|The HSP90B1 hsp90b1 (Catalog #MBS604580) is an Antibody produced from Rat and is intended for research purposes only. The product is available for immediate purchase. The Glucose Regulated Protein 94 (Grp94, gp96) reacts with Bovine, Canine, Chicken, Guinea Pig, Hamster, Human, Monkey, Mouse, Porcine, Rabbit, Rat, Sheep, Xenopus and may cross-react with other species as described in the data sheet. MyBioSource\'s Glucose Regulated Protein 94 can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC).
Dilution: Western Blot (7,16-19): 0.5ug/ml
Immunohistochemistry: (9,11): 1:30
Immunoelectron Microscopy (10): 1:20
Optimal dilutions to be determined by researcher.
Rat immunoglobulins do not react well with Protein A. For immunoprecipitations, we recommend using Protein G. Researchers should empirically determine the suitability of the HSP90B1 hsp90b1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The HSP90B1 hsp90b1 product has the following accession number(s) (GI #553324) (Uniprot Accession #P14625). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
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Glucose-regulated protein 94, also known as Grp94 or gp96, is an abundant resident endoplasmic reticulum (ER) lumenal stress protein which together with cytosolic Hsp90 belongs to the Hsp90 family of molecular chaperones. Grp94 and other resident soluble proteins of the ER such as members of the Ca(2+) binding protein subfamily (CaBP), CaBPI and CaBP2 as well as calreticulin, possesses the COOH-terminal tetrapeptide Lys-Asp-Glu-Leu (KDEL) which is a sorting signal that is thought to lead to the retention of these proteins in the pre-Golgi compartments (1). Grp94 expression is upregulated by stress conditions such as glucose starvation and heat shock, which promote protein misfolding or unfolding (2). In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells (3,4). Grp94 and Hsp90 share high sequence identity and presumably identical adenosine nucleotide-dependent modes of regulation. But earlier data suggests that Hsp90 and Grp94 may differ in their nucleotide binding properties. The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket which also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol. However, the molecular basis for adenosine nucleotide-dependent regulation of Grp94 remains to be established. Recent data has identified a ligand dependent regulation of Grp94 function and suggest a model whereby Grp94 function is regulated through a ligand-dependent conversion of Grp94 from an inactive to an active conformation (5, 6).
Immunogen: Purified Grp94 isolated from chicken oviducts. Positive Control: HeLa Cell Lysate.