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p23 Protein
Human Recombinant p23 Protein
Artikelnummer
STRSPR-303B
Verpackungseinheit
100 µg
Hersteller
Stressmarq Biosciences
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Target: p23 .
Nature: Recombinant.
Swiss-Prot: Q15185.
Expression System: E. coli.
Amino Acid Sequence: SHMQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE.
Purification: Affinity Purified.
Purity: >90%.
Storage Buffer: 20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol.
Protein Size: ~23 kDa.
Conjugate: No tag.
Cellular Localization: Cytoplasm.
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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
Nature: Recombinant.
Swiss-Prot: Q15185.
Expression System: E. coli.
Amino Acid Sequence: SHMQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE.
Purification: Affinity Purified.
Purity: >90%.
Storage Buffer: 20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol.
Protein Size: ~23 kDa.
Conjugate: No tag.
Cellular Localization: Cytoplasm.
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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
| Artikelnummer | STRSPR-303B |
|---|---|
| Hersteller | Stressmarq Biosciences |
| Hersteller Artikelnummer | SPR-303B |
| Green Labware | Nein |
| Verpackungseinheit | 100 µg |
| Mengeneinheit | STK |
| Reaktivität | Human |
| Methode | Western Blotting, Functional Assay, SDS-PAGE |
| Human Gene ID | 10728 |
| Produktinformation (PDF) | Download |
| MSDS (PDF) | Download |
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Gernot Ensinger, M.Sc.
Laurent Haze
