Product Name	p23 Antibody
Catalog #	SMC-156C
Package size	25ug

Alternate Product Sizes	SMC-156D
Type	Monoclonal
Conjugate	N/A
Datasheet	SMC 156 p23 Heat Shock
Description	Anti-p23
Research Area	Chaperones, Heat Shock, Trafficking
Alternative Names	co-chaperone p23, PTGES3, TEBP, telomerase binding protein p23, unactive progesterone receptor 23kDa
Clone Number	JJ6
Host Species	Mouse
Isotype	IgG1
Immunogen	Recombinant Human full length p23 protein
Applications	WB, IP, ELISA
Species Reactivity	Human, Mouses, Rabbit, Chicken, Guinea pig, S. cerevisiae (lower)
Accession Number	NP_006592.3
Gene ID	10728
SwissProt	Q15185
Background Info	Detects ~23kDa.
Recommended Dilutions	1:2000 (WB)
Form	Protein G Purified
Storage Buffer	PBS, 50% glycerol, 0.09% sodium azide
Concentration	1mg/mL
Certificate of Analysis	0.5μg/mL of SMC-156 was sufficient for detection of p23 in 20μg of heat shocked cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Storage Temp	-20 °C
Shipping Temp	Blue Ice or 4 °C

Research 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.
Cited References	1. Shimamura, T. et al. (2012). Ganetespib (STA-9090), a Nongeldanamycin HSP90 Inhibitor, Has Potent Antitumour Activity in In Vitro and In Vivo Models of Non-Small Cell Lung Cancer. Clin Cancer Res. 18, 4973-4985. doi: 10.1158/1078-0432.CCR-11-2967