Application Note: Anti-Grp94 Antibody is tested for WB, IF, IP, and Flow cytometry. Expect a band approximately 98kDa protein corresponding to the molecular mass of Grp94 on SDS PAGE immunoblots. This monoclonal antibody reacts with purified Grp94. Specific conditions for reactivity should be optimized by the end user.
Clone ID: 9G10
Concentration Value: 1mg/mL
Flow Cytometry Dilution: User Optimized
Immunoprecipitation Dilution: User Optimized
Western Blot Dilution: 0.5µg/ml
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Immunogen: Grp94 Antibody was produced in rat by repeated immunizations with purified Grp94 isolated from chicken oviducts.
Physical State: Liquid (sterile filtered)
Purity and Specificity: Anti-GRP94 Antibody was purified by Protein G chromatography. A BLAST analysis was used to suggest cross-reactivity with GRP94 from Human, Mouse, Rat, Bovine, Canine, Chicken, Guinea pig, Hamster, Horse, Monkey, Pig, Rabbit, Sheep, Xenopus sources based on 100% homology with the immunizing sequence. Does not detect human Hsp90, Grp74, or GrpE from E.coli. Cross-reactivity with GRP94 from other sources has not been determined. Heat Shock research.
Background: Grp94 (glucose regulated protein 94, gp96) 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. Grp94 also plays a role in antigen presentation by accessing the endogenous pathway and eliciting specific CTL responses to chaperone bound peptides via MHC class I pathway Grp94 is a member of the Hsp90 family of stress proteins and shares sequence homology with its cytosolic equivalent, Hsp90. Both Hsp90 and Grp94 are calcium binding proteins. 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. 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. Grp94 contains a carboxy terminal KDEL (Lys-Asp-Glu-Leu) sequence which is believed to aid in its retention in the ER
Low Endotoxin: No
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