*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
293T , A431 , HeLa , HepG2 , NIH3T3 , PC-12 , Rat-2
Zebrafish, Bovine, Dog, Chicken, Pig, Xenopus laevis, Chimpanzee, Rhesus Monkey(>80% identity)
1XPBS, 20% Glycerol (pH7). 0.025% ProClin 300 was added as a preservative.
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
1mg/ml(Please refer to the vial label for the specific concentration.)
Recombinant protein encompassing a sequence within the C-terminus region of human GRP94. The exact sequence is proprietary.
Purified by antigen-affinity chromatography.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
ECGP antibody, GP96 antibody, GRP94 antibody, TRA1 antibody, HSP90B1 antibody, endothelial cell (HBMEC) glycoprotein antibody, tumor rejection antigen 1 antibody, GRP-94 antibody, tumor rejection antigen (gp96) 1 antibody, Tumor rejection antigen-1 (gp96) antibody, 94 kDa glucose-regulated protein antibody, heat shock protein 90 kDa beta member 1 antibody, "glucose regulated protein, 94 kDa antibody", endoplasmin antibody, gp96 homolog antibody, "heat shock protein 90kDa beta (Grp94), member 1 antibody"
Endoplasmic reticulum lumen , Melanosome
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. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]