p23 (AA 1-94) antibody
Western Blotting (WB), Immunofluorescence (IF)
|4 references available|
|Quantity||50 µg (250 µg/ml)|
|Price||Product not available in this region.|
|Description||Molecular chaperones are a diverse group of proteins that modulate polypeptide stability through a process of ATP hydrolysis and the interaction with exposed hydrophobic residues on substrate proteins. Members of the heat shock protein (Hsp) group of chaperones were so named because their expression is rapidly induced upon heat shock or stress. Hsp90 and Hsp70 form complexes with chaperone accessory factors, such as TCP-1, Hsp104, HiP, immunophilins (FKBP52 and FKBP51), HOP, Hsp40, Bag-1, and p23. A complex of Hsp90, Hsp70, p48, Cyp-40, and p60 is known as the steroid aporeceptor complex that maintains a high affinity binding site in unbound intracellular hormone receptors. p23 is a widely expressed chaperone-associated protein that interacts with the ligand-bound steroid holoreceptor complex, and regulates holoreceptor-mediated transcriptional activity. In addition, p23/Hsp90 complexes may regulate telomerase complex assembly, and remain associated with the active telomerase holoenzyme. Thus, p23 is a chaperone accessory factor involved in the assembly of protein complexes, such as steroid hormone receptor and telomerase complexes.|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
|Molecular Weight||23 kDa|
Related Products: ABIN967389
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at -20° C.|
|Research Area||Cancer, Metabolism|
|Restrictions||For Research Use only|
|Western blot analysis of p23 on a mouse testis lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-p23 antibody. Immunofluorescence staining of normal rat kidney cells.|
Johnson, Beito, Krco et al.: "Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes." in: Molecular and cellular biology, Vol. 14, Issue 3, pp. 1956-63, 1994 (PubMed).
Freeman, Toft, Morimoto: "Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23." in: Science (New York, N.Y.), Vol. 274, Issue 5293, pp. 1718-20, 1997 (PubMed).
Freeman, Felts, Toft et al.: "The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies." in: Genes & development, Vol. 14, Issue 4, pp. 422-34, 2000 (PubMed).
Forsythe, Jarvis, Turner et al.: "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase." in: The Journal of biological chemistry, Vol. 276, Issue 19, pp. 15571-4, 2001 (PubMed).