|Reactivity||Human Mouse Rat|
|Tested applications||WB IHC IF IP FC|
|Recommended Dilution||WB 1:500 - 1:2000
IHC 1:50 - 1:200
IF 1:50 - 1:200
IP 1:20 - 1:50
FC 1:20 - 1:50|
|Observed MW||Refer to Figures|
|Immunogen||Recombinant protein of human HSP90B1|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
|Synonym||CGP; GP96; GRP94; TRA1|
HSP90 proteins are highly conserved molecular chaperones, which normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 (GP96 or GRP94) is an endoplasmic reticulum paralogue of the cytosolic HSP90. As a major ER chaperone to mediate the UPR and a master chaperone for Toll-like receptors (TLRs), HSP90b1 chaperones peptides to MHC class I molecules of dendritic cells and other antigen-presenting cells, as well as facilitating the assembly of immunoglobulin. The protein is also involved in many other bio-processes. This antibody was generated against the C-terminal region of full-length HSP90b1.
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