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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-cdc2 (Tyr15) (10A11) Rabbit mAb 4539 40 µl
Western Blotting Immunoprecipitation Immunofluorescence Flow Cytometry
H M R Mk 34 Rabbit IgG
Phospho-Chk1 (Ser345) (133D3) Rabbit mAb 2348 40 µl
Western Blotting Immunofluorescence Flow Cytometry
H M R Mk 56 Rabbit IgG
Phospho-Chk2 (Thr68) (C13C1) Rabbit mAb 2197 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Flow Cytometry
H 62 Rabbit IgG
Phospho-Rb (Ser807/811) (D20B12) XP® Rabbit mAb 8516 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry
H M R Mk 110 Rabbit IgG
Phospho-Rb (Ser795) Antibody 9301 40 µl
Western Blotting Immunoprecipitation
H R Mk 110 Rabbit 
Phospho-p53 (Ser15) (16G8) Mouse mAb 9286 40 µl
Western Blotting Immunofluorescence Flow Cytometry
H 53 Mouse IgG1
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 100 µl
Western Blotting
All Horse 

Product Description

The Cell Cycle/Checkpoint Antibody Sampler Kit provides a fast and economical means of evaluating multiple proteins involved in the cell cyle and checkpoint control. The kit contains enough primary and secondary antibody to perform four Western blot experiments.


Specificity / Sensitivity

Phospho-cdc2 (Tyr15) (10A11) Rabbit mAb detects endogenous levels of cdc2 protein only when phosphorylated at tyrosine 15. Based on sequence similarity, the antibody may cross-react with CDK2 and CDK3. Phospho-Chk2 (Thr68) (C13C1) Rabbit mAb detects endogenous levels of Chk2 only when phosphorylated at Thr68. Phospho-Chk1 (Ser345) Antibody detects Chk1 only when phosphorylated at Ser345 and does not cross-react with other proteins. Phospho-Rb (Ser795) Antibody detects Rb only when phosphorylated at Ser795 and does not cross-react with Rb phosphorylated at other sites. Phospho-Rb (Ser807/811) (D20B12) XP® Rabbit mAb recognizes endogenous levels of Rb protein only when phosphorylated at Ser807, Ser811, or at both sites. This antibody does not cross-react with Rb phosphorylated at Ser608. Phospho-p53 (Ser15) (16G8) Mouse mAb detects endogenous levels of p53 only when phosphorylated at Ser15. The antibody does not cross-react with p53 phosphorylated at other sites.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser795 of human Rb. Polyclonal antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser807/811 of human Rb protein, residues surrounding Ser345 of human Chk1, residues surrounding Ser15 of human p53, residues surrounding Tyr15 of human cdc2, and residues surrounding Thr68 of human Chk2.

The cell division cycle demands accuracy to avoid the accumulation of genetic damage. This process is controlled by molecular circuits called "checkpoints" that are common to all eukaryotic cells (1). Checkpoints monitor DNA integrity and cell growth prior to replication and division at the G1/S and G2/M transitions, respectively. The cdc2-cyclin B kinase is pivotal in regulating the G2/M transition (2,3). Cdc2 is phosphorylated at Thr14 and Tyr15 during G2-phase by the kinases Wee1 and Myt1, rendering it inactive. The tumor suppressor protein retinoblastoma (Rb) controls progression through the late G1 restriction point (R) and is a major regulator of the G1/S transition (4). During early and mid G1-phase, Rb binds to and represses the transcription factor E2F (5). The phosphorylation of Rb late in G1-phase by CDKs induces Rb to dissociate from E2F, permitting the transcription of S-phase-promoting genes. In vitro, Rb can be phosphorylated at multiple sites by cdc2, cdk2, and cdk4/6 (6-8). DNA damage triggers both the G2/M and the G1/S checkpoints. DNA damage activates the DNA-PK/ATM/ATR kinases, which phosphorylate Chk at Ser345 (9), Chk2 at Thr68 (10) and p53 (11). The Chk kinases inactivate cdc25 via phosphorylation at Ser216, blocking the activation of cdc2.


1.  Nurse, P. (1997) Cell 91, 865-7.

2.  Sherr, C.J. (1996) Science 274, 1672-7.

3.  Norbury, C. and Nurse, P. (1992) Annu Rev Biochem 61, 441-70.

4.  Zhao, H. and Piwnica-Worms, H. (2001) Mol Cell Biol 21, 4129-39.

5.  Watanabe, N. et al. (1995) EMBO J 14, 1878-91.

6.  Dyson, N. (1998) Genes Dev 12, 2245-62.

7.  Lundberg, A.S. and Weinberg, R.A. (1998) Mol Cell Biol 18, 753-61.

8.  Matsuoka, S. et al. (2000) Proc. Natl. Acad. Sci. USA 97, 10389-10394.

9.  Tibbetts, R.S. et al. (1999) Genes Dev 13, 152-7.

10.  Kitagawa, M. et al. (1996) EMBO J 15, 7060-9.

11.  Harbour, J.W. et al. (1999) Cell 98, 859-69.


Entrez-Gene Id 983 , 1111 , 11200 , 7157 , 5925
Swiss-Prot Acc. P06493 , O14757 , O96017 , P04637 , P06400

