| References |
| Synonyms |
- Telomerate-binding protein p23
- cPGE Synthase
- p23
- Hsp90 Co-chaperone
|
| Formulation |
protein G affinity-purified mouse IgG at a concentration of 1 mg/ml in PBS, pH 7.2, containing 0.09% sodium azide and 50% glycerol |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
| Specificity |
| Human p23 |
+ |
| Mouse p23 |
+ |
| Rabbit p23 |
+ |
| Chicken p23 |
+ |
| Guinea pig p23 |
+ |
| S. cerevisiae (lower) p23 |
+ |
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Background Reading
Johnson, J.J., Beito, T.G., Krco, C.J., et al. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol Cell Biol 14(3) 1956-1963 (1994).
Gausdal, G., Gjertsen, B.T., Fladmark, K.E., et al. Caspase-dependent, geldanamycin-enhanced cleavage of co-chaperone p23 in leukemic apoptosis. Leukemia 18 1989-1996 (2004).
Felts, S.J., and Toft, D.O. p23, a simple protein with complex activities. Cell Stress Chaperones 8(2) 108-113 (2003).
Hu, J., Toft, D., Anselmo, D., et al. In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins. J Virol 76(1) 269-279 (2002).
Holt, S.E., Aisner, D.L., Baur, J., et al. Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev 13 817-826 (1999).
Xu, Z., Pal, J.K., Thulasiraman, V., et al. The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2α kinase in reticulocyte lysates during heat stress. Eur J Biochem 246 461-470 (1997).
Nair, S.C., Toran, E.J., Rimerman, R.A., et al. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor. Cell Stress Chaperones 1(4) 237-250 (1996).
Weaver, A.J., Sullivan, W.P., Felts, S.J., et al. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J Biol Chem 275(30) 23045-23052 (2000).
Weikl, T., Abelmann, K., and Buchner, J. An unstructured C-terminal region of the Hsp90 co-chaperone p23 in important for its chaperone function. J Mol Biol 293 685-691 (1999).
Tanioka, T., Nakatani, Y., Semmyo, N., et al. Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 immediate prostaglandin E2 biosynthesis. J Biol Chem 275 32775-32782 (2000).
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| Size |
Global Purchasing |
| 25 µg |
|
| 100 µg |
|
Description
Antigen:
Recombinant human full length p23 protein
·
Clone designation:
JJ6
·
Host:
Mouse
·
Isotype:
IgG1
·
Application(s):
WB,IP, and ELISA
·
Mr:
23 kDa
·
p23 is a highly conserved ubiquitous protein, known to have an important function as a co-chaperone for the Hsp90 chaperoning system.1 Studies have revealed that p23 is a small protein (18-25 kDa) with a simple structure.2,3 p23 does not have any structural homology with any other known proteins.1 p23 was first discovered as a part of the Hsp90-progesterone receptor complex along with Hsp70, p54, and p50.1 p23 is a phospho-protein, which is highly acidic and has an aspartic acid-rich C-terminal domain.1 Numerous studies have found p23 to be associated with other client proteins like Fes tyrosine kinase4, the heme-regulated kinase HRI5, Hsf1 transcription factor4, aryl hydrocarbon receptor4, telomerase6, and Hepadnavirus reverse transcriptase.7 In spite of several years of study, the exact functional significance of p23 is still not clear.p23 is identical to cytosolic prostaglandin E synthase (cPGES), coverting to PGH2 to PGE2 downstream of COX-1.8 p23 is also thought to be involved in the adenosine triphosphate-mediated Hsp90 binding of client proteins.9 Since many Hsp90 client proteins are involved in oncogenic survival signaling, a recent study has concluded p23 to be a promising target in leukemic apoptosis.10 Hsp90 and its co-chaperone p23 are certainly among the emerging anti-tumor targets in oncology.
1
Johnson, J.J., Beito, T.G., Krco, C.J., et al. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol Cell Biol 14(3) 1956-1963 (1994).
2
Weikl, T., Abelmann, K., and Buchner, J. An unstructured C-terminal region of the Hsp90 co-chaperone p23 in important for its chaperone function. J Mol Biol 293 685-691 (1999).
3
Weaver, A.J., Sullivan, W.P., Felts, S.J., et al. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J Biol Chem 275(30) 23045-23052 (2000).
4
Nair, S.C., Toran, E.J., Rimerman, R.A., et al. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor. Cell Stress Chaperones 1(4) 237-250 (1996).
5
Xu, Z., Pal, J.K., Thulasiraman, V., et al. The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2α kinase in reticulocyte lysates during heat stress. Eur J Biochem 246 461-470 (1997).
6
Holt, S.E., Aisner, D.L., Baur, J., et al. Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev 13 817-826 (1999).
7
Hu, J., Toft, D., Anselmo, D., et al. In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins. J Virol 76(1) 269-279 (2002).
8
Tanioka, T., Nakatani, Y., Semmyo, N., et al. Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 immediate prostaglandin E2 biosynthesis. J Biol Chem 275 32775-32782 (2000).
9
Felts, S.J., and Toft, D.O. p23, a simple protein with complex activities. Cell Stress Chaperones 8(2) 108-113 (2003).
10
Gausdal, G., Gjertsen, B.T., Fladmark, K.E., et al. Caspase-dependent, geldanamycin-enhanced cleavage of co-chaperone p23 in leukemic apoptosis. Leukemia 18 1989-1996 (2004).
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