HSP90 has been identified in the cytosol， nucleus and endoplasmic reticulum， and is reported to exist in many tissue types. In several tissues， including smooth muscle， HSP90 comprises up to 2% of total cellular protein. HSP90 functions as a dimer， assembled as part of heterocomplex. It possesses ATP-binding site and low ATPase activity. HSP90 is able to associate with actin filaments in certain conditions. Another important property of HSP90 is the binding of unoccupied steroid hormone receptors. HSP90 has been characterized as a molecular chaperone able to keep the target protein in a folding-competent state. It has an enhanced chaperone activity in oligomeric form at high temperatures. HSP90 function is sensitive to bivalent cations concentration.
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来源宿主
大肠杆菌中重组表达
溶解建议
Sterile filtered colorless solution. The HSP90 protein solution contains 20mM Tris-HCl， pH-7.4 and 100mM NaCl.
保存建议
Store at 4℃ if entire vial will be used within 2-4 weeks.
Store， frozen at -20℃ for longer periods of time.
For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）.
Avoid multiple freeze-thaw cycles.
