Recombinant Human GRP94 protein is a Human Full Length protein, in the 22 to 803 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, WB.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes ab87144 can be used as a WB positive control in conjunction with Anti-GRP94 antibody ab13509. |
Select an associated product type
Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).
GRP94, HSPC4, TRA1, HSP90B1, Endoplasmin, 94 kDa glucose-regulated protein, Heat shock protein 90 kDa beta member 1, Heat shock protein family C member 4, Tumor rejection antigen 1, gp96 homolog, GRP-94
Recombinant Human GRP94 protein is a Human Full Length protein, in the 22 to 803 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, WB.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0292% EDTA, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab87144 was purified using conventional chromatography
Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).
Belongs to the heat shock protein 90 family.
GRP94 also known as HSP90b1 is a glycoprotein that belongs to the heat shock protein 90 family. It has a molecular mass of approximately 94 kDa. GRP94 is expressed mainly in the endoplasmic reticulum and appears in high levels in cells undergoing stress. This protein acts as a chaperone assisting in the proper folding and assembly of other proteins playing an essential role in protein homeostasis. GRP94 ensures the quality control of proteins by preventing misfolding and aggregation.
GRP94 influences the stability of many secretory and cell-surface proteins. It forms part of a multi-protein complex that stabilizes client proteins and assists their proper folding. GRP94 is essential for the maturation of proteins involved in the immune response including immunoglobulins and integrins. Overexpression of GRP94 has been noted in various cancers where it supports the folding of proteins required for tumor growth and survival.
GRP94 is an important element of the protein folding quality control mechanism within the endoplasmic reticulum. It functions in coordination with other chaperones like BiP and calnexin within the unfolded protein response (UPR) pathway. The UPR pathway is essential during stress conditions where increased protein synthesis occurs. GRP94 also contributes to calcium homeostasis and directly interacts with proteins like integrins affecting cell adhesion and motility.
GRP94 has been implicated in the progression of cancer and neurodegenerative diseases. Overexpression of GRP94 is often linked to cancer where it stabilizes oncogenic proteins necessary for cancer cell survival. In neurodegenerative disorders GRP94 shows altered expression levels which may influence the pathogenesis of diseases like Alzheimer's. The interaction between GRP94 and other proteins such as tau protein in Alzheimer's highlights its potential role in disease mechanisms.
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15% SDS-PAGE showing ab87144 (3ug) at 94.4 kDa
All lanes: Western blot - Anti-GRP94 antibody (Anti-GRP94 antibody ab13509) at 2 µg/mL
All lanes: Western blot - Recombinant Human GRP94 protein (ab87144) at 0.01 µg
All lanes: Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (Goat Anti-Rabbit IgG H&L (HRP) preadsorbed ab97080) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 92 kDa
Exposure time: 150s
All lanes: Western blot - Anti-GRP94 antibody (Anti-GRP94 antibody ab13509) at 2 µg/mL
All lanes: Western blot - Recombinant Human GRP94 protein (ab87144) at 0.01 µg
All lanes: Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (Goat Anti-Rabbit IgG H&L (HRP) preadsorbed ab97080) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 92 kDa
Exposure time: 150s
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