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Cow (Bovine) Polyclonal SELS Primary Antibody für WB - ABIN2783218
Moses, Johnson, Tømmerdal, Forsmo, Curran, Abraham, Charlesworth, Brennecke, Blangero, Austgulen: Genetic association of preeclampsia to the inflammatory response gene SEPS1. in American journal of obstetrics and gynecology 2008
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Human Polyclonal SELS Primary Antibody für ICC, IF - ABIN4352486
Bubenik, Miniard, Driscoll: Alternative transcripts and 3'UTR elements govern the incorporation of selenocysteine into selenoprotein S. in PLoS ONE 2013
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Human Polyclonal SELS Primary Antibody für IP, WB - ABIN527713
Huang, Hsiao, Chu, Ye, Chen: Derlin2 protein facilitates HRD1-mediated retro-translocation of sonic hedgehog at the endoplasmic reticulum. in The Journal of biological chemistry 2013
In these studies found that SelS increases in negative correlation with tau phosphorylation in brain.
The results suggest that SelS is required for C99 degradation through endoplasmic reticulum-associated degradation, resulting in inhibition of amyloid beta production.
regulating liver and serum Selenoprotein S levels might become a new strategy for the prevention and treatment of DM and its macrovascular complications
SEPS1 may be a potential gene marker for disease diagnosis and prognosis.
interaction between SelK and p97(VCP) is SelS-dependent, and the resulting ERAD complex (SelS-p97(VCP)-SelK) plays an important role in ERAD and ER stress
Potential roles of the SEPS1 gene in the pathogenesis and etiology of Hashimoto's thyroiditis.
SNP rs4965814 of SELS may affect the susceptibility to ischemic stroke.
The SEPS1 -105G>A is associated with an increased risk of Kashin-Beck disease and influences the expression of PI3K/Akt signaling pathway in Kashin-Beck disease patients
Although VIMP can interact with CLIMP-63 and Syn5L, it does not interact with MT-binding ER proteins (such as Reep1) that shape the tubular smooth ER
Selenoprotein S is a marker but not a regulator of endoplasmic reticulum stress in intestinal epithelial cells in inflammatory bowel diseases.
Pro(178) and Pro(183) of SelS play important roles in the translocation of p97(VCP) to the ER membrane and protect cells from ER stress
that SEPS1 may protect mice against LPS-induced sepsis and organ damage. Therefore, SEPS1 may be a new target to resolve LPS-induced sepsis.
Existence of a link between SEPS1 promoter genetic variation and Hashimoto thyroiditis risk.
Findings suggest that the SEPS1 G-105A polymorphism contributes to the risk of developing SPTB in a Chinese population.
Our results indicated that the rs12910524 in the Tanis gene was associated with triglyceride concentrations in subjects without diabetes in China.
Data suggest that selenocysteine allows selenoprotein S (SelS, VIMP) to sustain activity under oxidative stress.
These results suggest a potential role for the SELS region in the development subclinical cardiovascular disease in this sample enriched for type 2 diabetes mellitus.
the redox properties observed for recombinant VIMP are compatible with a function as a reductase
Upregulation of SelS expression in reactive astrocytes reveals a new protective role for SelS against inflammation and endoplasmic reticulum stress that can be relevant to astrocyte function.
a role for SELS in the development of metabolic disease, especially in the context of insulin resistance.
These results suggest that VIMP may function as a novel regulator to modulate beta-cell survival, proliferation, cell cycle, unfolded protein response and insulin secretion in MIN6 cells. VIMP knockdown (KD) decreases cell proliferation and G1 cell cycle arrest.
It has been proposed that SelS promoted cell survival through the IRE1a-XBP1 signaling pathway.
findings suggest that SelS protects endothelial cells against TNF-alpha-induced dysfunction by inhibiting the activation of p38 MAPK and NF-kappaB pathways and implicates it as a possible modulator of vascular inflammatory diseases.
the genetic reduction of Seps1 appears to specifically exacerbate the inflammatory profile of fast-twitch muscle fibres, which are typically more vulnerable to degeneration in dystrophy.
SelS expression is prominent in neurons and hardly detectable in astrocytes from control mice
The SEPS1 protein expression in liver of septic mouse is markedly elevated.
Selenoprotein biosynthesis becomes redirected in hepatocytes during the acute-phase response at the expense of dispensable selenoproteins (e.g., SepP) and in favor of SepS expression, thereby causing declining serum selenium and improving liver function.
These findings suggest that SEPS1 could be a new ER stress-dependent survival factor that protects macrophage against ER stress-induced cellular dysfunction.
We found that suppression of SEPS1 by small interfering RNA severely increases astrocyte injure caused by OGD, suggesting that selenoprotein S protects astrocytes against ischemia.
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies suggest that this protein may regulate cytokine production, and thus play a key role in the control of the inflammatory response. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
, histocompatibility 47
, minor histocompatibility antigen H47