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Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Additionally we are shipping Heat Shock 105kDa/110kDa Protein 1 Antibodies (153) and Heat Shock 105kDa/110kDa Protein 1 Proteins (13) and many more products for this protein.
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These studies demonstrate that Xenopus hsp110 gene expression is constitutive and stress inducible in cultured cells and developmentally- and tissue specifically-regulated during early embryogenesis[hsp110]
HSP110 HT17 alone correctly classified samples judged to be uncertain with the pentaplex panel.
deletion of the HSP110 T17 repeat was frequently observed in microsatellite-unstable advanced gastric cancers.
Hsp105alpha localizes to the nucleus, interacts with HIF-1alpha (show HIF1A ELISA Kits) and induces HIF-1a (show HIF1A ELISA Kits) accumulation in CoCl2-treated cells.
the expression of HSP110 in colon cancer contributes to STAT3 (show STAT3 ELISA Kits)-dependent tumor growth
About 25% of patients with stages II-III colorectal tumors with microsatellite instability have an excellent response to chemotherapy, due to large, biallelic deletions in the T(17) intron repeat of HSP110 in tumor DNA.
HSP105 depletion disrupts the integration of protein phosphatase 2A into the beta-catenin (show CTNNB1 ELISA Kits) degradation complex, favoring the hyperphosphorylation and degradation of beta-catenin (show CTNNB1 ELISA Kits).
A receiver operating characteristic curve constructed with HSP105 and TIM gave a sensitivity of 54.3% and 95% (38/40) specificity in discriminating esophageal squamous cell carcinoma from matched controls.
we measured the binding of human Hsp72 (HSPA1A (show HSPA1A ELISA Kits)) to BAG1 (show BAG1 ELISA Kits), BAG2 (show BAG2 ELISA Kits), BAG3 (show BAG3 ELISA Kits), and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 (show BAG3 ELISA Kits) > BAG1 (show BAG1 ELISA Kits) > Hsp105 >> BAG2 (show BAG2 ELISA Kits).
HSPH1 and HSPH2 are bona fide chaperones on their own that collaborate with DNAJA1 (show DNAJA1 ELISA Kits) and DNAJB1 (show DNAJB1 ELISA Kits) to hydrolyze ATP and unfold polypeptides and HSPA1A (show HSPA1A ELISA Kits) and HSPH1 formed a powerful molecular machinery.
High HSP105 expression is associated with Barrett's esophagus.
Hsp105 may play an important role in the refolding of denatured proteins and protection against stress-induced cell death in mammalian cells.
Hsp110 over-expression increases the immunogenicity of the murine CT26 colon tumor.
Data suggest that Hsp105 has opposite effects on stress-induced apoptosis depending on the cell type; a pro-apoptotic effect in embryonal cells and an anti-apoptotic effect in neuronal cells.
enhances activation of p38 (show CRK ELISA Kits), release of cytochrome c (show CYCS ELISA Kits) and caspase (show CASP3 ELISA Kits) activation; may play important roles in organogenesis, during which marked apoptosis occurs, by enhancing apoptosis during mouse embryogenesis
Hsp105alpha is suggested to regulate the substrate binding cycle of Hsp70/Hsc70 by inhibiting the ATPase activity of Hsp70/Hsc70, thereby functioning as a negative regulator of the Hsp70/Hsc70 chaperone system.
The constitutive overexpression of HSP105 in cancer cells is involved in malignant transformation by protecting tumor cells from apoptosis.
it is suggested that Hsp105 suppresses the stress-induced apoptosis at its initial step, the translocation of Bax (show BAX ELISA Kits) to mitochondria
HSP105 appears to chaperone the responses to endoplasmic reticulum (ER) stress through its interactions with GRP78 (show HSPA5 ELISA Kits) and GSK3 (show GSK3b ELISA Kits), and without HSP105 cell death following ER stress proceeds by a non-caspase-3 (show CASP3 ELISA Kits)-dependent process.
hsp110/105 KO mice are resistant to ischemic injury and that the protective effects of hsp110/105 deficiency in cerebral ischemia may partly be mediated by an increase in the chaperone activity of Hsp70 (show HSP70 ELISA Kits).
Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity).
heat shock 105kD
, heat shock protein 105
, heat shock 105kDa/110kDa protein 1b
, heat shock 105kDa/110kDa protein 1
, heat shock protein 105 kDa-like
, heat shock 105kDa
, heat shock 110 kDa protein
, heat shock protein 105 kDa
, antigen NY-CO-25
, heat shock 105kD alpha
, heat shock 105kD beta
, heat shock 105kDa protein 1
, 42 degrees C-HSP
, HSP105 42 C-HSP
, heat shock protein 110
, heat shock protein, 105 kDa
, heat shock-related 100 kDa protein E7I
, heat shock 105kDa/110kDa protein 1a