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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 (Montrer EPHB2 Protéines) and p38 (Montrer CRK Protéines). These results reveal for the first time a crucial role for gp96 in the regulation of ERK (Montrer EPHB2 Protéines) and p38 (Montrer CRK Protéines) 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 (Montrer SLC11A1 Protéines) vaccine.
binding of PCSK9 (Montrer PCSK9 Protéines) to GRP94 protects LDLR (Montrer LDLR Protéines) from degradation likely by preventing early binding of PCSK9 (Montrer PCSK9 Protéines) to LDLR (Montrer LDLR Protéines)
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 (Montrer HSPA5 Protéines), but not GRP94, is required for mammary gland development.
GRP94 deficiency in the liver led to injury, LPC (Montrer PCSK7 Protéines) expansion, increased proliferation, activation of oncogenic signaling, progressive repopulation of GRP94-positive hepatocytes and HCC (Montrer FAM126A Protéines) development in aged mice.
GP96 serves as an essential chaperone for the cell-surface protein (Montrer CD28 Protéines) glycoprotein A repetitions predominant (GARP (Montrer LRRC32 Protéines)), which is a docking receptor for latent membrane-associated TGF-beta (Montrer TGFB1 Protéines) (mLTGF-beta).
Overexpressed miR (Montrer MLXIP Protéines)-150 attenuates hypoxia-induced human cardiomyocyte cell apoptosis by targeting GRP94.
Regulation of CLC-1 (Montrer CLCN1 Protéines) chloride channel (Montrer CLCA1 Protéines) biosynthesis by FKBP8 (Montrer FKBP8 Protéines) and Hsp90beta (Montrer HSP90AB1 Protéines) 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 (Montrer HMGB1 Protéines) 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 (Montrer ATP5B Protéines)/CALR (Montrer CALR Protéines)/HSP90B1/HSPB1 (Montrer HSPB1 Protéines)/HSPD1 (Montrer HSPD1 Protéines)-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.
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 (Montrer TGFBR1 Protéines) and phosphorylated heat shock protein 27 specifically accumulate in the cytoskeleton fraction, and ALK1 (Montrer ACVRL1 Protéines) and ALK5 (Montrer TGFBR1 Protéines) interact with heat shock protein 90(HSP90 (Montrer HSP90 Protéines)).
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