|Application ||WB, IHC, FC, ICC, E|
|Reactivity||Human, Mouse, Rat, Monkey|
|Description||HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1 (MIM 140571), an inducible form, and HSP90AB1, a constitutive form.|
|Immunogen||Purified recombinant fragment of human HSP90AB1 expressed in E. Coli. |
|Formulation||Ascitic fluid containing 0.03% sodium azide.|
|Other Names||Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSP90AB1, HSP90B, HSPC2, HSPCB|
WB~~1/500 - 1/2000
IHC~~1/500 - 1/2000
IF~~1/200 - 1/1000
FC~~1/200 - 1/400
|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||HSP90AB1 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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