10011424  GRP94 Monoclonal Antibody (Clone 9G10)

GP96; Glucose Regulated Protein 94

• See below for pricing and ordering
• See more Flow Cytometry; Immunoprecipitation; Western Blot; Antibodies; Metabolism; Oxidative Injury

For active pharmaceutical ingredients (APIs) related to GRP94 Monoclonal Antibody (Clone 9G10), see Cayman Pharma

Antigen: purified recombinant GPR94 protein · Clone designation: 9G10 · Host: rat · Isotype: IgG2a · Application(s): WB. IP, and flow cytometry · Glucose regulated protein 94 (GRP94) is a constitutively expressed endoplasmic reticulum (ER) lumenal protein that is up-regulated in response to cellular stress such as heat shock, oxidative stress or glucose depletion. GRP94 is thought to play a role in protein translocation to the ER, in their subsequent folding and assembly, and in regulating protein secretion.1 GRP94 also plays a role in antigen presentation by accessing the endogenous pathway and eliciting specific cytotoxic T lymphocyte (CTL) responses to chaperone bound peptides via the major histocompatibility complex (MHC) class I pathway.2 GRP94 is a member of the Hsp90 family of stress proteins and shares sequence homology with its cytosolic equivalent, Hsp90.3 Both Hsp90 and GRP94 are calcium binding proteins.4 Despite sharing 50% sequence homology over its N domains and complete conservation in its ligand binding domains with Hsp90, GRP94, and Hsp90 differ in their interactions with regulatory ligands as GRP94 has weak ATP binding and hydrolysis activity.5 GRP94 exists as a homodimer and the two subunits interact at two distinct intermolecular sites, C-terminal dimerization domains and the N-terminal interacts with the middle domain of opposing subunits.6 GRP94 contains a carboxy terminal KDEL (Lys-Asp-Glu-Leu) sequence which is believed to aid in its retention in the ER.7
1  Ruddon, R.W., Bedows, E. Assisted protein folding. J Biol Chem 272(6) 3125-3128 (1997).
2  Srivastava, P.K., Udono, H., Blachere, N.E., et al. Heat shock protein transfer peptides during antigen processing and CTL priming. Immunogenetics 39(2) 93-98 (1994).
3  Mazzarella, R.A., Green, M. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J Biol Chem 262(18) 8875-8883 (1987).
4  Kang, H.S., Welch, W.J. Characterization and purification of the 94-kDa glucose-regulated protein. J Biol Chem 266(9) 5643-5649 (1991).
5  Soldano, K.L., Jivan, A., Nicchitta, C.V., et al. Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation. J Biol Chem 278(48) 48330-48338 (2003).
6  Chu, F., Maynard, J.C., Chiosis, G., et al. Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94. Protein Sci 15 1260-1269 (2006).
7  Peter, F., Van, P.N., Söling, H. Different sorting of Lys-Asp-Glu-Leu proteins in rat liver. J Biol Chem 267(15) 10631-10637 (1992).

Download Product Insert 83 Kb PDF

Pricing Information

Prices listed here are the Manufacturer's Suggested European Retail Price. The actual prices quoted by each individual distributor may vary. Please visit the Global Buyer's Guide on the Cayman Chemical (world) website to locate a distributor in your region.

This product is also available to buy in bulk quantities. Please contact us for a quote or to purchase.

Cayman strives to be a reliable biochemical reagent vendor by providing the best possible products and services. To ask for assistance with one of our products please contact our Technical Help staff.

Warning This product is not for human or veterinary use.

Item total €0.00
Shopping cart total €0.00
Size Price Quantity
50 µg €142.00
200 µg €306.00
Pricing updated 2010-08-01.
Prices are subject to change without notice.