|Reactivity||Human, Mouse, Rat|
|Description||Rabbit IgG polyclonal antibody for Endoplasmin(HSP90B1) detection. Tested with WB in Human;Mouse;Rat.|
|Reconstitution||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Other Names||Endoplasmin, 94 kDa glucose-regulated protein, GRP-94, Heat shock protein 90 kDa beta member 1, Tumor rejection antigen 1, gp96 homolog, HSP90B1, GRP94, TRA1|
|Calculated MW||92469 MW KDa|
|Application Details||Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat|
|Subcellular Localization||Endoplasmic reticulum lumen. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.|
|Immunogen||E.coli-derived human GRP94 recombinant protein (Position: R43-H221). Human GRP94 shares 99.4% and 98.9% amino acid (aa) sequence identity with mouse and rat GRP94, respectively.|
|Purification||Immunogen affinity purified.|
|Cross Reactivity||No cross reactivity with other proteins|
|Storage||At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.|
|Function||Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.|
|Cellular Location||Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Heat shock protein 90kDa beta member 1 (HSP90B1), known as endoplasmin, or GRP94, is a chaperone protein that in humans is encoded by the HSP90B1 gene. It is mapped to chromosome 12q23.3. This gene encodes a member of a family of adenosine triphosphate (ATP)-metabolizing molecular chaperones with roles in stabilizing and folding other proteins. The encoded protein is localized to melanosomes and the endoplasmic reticulum. Expression of this protein is associated with a variety of pathogenic states, including tumor formation.
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