GRP94 Antibody: HRP

Biorbyt

GRP94 antibody

16

0.5 microg/ml of SMC-105 was sufficient for detection of Grp94 in 20 microg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody.

Western Blot, ELISA, ImmunoHistoChemistry

WB (1:2000), ICC/IF (1:100) ELISA, IHC, WB

Research Use Only

Monoclonal

9G10

1 mg/ml

HRP

HSP90B1

heat shock protein 90 beta family member 1

94 kDa glucose-regulated protein; ECGP; endoplasmin; endothelial cell (HBMEC) glycoprotein; epididymis luminal protein 35; epididymis secretory sperm binding protein Li 125m; GP96; GRP94; heat shock protein 90 kDa beta member 1; heat shock protein 90kDa beta (Grp94), member 1; heat shock protein 90kDa beta family member 1; HEL35; HEL-S-125m; stress-inducible tumor rejection antigen gp96; TRA1; tumor rejection antigen (gp96) 1; tumor rejection antigen 1

Rat

IgG2a

Endoplasmin

Rat monoclonal to GRP94 (HRP). 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..

Amphibian, Bovine, Canine, Chicken, Equine, Guinea Pig, Hamster, Human, Monkey, Mouse, Porcine, Rabbit, Rat, Sheep

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