Application Note: HSP90β Protein is stored in 50mM NaPhosphate pH7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.2mM DTT, 25% glycerol. HSP90β Protein is suitable for use in Western Blot and ATPase Assay. Expect a band approximately ~91kDa on specific lysates or tissues. Specific conditions for reactivity should be optimized by the end user.
Concentration Value: 0.2 µg/µL
Western Blot Dilution: User Optimized
General Disclaimer Note: This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
Physical State: Liquid (sterile filtered)
Purity and Specificity: Recombinant full length human HSP90β was expressed by baculovirus in Sf9 insect cells using an N-Terminal his epitope. The purity was determined to be >90% by densitometry.
Background: HSP90β is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins (1). HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis (2). HSP90β Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, and Cellular Stress research.
Low Endotoxin: No
Other: ATPase Assay-User Optimized
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