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Goat anti-mouse IgM was used to bind 25 µl of protein G-Sepharose. MA5-45106 IgM from 0.5 ml of high speed supernatant medium was loaded onto the IgG resin and incubated with 100 µl of rabbit reticulocyte lysate for 30 min. at 30C. After washing (4X1 ml), bound proteins were resolved on SDS PAGE, including HSP90, HSP70 and Hop. |Detects 90kDa. Co-immunoprecipitates HSP90 complexes, including HSP70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha ) kinase (HRI).
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, an inducible form, and HSP90AB1 and mitochondria (Chen et al., 2005 ).
仅用于科研。不用于诊断过程。未经明确授权不得转售。