p23 Protein__Human Recombinant p23 Protein UNC0643
Storage Buffer
20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Storage Temperature
-20ºC
Shipping Temperature
Blue Ice or 4ºC
Purification
Affinity Purified
Specificity
~23 kDa
Cite This Product
Human Recombinant p23 Protein (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-303)
Certificate of Analysis
This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-303, when added to 2uM SPR-300 (Aha1)-activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).
Alternative Names
Sid 3177 Protein, Co chaperone p23 Protein, cPGES Protein, HSP90 co chaperone Protein, cytosolic prostaglandin E2 synthase Protein, PTGES3 Protein, TEBP Protein, Prostaglandin E synthase 3 protein
Research Areas
Cancer, Heat Shock
Cellular Localization
Cytoplasm
Accession Number
NP_006592.3
Gene ID
10728
Swiss Prot
Q15185
Scientific Background
p23 is a highly conserved ubiquitous protein, known to have an important function as a cochaperone for the HSP90 chaperoning system (1). Studies have revealed that p23 is a small protein (18 to 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 phosphor-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 kinase (4), the heme regulated kinase HRI (5), hsf1 transcription factor (4), aryl hydrocarbon receptor (4), telomerase (6), and Hepadnavirus reverse transcriptase (7). In spite of several years of study, the exact functional significance of p23 is still not clear (8). p23 is thought to be involved in the adenosine triphosphate–mediated HSP90 binding of client proteins (8). 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 (9). HSP90 and its co-chaperone p23 are certainly among the emerging anti-tumor targets in oncology.
References
1. Johnson J.L., Beito T. G., Krco C.J. & Toft D.O. (1994) Mol Cell Biol. 14: 1956-63.
2. Weikl T., Abelmann K. & Buchner J. (1999) J Mol Biol. 293: 685-91.
3. Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A. & Toft, D.O. (2000) J Biol Chem. 275: 23045-52.
4. Nair S.C., et al. (1996) Cell Stress Chaperones. 1: 237-50.
5. Xu Z., et al. (1997) Eur J Biochem. 246, 461-70.
6. Holt S.E., et al. (1999) Genes Dev. 13: 817-26.
7. Hu J., Toft D., Anselmo D. & Wang X. (2002) J Virol. 76: 269-79.
8. Felts S.J. & Toft D.O. (2003) Cell Stress Chaperones. 8: 108-13.
9. Gausdal G., Gjertsen B.T., Fladmark K.E., Demol H., Vandekerckhove J. & Doskeland S.O. (2004) Leukemia.
2. Weikl T., Abelmann K. & Buchner J. (1999) J Mol Biol. 293: 685-91.
3. Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A. & Toft, D.O. (2000) J Biol Chem. 275: 23045-52.
4. Nair S.C., et al. (1996) Cell Stress Chaperones. 1: 237-50.
5. Xu Z., et al. (1997) Eur J Biochem. 246, 461-70.
6. Holt S.E., et al. (1999) Genes Dev. 13: 817-26.
7. Hu J., Toft D., Anselmo D. & Wang X. (2002) J Virol. 76: 269-79.
8. Felts S.J. & Toft D.O. (2003) Cell Stress Chaperones. 8: 108-13.
9. Gausdal G., Gjertsen B.T., Fladmark K.E., Demol H., Vandekerckhove J. & Doskeland S.O. (2004) Leukemia.