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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 and p38. These results reveal for the first time a crucial role for gp96 in the regulation of ERK and p38 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 vaccine.
binding of PCSK9 to GRP94 protects LDLR from degradation likely by preventing early binding of PCSK9 to LDLR
mgp96 could be a potential therapeutic target for ER-alpha36-overexpressing breast cancer.
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, but not GRP94, is required for mammary gland development.
GRP94 deficiency in the liver led to injury, LPC expansion, increased proliferation, activation of oncogenic signaling, progressive repopulation of GRP94-positive hepatocytes and HCC development in aged mice.
GP96 serves as an essential chaperone for the cell-surface protein glycoprotein A repetitions predominant (GARP), which is a docking receptor for latent membrane-associated TGF-beta (mLTGF-beta).
this work uncovered the essential role of gp96 in regulating melanogenesis.
Deletion of CD24 impairs development of heat shock protein gp96-driven autoimmune disease through expansion of myeloid-derived suppressor cells.
This study uncovers novel and unique roles of GRP94 in regulating hematopoietic stem cell proliferation.
gp96 is an endoplasmic reticulum heat shock protein that serves as a morphogenetic and immunoregulatory factor in syngeneic pregnancy
GRP94 is a novel regulator of cell adhesion, liver homeostasis, and tumorigenesis.
gp96 is an immune chaperone with a role in macrophage-involved inflammatory colon tumorigenesis
Induction of regulatory T cells by high-dose gp96 suppresses murine liver immune hyperactivation.
gp96 is the major interaction partner of YFAK copolymer in RAW264.7 cells, confirmed by analysis of gp96-deficient cell lines and primary antigen-presenting cells.
Data indicate that the dimerization of integrin alphaL and beta2 is highly dependent on gp96.
Glucose-regulated protein GRP94 contributes to the development of an aggressive phenotype in breast cancer cells.
Concomitant high expression of ERalpha36, GRP78 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-150 attenuates hypoxia-induced human cardiomyocyte cell apoptosis by targeting GRP94.
Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90beta 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 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/CALR/HSP90B1/HSPB1/HSPD1-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/c-Jun/EMT signaling cascade might be a new therapeutic target for HCC
We filtered four OSCC genes including SERPINB9, SERPINE2, GAK, and HSP90B1 through the gene global prioritization score (P < 0.005).
Our results demonstrated that GRP94 is a key molecule in Hepatocellular carcinoma (HCC) progression that modulates the AKT pathway and eNOS levels
Results indicate that FN14 and GRP94 are prediction/prognosis markers which open up new possibilities for preventing/treating brain metastasis in breast cancer patients.
This study clarifies a Grp94-mediated ERAD pathway for GABAA receptors, which provides a novel way to finely tune their function in physiological and pathophysiological conditions.
GRP94 knockdown cells are defective in intracellular transport and, consequently, negatively impact the trafficking of F-actin toward the cellular cortex, integrin alpha2 and integrin alphaL toward the cell membrane and filopodia
Our results indicate that GRP94 and TRAP1 might contribute more to the carcinogenesis or biology of SCLC than HSP90alpha and HSP90beta
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 and phosphorylated heat shock protein 27 specifically accumulate in the cytoskeleton fraction, and ALK1 and ALK5 interact with heat shock protein 90(HSP90).
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