gp96/HSP90B1/GRP94 Antibody

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, possess 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 lucose 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. 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 inding site for the Hsp90 inhibitors geldanamycin and radicicol. However, the molecular basis for adenosine nucleotide-dependent regulation of Grp94remains to be established. Recent data has entified 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).

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Showing Publications 1 - 2 of 2.

Publications using NBP1-81803	Applications	Species
Ito A, Mimae T, Yamamoto YS et al. Novel application for pseudopodia proteomics using excimer laser ablation and two-dimensional difference gel electrophoresis. Lab Invest 2012-09-01 [PMID: 22751350]
Cawthorn TR, Moreno JC, Dharsee M et al. Proteomic Analyses Reveal High Expression of Decorin and Endoplasmin (HSP90B1) Are Associated with Breast Cancer Metastasis and Decreased Survival. PLoS One 2012-01-01 [PMID: 22363530]

Images	Ratings	Applications	Species	Date	Details
Enlarge	5 reviewed by: Takayuki Marutani	WB	Human	09/06/2017	View Summary Application Western Blot Sample Tested Neutrophilic cells whole cell lysate Species Human Lot A114214

Array NBP1-81803

• gp96/HSP90B1/GRP94 Antibodies
• gp96/HSP90B1/GRP94 ELISA Kits
• gp96/HSP90B1/GRP94 Lysate
• gp96/HSP90B1/GRP94 Proteins