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GRP94 is tightly associated with the cell surface of parietal cells from rabbit gastric mucosa, where it exhibits high-affinity binding for the adenosine receptor agonist NECA and specific inhibitor radicicol.
These data demonstrate the essential role of the gp96-TLR interaction in priming T cell immunity and provide further molecular basis for the coupling of gp96-mediated innate with adaptive immunity.
Heat-shock protein gp96 enhances T cell responses and protective potential to BCG (show SLC11A1 Proteins) vaccine.
binding of PCSK9 (show PCSK9 Proteins) to GRP94 protects LDLR (show LDLR Proteins) from degradation likely by preventing early binding of PCSK9 (show PCSK9 Proteins) to LDLR (show LDLR Proteins)
These data indicate that macrophage gp96 is essential for protective immunity during Gram-negative pneumonia
gp96 participates in the generation of natural Treg cells, which might be involved in the control of liver regeneration in the periphery
These studies imply GRP78 (show HSPA5 Proteins), but not GRP94, is required for mammary gland development.
GRP94 deficiency in the liver led to injury, LPC (show PCSK7 Proteins) expansion, increased proliferation, activation of oncogenic signaling, progressive repopulation of GRP94-positive hepatocytes and HCC (show FAM126A Proteins) development in aged mice.
GP96 serves as an essential chaperone for the cell-surface protein (show CD28 Proteins) glycoprotein A repetitions predominant (GARP (show LRRC32 Proteins)), which is a docking receptor for latent membrane-associated TGF-beta (show TGFB1 Proteins) (mLTGF-beta).
this work uncovered the essential role of gp96 in regulating melanogenesis.
Deletion of CD24 (show CD24 Proteins) impairs development of heat shock protein gp96-driven autoimmune disease through expansion of myeloid-derived suppressor cells.
High GRP94 expression is associated with endometrioid adenocarcinoma.
Immuno-stimulating peptide derived from HMGB1 (show HMGB1 Proteins) is more effective than the N-terminal domain of Gp96 as an endogenous adjuvant for improvement of protein vaccines.
mutations in GRP94 that affect its IGF chaperone activity represent a novel causal genetic mechanism that limits IGF biosynthesis, quite a distinct mechanism from the known genes in the GH/IGF signaling network.
In this instance, the ATP5B (show ATP5B Proteins)/CALR (show CALR Proteins)/HSP90B1/HSPB1 (show HSPB1 Proteins)/HSPD1 (show HSPD1 Proteins)-signaling network was revealed as the predominant target which was associated with the majority of the observed protein-protein interactions. As a result, the identified targets may be useful in explaining the anticancer mechanisms of ursolic acid and as potential targets for colorectal cancer therapy.
High HSP90B1 expression is associated with non-small-cell lung cancer.
data suggest that the GRP94/CCT8 (show CCT8 Proteins)/c-Jun (show JUN Proteins)/EMT (show ITK Proteins) signaling cascade might be a new therapeutic target for HCC (show FAM126A Proteins)
We filtered four OSCC genes including SERPINB9 (show SERPINB9 Proteins), SERPINE2 (show SERPINE2 Proteins), GAK (show GAK Proteins), and HSP90B1 through the gene global prioritization score (P < 0.005).
Our results demonstrated that GRP94 is a key molecule in Hepatocellular carcinoma (HCC (show FAM126A Proteins)) progression that modulates the AKT (show AKT1 Proteins) pathway and eNOS (show NOS3 Proteins) levels
Results indicate that FN14 (show TNFRSF12A Proteins) and GRP94 are prediction/prognosis markers which open up new possibilities for preventing/treating brain metastasis in breast cancer patients.
structural maturation of the client protein substrate, rather than ATP binding or hydrolysis, serves as the primary signal for dissociation of GRP94-client protein complexes [GRP94]
These results identify a compact, intertwined quaternary conformation of native GRP94
This study showed that ubiquitinated ALK5 (show TGFBR1 Proteins) and phosphorylated heat shock protein 27 specifically accumulate in the cytoskeleton fraction, and ALK1 (show ACVRL1 Proteins) and ALK5 (show TGFBR1 Proteins) interact with heat shock protein 90(HSP90 (show HSP90 Proteins)).
In Xenopus, gp96 can prime CD8(+) T-cell effectors that are not MHC restricted.
This gene encodes a member of a family of adenosine triphosphate(ATP)-metabolizing molecular chaperones with roles in stabilizing and folding other proteins. The encoded protein is localized to melanosomes and the endoplasmic reticulum. Expression of this protein is associated with a variety of pathogenic states, including tumor formation. There is a microRNA gene located within the 5' exon of this gene. There are pseudogenes for this gene on chromosomes 1 and 15.
tumor rejection antigen (gp96) 1
, 94 kD glucose-regulated protein
, endoplasmin-like protein
, 94 kDa glucose-regulated protein
, endoplasmic reticulum resident protein 99
, heat shock protein 90 kDa beta member 1
, polymorphic tumor rejection antigen 1
, transforming growth factor alpha regulated gene 2
, tumor rejection antigen gp96
, heat shock protein 90kDa beta (grp94), member 1
, heat shock protein 90kDa beta (Grp94), member 1
, endothelial cell (HBMEC) glycoprotein
, stress-inducible tumor rejection antigen gp96
, tumor rejection antigen 1
, 98 kDa protein kinase
, PPK 98
, gp96 homolog
, heat shock protein 90kDa beta, member 1
, heat shock protein gp96
, HSP 108
, heat shock 108 kDa protein
, heat shock protein 108
, transferrin-binding protein