- CITATIONS: 1
|Application ||WB, IHC-P, FC, IF, E|
|Other Accession||Q66HD0, Q29092, P08113, Q4R520, P08110, Q95M18|
|Reactivity||Human, Hamster, Mouse|
|Predicted||Bovine, Chicken, Monkey, Pig, Rat|
|Calculated MW||92469 Da|
|Antigen Region||16-43 aa|
|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|
|Target/Specificity||This HSP90B1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 16-43 amino acids from the N-terminal region of human HSP90B1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSP90B1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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|
Provided below are standard protocols that you may find useful for product applications.
HSP90B1 is 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.
Koo, B.H., et al. J. Biol. Chem. 285(1):197-205(2010) Suriano, R., et al. Glycobiology 19(12):1427-1435(2009) Lev, A., et al. J. Immunol. 183(7):4205-4210(2009)
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