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The protein encoded by HSPB8 belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. Additionally we are shipping Heat Shock 22kDa Protein 8 Antibodies (228) and Heat Shock 22kDa Protein 8 Proteins (26) and many more products for this protein.
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We identified impaired RNA metabolism, secondary to TDP-43 (show TARDBP ELISA Kits) loss of function, as a possible pathological mechanism of HSPB8 toxicity, leading to muscle and nerve degeneration
Data indicated that the HSPB8 expression level was strongly positively correlated with MAPK (show MAPK1 ELISA Kits) signaling pathway and CREB (show CREB1 ELISA Kits) pathway and worse prognosis. The methylation level of its DNA was negatively associated with its expression and positively associated with overall survival. These results suggest that HSPB8 could promote the proliferation and inhibit the apoptosis of GC cells by activating ERKCREB signaling.
HSPB2 (show HSPB2 ELISA Kits) competes with HSPB8 for binding to BAG3 (show BAG3 ELISA Kits). In contrast, HSPB3 (show HSPB3 ELISA Kits) negatively regulates HSPB2 (show HSPB2 ELISA Kits) association with BAG3 (show BAG3 ELISA Kits).
Silencing of HSPB8 markedly decreased the mitotic levels of BAG3 in HeLa cells, supporting its crucial role in BAG3 mitotic functions. The results support a role for the HSPB8-BAG3 chaperone complex in quality control of actin-based structure dynamics that are put under high tension, notably during cell cytokinesis.
HSPB8 is involved in regulating the cell cycle and cell migration in MCF-7 cells.
suggest that HSPB8 may act as an intracellular factor against hepatitis C virus replication and that DNAJC5B has the same function, with more relevant results for genotype 3
It has been demonstrated that HSPB8-BAG3 (show BAG3 ELISA Kits)-HSP70 (show HSP70 ELISA Kits) ensures the functionality of stress granules and restores proteostasis by targeting defective ribosomal products for degradation.
We report that overexpression of HSPB8 in immortalized motor neurones decreased the accumulation of TDP-25 and TDP-35 and that protection against mislocalized/truncated TDP-43 (show TARDBP ELISA Kits) was observed for HSPB8 in Drosophila melanogaster Overexpression of HSP67Bc, the functional ortholog of human HSPB8, suppressed the eye degeneration caused by the cytoplasmic accumulation of a TDP-43 (show TARDBP ELISA Kits) variant
HSPB8 counteracts accumulation of aberrantly localized misfolded forms of TDP-43 (show TARDBP ELISA Kits) and its 25 KDa fragment involved in most sporadic cases of Amyotrophic Lateral Sclerosis and of Fronto Lateral Temporal Dementia.
expands the understanding of disease mechanisms, tissue involvement, and phenotypic outcome of HSPB8 mutations
GA genotype of SNP g.507G>A of HSPB8 gene has a probable role in heat tolerance in Sahiwal cattle.
HSP22 functions as a negative regulator in the TGF-beta (show TGFB1 ELISA Kits)-stimulated migration of osteoblasts.
Results revealed that the apoptosis-suppressing effect of heat shock protein B8 was mediated by the PI3K/Akt (show AKT1 ELISA Kits) pathway in an in vitro model of ischemia.
Increased Hsp20 (show HSPB6 ELISA Kits) expression protects against OGDR-induced Golgi fragmentation and apoptosis, likely through interaction with Bax (show BAX ELISA Kits) and subsequent amelioration of the OGDR-induced elevation in p115 cleavage via the Fas (show FAS ELISA Kits)/FasL (show FASL ELISA Kits) signaling pathway.
Translocation of both Hsp22 and iNOS to the mitochondria is necessary for Hsp22-mediated stimulation of oxidative phosphorylation
analysis of the phenotype of cardiomyopathy in cardiac-specific heat shock protein B8 K141N transgenic mouse
The results of this study strongly suggested that Hspb8 and its alpha-crystallin domain might act as pleiotropic prosurvival factor in the adult hippocampus.
Hspb8 mRNA is constitutively expressed in specific brain structures across ontogeny; eventually these structures could be affected by the malfunction or deregulation of the Hspb8 molecule.
Hsp22 represents a previously undescribed activator of both nuclear and mitochondrial functions of STAT3 (show STAT3 ELISA Kits), and its deletion in the context of pressure overload in vivo accelerates the transition into heart failure and increases mortality.
HspB8 increases misfolded SOD1 (show SOD1 ELISA Kits) clearance via autophagy.
Findings show that despite the ubiquitous presence of HSPB8, only motor neurons appear to be affected by the K141N and K141E mutations.
The protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. The expression of this gene in induced by estrogen in estrogen receptor-positive breast cancer cells, and this protein also functions as a chaperone in association with Bag3, a stimulator of macroautophagy. Thus, this gene appears to be involved in regulation of cell proliferation, apoptosis, and carcinogenesis, and mutations in this gene have been associated with different neuromuscular diseases, including Charcot-Marie-Tooth disease.
E2-induced gene 1 protein
, alpha-crystallin C chain
, heat shock 27kDa protein 8
, heat shock protein beta-8
, protein kinase H11
, small stress protein-like protein HSP22
, heat shock 22kDa protein 8
, H11 kinase
, heat shock 70 kDa protein 8
, heat shock 70kDa protein 8
, heat shock cognate 71 kDa protein
, heat shock cognate 71-kd protein
, crystallin, alpha C
, heat shock protein 20-like protein
, heat shock protein 8