|Application ||WB, IHC, IP|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||84660 Da|
|Application & Usage||Western blotting (0.5-4 µg/ml), in immunoprecipitation (10-20 µg/ml) and Immunohistochemistry (frozen sections, 10-20 µg/ml). However, the optimal concentrations should be determined individually. The antibody recognizes Hsp90α and Hsp90β of human, mouse, and rat origins.|
|Other Names||HSP90AA1 , HSP90A , HSPCAL1 , HSPCAL4 , HSPN , HSPCA , HSP90N , LAP2 , HSPC1 , FLJ31884|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 30% glycerol, 0.5% BSA, and 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Hsp90 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||HSP90A, HSPC1, HSPCA|
|Function||Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11274138, PubMed:11276205, PubMed:15577939, PubMed:15937123, PubMed:27353360).|
|Cellular Location||Cytoplasm. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Provided below are standard protocols that you may find useful for product applications.
Heat shock proteins (HSPs) are ubiquitously expressed in all organisms. A major function of HSP90 and other HSPs is to act as molecular chaperones. HSP90 forms a complex with glucocorticoid receptor (GR), rendering the non ligand-bound receptor transcriptionally inactive. HSP 90 binds the GR as a heterocomplex composed of either HSP56 or cyclophilin-40, forming an aporeceptor complex. HSP90 also exists as a dimer with other proteins such as p60/sti1 and p23, forming an aporeceptor complex with estrogen and androgen receptors.
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