Browse our anti-Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) Antibodies

Rabbit Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) interaction partners

1. 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.

Mouse (Murine) Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) interaction partners

1. this study shows that gp96 activates inflammasome-signaling platforms in antigen-presenting cells

2. 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.

3. GRP94 Knock-out mice exhibits impaired glucose tolerance. GRP94 is an essential regulator of pancreatic beta-cell development, mass, and function.

4. 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.

5. Heat-shock protein gp96 enhances T cell responses and protective potential to BCG vaccine.

6. binding of PCSK9 to GRP94 protects LDLR from degradation likely by preventing early binding of PCSK9 to LDLR

7. mgp96 could be a potential therapeutic target for ER-alpha36-overexpressing breast cancer.

8. These data indicate that macrophage gp96 is essential for protective immunity during Gram-negative pneumonia

9. gp96 participates in the generation of natural Treg cells, which might be involved in the control of liver regeneration in the periphery

10. These studies imply GRP78, but not GRP94, is required for mammary gland development.

11. 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.

12. 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).

13. this work uncovered the essential role of gp96 in regulating melanogenesis.

14. Deletion of CD24 impairs development of heat shock protein gp96-driven autoimmune disease through expansion of myeloid-derived suppressor cells.

15. This study uncovers novel and unique roles of GRP94 in regulating hematopoietic stem cell proliferation.

16. gp96 is an endoplasmic reticulum heat shock protein that serves as a morphogenetic and immunoregulatory factor in syngeneic pregnancy

17. GRP94 is a novel regulator of cell adhesion, liver homeostasis, and tumorigenesis.

18. gp96 is an immune chaperone with a role in macrophage-involved inflammatory colon tumorigenesis

19. Induction of regulatory T cells by high-dose gp96 suppresses murine liver immune hyperactivation.

20. 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.

Human Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) interaction partners

1. data allowed us to determine that Gp96 binds to a complement C3 fragment encompassing amino acids 749-954, a functional complement C3 hot spot important for binding of different regulators

2. GRP94 silencing modulates antineoplastic drug resistance of MG63 and 143B cells by inhibiting the induction of apoptosis.

3. Among infants, an HSP90B1 gene-region variant is associated with BCG-induced IL-2 production and may be associated with protection from TB disease. HSP90B1 knockdown in human monocyte-like cell lines did not influence TLR2 surface localization nor Mtb replication. Together, these data suggest that HSP90B1 regulates T-cell, but not monocyte, responses to mycobacteria in humans.

4. we found that Hsp90beta was positively correlated with vasculogenic mimicry and epithelial-mesenchymal transformation-related proteins in hepatocellular carcinoma

5. Glucose-regulated protein GRP94 contributes to the development of an aggressive phenotype in breast cancer cells.

6. 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.

7. Overexpressed miR-150 attenuates hypoxia-induced human cardiomyocyte cell apoptosis by targeting GRP94.

8. Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90beta as a molecular model for myotonia congenita has been described.

9. 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.

10. HSP-gp96 promotes T cell response, enhances DC antigen presentation and induces cytokine secretion in human gastric cancer cell lines.

11. 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.

12. High GRP94 expression is associated with endometrioid adenocarcinoma.

13. 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.

14. 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.

15. 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.

16. 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.

17. High HSP90B1 expression is associated with non-small-cell lung cancer.

18. data suggest that the GRP94/CCT8/c-Jun/EMT signaling cascade might be a new therapeutic target for HCC

19. We filtered four OSCC genes including SERPINB9, SERPINE2, GAK, and HSP90B1 through the gene global prioritization score (P < 0.005).

20. Our results demonstrated that GRP94 is a key molecule in Hepatocellular carcinoma (HCC) progression that modulates the AKT pathway and eNOS levels

Pig (Porcine) Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) interaction partners

1. 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]

2. These results identify a compact, intertwined quaternary conformation of native GRP94

Cow (Bovine) Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) interaction partners

1. 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).

Xenopus laevis Heat Shock Protein 90kDa beta (Grp94), Member 1 (HSP90B1) interaction partners

1. In Xenopus, gp96 can prime CD8(+) T-cell effectors that are not MHC restricted.