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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.
Study demonstrated that the lack of gp96 in both the human monocytic cell line MM6 and in macrophages from LysMcre-gp96 floxed mice neither leads to a complete loss of TLR 2 expression nor to a complete loss of TLR-induced signaling, but is associated with an impaired phosphorylation of ERK (show EPHB2 Proteins) and p38 (show CRK Proteins). These results reveal for the first time a crucial role for gp96 in the regulation of ERK (show EPHB2 Proteins) and p38 (show CRK Proteins) kinases.
GRP94 Knock-out mice exhibits impaired glucose tolerance. GRP94 is an essential regulator of pancreatic beta-cell development, mass, and function.
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).
Glucose-regulated protein GRP94 contributes to the development of an aggressive phenotype in breast cancer cells.
Concomitant high expression of ERalpha36, GRP78 (show HSPA5 Proteins) and GRP94 is associated with aggressive papillary thyroid cancer behavior and may be used as a predictor for extrathyroid extension, lymph node metastasis, and distant metastasis.
Overexpressed miR (show MLXIP Proteins)-150 attenuates hypoxia-induced human cardiomyocyte cell apoptosis by targeting GRP94.
Regulation of CLC-1 (show CLCN1 Proteins) chloride channel (show CLCA1 Proteins) biosynthesis by FKBP8 (show FKBP8 Proteins) and Hsp90beta (show HSP90AB1 Proteins) as a molecular model for myotonia congenita has been described.
HSP-gp96 promotes T cell response, enhances DC antigen presentation and induces cytokine secretion in human gastric cancer cell lines.
our results besides adding further evidence in support of Grp94 as the shared tumor antigen in tumors of the GI tract, prove that it can be measured in plasma as valuable diagnostic marker of disease in the form of complexes with IgG that also exert immune-modulating activities on circulating immune 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.
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