Anti-GRP94 (C-terminal) antibody produced in rabbit

synthetic peptide corresponding to amino acids 733-750 located near the C-terminus of human GRP94. This sequence is identical in mouse, rat, dog, porcine, and bovine GRP94 and highly conserved (1 amino acid substitutuion) in chicken.

Anti-GRP94 (C-terminal) antibody produced in rabbit has been used in immunocytochemistry.

Anti-GRP94 (C-terminal) antibody produced in rabbit is suitable for immunoblotting at a working concentration of 0.5-1μg/mL using whole cell extracts of the human epitheloid carcinoma HeLa cells, Madin Darby canine kidney (MDCK) cells, and mouse fibroblast NIH3T3 cells. It is also suitable for immunoprecipitation of GRP94 protein from a MDCK whole cell lysate at 10-20μg concentration.

GRP94 (glucose-regulated protein 94) is involved in protein folding, sorting and secretion, and binding of immunogenic peptides. GRP94 has a role in peptide antigen presentation to major histocompatibility complex class I molecules of antigen presenting cells (APCs). It binds specifically to CD91 (α2-macroglobulin receptor), and possibly to the Toll-like receptors (TLRs) on the surface of APCs. Overexpression of GRP94 has been associated with cellular transformation and tumorigenesis.

GRPs are unresponsive to heat stress and are induced by stress related to glucose starvation or defects in glycoprotein processing, depletion of Ca²⁺ stores, acidosis, and hypoxia conditions that are also common in poorly vascularized tumor tissues.

The GRP94 (glucose-regulated protein 94) is a 94 kDa Ca²⁺- binding glycoprotein that belongs to a subfamily of the heat shock proteins Hsp90. It is a chaperone protein constitutively localized to the endoplasmic reticulum (ER) of mammalian cells.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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