|Application ||WB, IHC|
|Calculated MW||83264 Da|
|Other Names||Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSP90AB1, HSP90B, HSPC2, HSPCB|
|Target/Specificity||A synthetic peptide corresponding to residues in N-terminus of human Hsp90 β was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSP90 beta Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||HSP90B, HSPC2, HSPCB|
|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. 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.|
|Cellular Location||Cytoplasm. Melanosome. 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.
The 90-kDa heat shock protein (Hsp90) is a highly conserved, and abundant cytosolic homodimeric molecular chaperone (1). Hsp90 is distinguished from other chaperones in that most of its known substrates are signal transduction proteins, non activated steroid hormone receptors, several protooncogenic tyrosine and serine/threonine kinases and actin (2-3). Two isoforms which correspond to the major and minor isoform , (Hsp90 α and Hsp90 β ) can be found in nearly equal amount in humans, and operates as part of a multichaperone machinery in the cytosol, which includes Hsp70, peptidyl-prolyl isomerases and other cochaperones (3).
1. Lees-Miller S., Anderson C.W.; Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II.;J. Biol. Chem. 264:2431-2437(1989).
2. Lees-Miller S., Anderson C.W.; The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues.; J. Biol. Chem. 264:17275-17280(1989).
3. Lotz G.P., Lin H., Harst A., Obermann W.M.J.; Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.; J. Biol. Chem. 278:17228-17235(2003).
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