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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 (162) and Heat Shock 105kDa/110kDa Protein 1 Kits (3) and many more products for this protein.
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Human HSPH1 Protein expressed in HEK-293 Cells - ABIN2722568
Berthenet, Boudesco, Collura, Svrcek, Richaud, Hammann, Causse, Yousfi, Wanherdrick, Duplomb, Duval, Garrido, Jego: Extracellular HSP110 skews macrophage polarization in colorectal cancer. in Oncoimmunology 2016
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]
Established heat shock protein 110 (HSP110) as a prognostic biomarker of colorectal carcinomas (CRCs) with microsatellite instability-high (MSI (show MSI1 Proteins)-H) by considering the intratumoral heterogeneity of HSP110 expression. The HSP110wt-low MSI (show MSI1 Proteins)-H CRCs were significantly correlated with larger deletions in the HSP110 T17 mononucleotide repeat (>/=4 bp; p < 0.001).
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 Proteins) and induces HIF-1a (show HIF1A Proteins) accumulation in CoCl2-treated cells.
the expression of HSP110 in colon cancer contributes to STAT3 (show STAT3 Proteins)-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 Proteins) degradation complex, favoring the hyperphosphorylation and degradation of beta-catenin (show CTNNB1 Proteins).
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 Proteins)) to BAG1 (show BAG1 Proteins), BAG2 (show BAG2 Proteins), BAG3 (show BAG3 Proteins), and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 (show BAG3 Proteins) > BAG1 (show BAG1 Proteins) > Hsp105 >> BAG2 (show BAG2 Proteins).
HSPH1 and HSPH2 are bona fide chaperones on their own that collaborate with DNAJA1 (show DNAJA1 Proteins) and DNAJB1 (show DNAJB1 Proteins) to hydrolyze ATP and unfold polypeptides and HSPA1A (show HSPA1A Proteins) and HSPH1 formed a powerful molecular machinery.
These observations suggest that GGA administration is a therapeutic candidate for depressive diseases by increasing hippocampal BDNF (show BDNF Proteins) levels via HSP105 expression.
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 Proteins), release of cytochrome c (show CYCS Proteins) and caspase (show CASP3 Proteins) 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 Proteins) to mitochondria
HSP105 appears to chaperone the responses to endoplasmic reticulum (ER) stress through its interactions with GRP78 (show HSPA5 Proteins) and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3 (show CASP3 Proteins)-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 Proteins).
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