Protein Specific References

Smits VA et al. (2000) J Biol Chem 275, 30638–43

Casagrande F and Darbon JM (2001) Biochem Pharmacol 61, 1205–15

Yarden RI et al. (2002) Nat Genet 30, 285–9

Lee S et al. (2002) Cancer Res 62, 5703–10

Chao JI et al. (2004) J Biol Chem 279, 20267–76

Xiao D et al. (2004) Mol Cancer Ther 3, 567–75

Wang G et al. (2005) Cell Mol Life Sci 62, 881–93

Normand G et al. (2005) J Biol Chem 280, 7118–30

Yamaura M et al. (2009) Cancer Res 69, 2647–54

Olsen BB et al. (2010) Int J Oncol 36, 1175–82

Ahn J and Prives C (2002) J Biol Chem 277, 48418–26

Xu X et al. (2002) Mol Cell Biol 22, 4419–32

Lou Z et al. (2003) Nature 421, 957–61

Tsvetkov L et al. (2003) J Biol Chem 278, 8468–75

Bartkova J et al. (2004) Oncogene 23, 8545–51

Yin MB et al. (2004) Mol Pharmacol 66, 153–60

Li J and Stern DF (2005) J Biol Chem 280, 12041–50

Buscemi G et al. (2006) Mol Cell Biol 26, 7832–45

Yoda A et al. (2006) J Biol Chem 281, 24847–62

Sodha N et al. (2006) Cancer Res 66, 8966–70

Kass EM et al. (2007) J Biol Chem 282, 30311–21

Oliva-Trastoy M et al. (2007) Oncogene 26, 1449–58

Gabant G et al. (2008) J Mol Biol 380, 489–503

Guo X et al. (2010) J Biol Chem 285, 33348–57

Ahn, J.Y. et al. (2000) Cancer Res. 60, 5934-5936.

Brantley MA Jr and Harbour JW (2000) Cancer Res 60, 4320–3

Panigone S et al. (2000) Oncogene 19, 4035–41

Chan HM et al. (2001) Nat Cell Biol 3, 667–74

Taneja SS et al. (2001) J Cell Biochem 84, 188–99

Schroeder MD et al. (2002) Mol Endocrinol 16, 45–57

Balasenthil S and Vadlamudi RK (2003) J Biol Chem 278, 22119–27

Huang H et al. (2004) Oncogene 23, 2161–76

Benzeno S et al. (2004) Cancer Res 64, 3885–91

Youn CK et al. (2005) Nat Cell Biol 7, 137–47

Schmitz NM et al. (2005) Leukemia 19, 1783–7

Leibundgut K et al. (2005) Stem Cells 23, 1002–11

Wallick CJ et al. (2005) Oncogene 24, 5606–18

Roesch A et al. (2005) Mod Pathol 18, 565–72

Swarbrick A et al. (2005) Oncogene 24, 381–9

Ledl A et al. (2005) Oncogene 24, 3810–8

Hamdane M et al. (2005) J Cell Sci 118, 1291–8

Schmitz NM et al. (2006) Am J Pathol 169, 1074–9

Inoue Y et al. (2007) EMBO J 26, 2083–93

Park Y et al. (2008) Cell Cycle 7, 2384–91

Chang TW et al. (2008) Oncogene 27, 332–8

Boulay PL et al. (2011) Oncogene 30, 3846–61

Sen S et al. (2011) J Biol Chem 286, 36580–91

Lentine B et al. (2012) Cell Cycle 11, 3324–30

Brantley MA Jr and Harbour JW (2000) Cancer Res 60, 4320–3

Panigone S et al. (2000) Oncogene 19, 4035–41

Chan HM et al. (2001) Nat Cell Biol 3, 667–74

Taneja SS et al. (2001) J Cell Biochem 84, 188–99

Schroeder MD et al. (2002) Mol Endocrinol 16, 45–57

Balasenthil S and Vadlamudi RK (2003) J Biol Chem 278, 22119–27

Huang H et al. (2004) Oncogene 23, 2161–76

Benzeno S et al. (2004) Cancer Res 64, 3885–91

Youn CK et al. (2005) Nat Cell Biol 7, 137–47

Schmitz NM et al. (2005) Leukemia 19, 1783–7

Leibundgut K et al. (2005) Stem Cells 23, 1002–11

Wallick CJ et al. (2005) Oncogene 24, 5606–18

Roesch A et al. (2005) Mod Pathol 18, 565–72

Swarbrick A et al. (2005) Oncogene 24, 381–9

Ledl A et al. (2005) Oncogene 24, 3810–8

Hamdane M et al. (2005) J Cell Sci 118, 1291–8

Schmitz NM et al. (2006) Am J Pathol 169, 1074–9

Inoue Y et al. (2007) EMBO J 26, 2083–93

Park Y et al. (2008) Cell Cycle 7, 2384–91

Chang TW et al. (2008) Oncogene 27, 332–8

Boulay PL et al. (2011) Oncogene 30, 3846–61

Sen S et al. (2011) J Biol Chem 286, 36580–91

Lentine B et al. (2012) Cell Cycle 11, 3324–30


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.

9917
Cell Cycle/Checkpoint Antibody Sampler Kit