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Agrisera
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Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
For reconstitution add 50 µL of sterile water.
Specific Species Reactivity: Arabidopsis thaliana, Brachypodium distachyon, Brassica napus, Chlamydomonas sp. UWO241, Fagopyrum esculentum, Hordeum vulgare, Salicornia sp., Solanum lycopersicum, Zea mays, Vicia faba
HSP90AA1 encodes the stress-inducible cytosolic molecular chaperone Hsp90alpha, a ~90 kDa protein that localizes predominantly to the cytosol but can also be detected in the nucleus; it functions as an ATP-dependent homodimer within multichaperone assemblies. Structurally, Hsp90alpha comprises an N-terminal ATP-binding domain, a charged linker, a middle domain that contributes to client and co-chaperone interactions, and a C-terminal dimerization domain that terminates in a conserved MEEVD motif used for docking tetratricopeptide repeat-containing co-chaperones. Biologically, Hsp90alpha is a central hub of proteostasis that promotes folding, maturation, stabilization, and regulated turnover of a broad set of client proteins (notably signaling proteins such as kinases and transcriptional regulators), thereby supporting stress adaptation and signal transduction; its chaperone cycle is driven by ATP binding/hydrolysis and is tuned by co-chaperones that modulate conformational transitions and client processing.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: ATHS83; AtHsp90-1; ATHSP90.1; F6N7.13; F6N7_13; HEAT SHOCK PROTEIN 81-1; HEAT SHOCK PROTEIN 83; HEAT SHOCK PROTEIN 90-1; heat shock protein 90.1; HSP81-1; HSP81.1; HSP83