is a member of the Jun Family, containing c-Jun, JunB, and JunD, and is a component of the transcription factor AP-1 (activator protein-1). Extracellular signals from growth factors, chemokines, and stress activate AP-1-dependent transcription. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73 through SAPK/JNK (reviewed in 14). AP-1 regulated genes exert diverse biological functions including cell proliferation, differentiation, and apoptosis, as well as transformation, invasion and metastasis, depending on cell type and context (13, 15-17). p38 MAP kinase (MAPK), also called RK (18) or CSBP (19), is the mammalian orthologue of the yeast HOG kinase that participates in a signaling cascade controlling cellular responses to cytokines and stress (17-20). MKK3, MKK6, and SEK activate p38 MAP kinase by phosphorylation at Thr180 and Tyr182. MAPKAPK-2 is a direct target of p38 MAPK (17). Multiple residues of MAPKAPK-2 are phosphorylated in vivo in response to stress. However, only four residues (Thr25, Thr222, Ser272 and Thr334) are phosphorylated by p38 MAPK in an in vitro kinase assay (21). Phosphorylation at Thr222, Ser272, and Thr334 appears to be essential for the activity of MAPKAPK-2 (6). Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. In response to stress, the expression level of HSP27 increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-2 as a result of the activation of the p38 MAP kinase pathway (19,22).


1.  Chehab NH et al. (1999) Proc Natl Acad Sci U S A 96, 13777–82

2.  Fernandes-Alnemri, T. et al. (1994) J Biol Chem 269, 30761-4.

3.  Levine, A.J. (1997) Cell 88, 323-31.

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

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

6.  Davis, R.J. (2000) Cell 103, 239-52.

7.  Han, J. et al. (1994) Science 265, 808-11.

8.  Ben-Levy, R. et al. (1995) EMBO J. 14, 5920-5930.

9.  Landry, J. et al. (1992) J. Biol. Chem. 267, 794-803.

10.  Kyriakis, J.M. and Avruch, J. (2001) Physiol Rev 81, 807-69.

11.  Rouse, J. et al. (1994) Cell 78, 1027-1037.

12.  Lee, J.C. et al. (1994) Nature 372, 739-46.

13.  Shieh, S.Y. et al. (1997) Cell 91, 325-334.

14.  Freshney, N.W. et al. (1994) Cell 78, 1039-49.

15.  Honda, R. et al. (1997) FEBS Lett. 420, 25-27.

16.  Leppä, S. and Bohmann, D. (1999) Oncogene 18, 6158-62.

17.  Shaulian, E. and Karin, M. (2002) Nat Cell Biol 4, E131-6.

18.  Weiss, C. and Bohmann, D. (2004) Cell Cycle 3, 111-3.

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

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

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

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


Entrez-Gene Id 836, 3315, 3725, 9261, 142, 1432, 5600, 5603, 6300, 7157, 5599
Swiss-Prot Acc. P42574, P04792, P05412, P49137, P09874, Q16539, Q15759, O15264, P53778, P04637, P45983

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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.