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| Product Name | Heat Shock Protein 90, Co-chaperone p23 |
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| Description | Purity ~90%. 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 25kD) 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 pro |
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| Size | 50ug, 100ug |
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| Concentration | n/a |
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| Applications | WB |
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| Other Names | Heat Shock Protein 90, Co-chaperone p23 (HSP90, Telomerase-Binding Protein p23, Progesterone Receptor Complex p23) |
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| Gene, Accession, CAS # | SwissProt: Q15185 |
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| Catalog # | H1834-62 |
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| Order / More Info | Heat Shock Protein 90, Co-chaperone p23 from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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