This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.
product summary
company name :
Enzo Life Sciences
other brands :
Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis
product type :
antibody
product name :
Grp94 monoclonal antibody (9G10) (PE conjugate)
catalog :
ADI-SPA-850PE-D
quantity :
50 µg
clonality :
monoclonal
host :
rat
conjugate :
PE
clone name :
9G10

The same clone is also sold as:
reactivity :
human, mouse, rat, dogs, chicken, bovine
application :
flow cytometry
citations: 8
Reference
Di X, Wang Y, Han D, Fu Y, Duerfeldt A, Blagg B, et al. Grp94 Protein Delivers γ-Aminobutyric Acid Type A (GABAA) Receptors to Hrd1 Protein-mediated Endoplasmic Reticulum-associated Degradation. J Biol Chem. 2016;291:9526-39 pubmed publisher
Chhabra S, Jain S, Wallace C, Hong F, Liu B. High expression of endoplasmic reticulum chaperone grp94 is a novel molecular hallmark of malignant plasma cells in multiple myeloma. J Hematol Oncol. 2015;8:77 pubmed publisher
Alkhateeb A, Buckett P, Gardeck A, Kim J, Byrne S, Fraenkel P, et al. The small molecule ferristatin II induces hepatic hepcidin expression in vivo and in vitro. Am J Physiol Gastrointest Liver Physiol. 2015;308:G1019-26 pubmed publisher
Patel P, Yan P, Seidler P, Patel H, Sun W, Yang C, et al. Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. Nat Chem Biol. 2013;9:677-84 pubmed publisher
Hong F, Liu B, Chiosis G, Gewirth D, Li Z. ?7 helix region of ?I domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasis. J Biol Chem. 2013;288:18243-8 pubmed publisher
Barton E, Park S, James J, Makarewich C, Philippou A, Eletto D, et al. Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production. FASEB J. 2012;26:3691-702 pubmed publisher
Wu S, Hong F, Gewirth D, Guo B, Liu B, Li Z. The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain. J Biol Chem. 2012;287:6735-42 pubmed publisher
Xargay Torrent S, Lopez Guerra M, Saborit Villarroya I, Rosich L, Campo E, Roué G, et al. Vorinostat-induced apoptosis in mantle cell lymphoma is mediated by acetylation of proapoptotic BH3-only gene promoters. Clin Cancer Res. 2011;17:3956-68 pubmed publisher
product information
Product ID :
ADI-SPA-850PE
Catalog Number :
ADI-SPA-850PE-D
Product Name :
Grp94 monoclonal antibody (9G10) (PE conjugate)
Host species :
Rat
Clonality :
Monoclonal
Conjugation :
PE
Product Type :
Antibody
Size :
50 µg
list of Pubmed id :
23995768
Clone :
9G10
Isotype :
IgG2a
SPECIES REACTIVITY :
Human, Mouse, Rat, Xenopus, Sheep, Rabbit, Porcine, Monkey, Hamster, Guinea pig, Dog, Chicken, Bovine
Background :
Glucose-regulated protein 94 (Grp94, gp96), an abundant resident endoplasmic reticulum (ER) lumenal stress protein, belongs to the Hsp90 family of molecular chaperones along with cytosolic Hsp90. Grp94 and such other resident soluble proteins of the ER as the Ca 2+ binding protein subfamily (CaBP, CaBPI, CaBP2 and calreticulin) possess the C-terminal tetrapeptide Lys-Asp-Glu-Leu (KDEL), a sorting signal considered responsible for the retention of these proteins in the pre-Golgi compartments. Stress conditions such as glucose starvation and heat shock which promote protein misfolding or unfolding increase Grp94 expression. 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. Grp94 and Hsp90 share high sequence identity and apparently identical adenosine nucleotide dependent modes of regulation, although previous 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 unclear. Data supports a ligand dependent regulation of Grp94 function, and suggests a model whereby Grp94 function is regulated through a ligand -dependent conversion of Grp94 from an inactive to an active conformation.
ALTnames :
Endoplasmin, Tra1, Hsp90B1, Gp96
Immunogen :
Native chicken Grp94.
Buffer :
Liquid. In PBS, pH 7.2, containing 0.09% sodium azide.
Uses :
Detects a band of ~94kDa by Western blot.
Application Summary :
FC
Storage :
+4°C
company information
Enzo Life Sciences
5777 Hines Drive
Ann Arbor, MI 48108
info-us@enzolifesciences.
https://www.enzolifesciences.com
1-800-942-0430
headquarters: USA
Enzo Life Sciences, incorporating ALEXIS® Biochemicals and BIOMOL® International, offers a comprehensive panel of innovative life science reagents. Antibodies, enzymes, proteins, small molecule inhibitors, product libraries, and assay kits are available for research in Cancer, Cell Death, Epigenetics, Genomics, Immunology, Neuroscience, Signal Transduction, and Ubiquitin & Proteasomes, Enabling Discovery in Life Science(tm). Visit www.enzolifesciences.com.