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SEPP1 encodes a selenoprotein containing multiple selenocysteine (Sec) residues, which are encoded by the UGA codon that normally signals translation termination.
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preliminary result indicated the beneficial effect of serine on the expression of SelP and GPx (显示 GPX1 抗体), which suggested that it might be a candidate for combined selenium supplement.
Genetic variations in selenoprotein genes modulated both GPX1 and SELENOP selenoprotein gene expression and global gene expression in response to Brazil nut supplementation.
SeP was higher in individuals who were overweight/obese, and associated with insulin resistance by HOMA-IR and by clamp, but not independently of BMI.
We have demonstrated a significant decrease in circulating SeP (显示 PLXNB1 抗体) levels according to MetS (显示 ETV3 抗体) status in patients with documented cardiovascular disease.
Results indicate a diversity of RNA elements conducting multiple occurrences of UGA redefinition to control the synthesis of full-length and truncated selenoprotein P (SELENOP) isoforms.
Study suggests the 3' UTR (显示 UTS2R 抗体) structural elements (SECIS) in Sepp1 functions with site specificity and further illustrates how mRNA processing may produce transcripts with altered coding potential to produce diversity in selenoprotein isoforms.
Inc (显示 PLXNB1 抗体)reased amounts of circulating SeP predicted the ineffectiveness of training on endurance capacity in humans.
Results indicate that the 2 genetic variants of rs7579 and rs230813 in SEPP1 may not play a role in the pathogenesis of preeclampsia in Chinese Han Women.
erum microRNA-7 and selenoprotein P appear to be potential non-invasive diagnostic markers for hepatocellular carcinoma. Moreover, the results suggest that selenium could be used as an anticancer therapy for hepatocellular carcinoma by affecting both microRNA-7 and selenoprotein P
The selenium levels in the tissues were correlated to the genotype of the SELENOP selenium carrier protein, but not to other proteins whose levels have been reported to be responsive to selenium availability, including GPX1 (显示 GPX1 抗体), SELENOF and SBP1 (显示 MEGF8 抗体).
SeP (显示 EPHX2 抗体) causes exercise resistance through its muscle receptor low-density lipoprotein receptor-related protein 1 (LRP1 (显示 LRP1 抗体)). SeP (显示 EPHX2 抗体)-deficient mice showed a 'super-endurance' phenotype after exercise training, as well as enhanced reactive oxygen species production, AMPK (显示 PRKAA1 抗体) phosphorylation and Ppargc-1alpha expression in skeletal muscle.
Through correlational analysis, it was determined that the effects of Se-supplement were closely related to SelP expression, inflammatory cytokines, and apoptosis molecule production.
This study showed that Male mice lacking two key genes involved in Se metabolism (Scly (显示 SCLY 抗体)(-/-)Sepp1(-/-) mice), selenoprotein P (Sepp1) and Sec lyase (Scly (显示 SCLY 抗体)), develop severe neurological dysfunction, neurodegeneration, and audiogenic seizures.
Results indicate that selenoprotein P (Sepp1) is important for this transport in selenium-replete mice but that glutathione peroxidase-3 (Gpx3 (显示 GPX3 抗体)) is not.
Sepp1 haploinsufficiency or mutations that disrupt either the selenium transport or the enzymatic domain of SEPP1 exhibit increased colitis-associated carcinogenesis via increased genomic instability and promotion of a protumorigenic microenvironment
plasma Sepp1(UF) and small selenium-containing proteins are filtered by the glomerulus and taken up by PCT (显示 UROD 抗体) cells via megalin (显示 LRP2 抗体)-mediated endocytosis.
Tandem Sepp1-apoER2 (显示 LRP8 抗体) interactions supply selenium for maintenance of brain neurons both at the blood-brain barrier and within the brain. Sepp1 inside the blood-brain barrier is taken up by neurons via apoER2 (显示 LRP8 抗体), concentrating brain selenium in them.
These findings provide the first in vivo evidence that Scly (显示 SCLY 抗体) and Sepp1 work cooperatively to maintain selenoprotein function in the mammalian brain.
This gene encodes a selenoprotein containing multiple selenocysteine (Sec) residues, which are 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), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This selenoprotein is an extracellular glycoprotein, and is unusual in that it contains 10 Sec residues per polypeptide. It is a heparin-binding protein that appears to be associated with endothelial cells, and has been implicated to function as an antioxidant in the extracellular space. Several transcript variants, encoding either the same or different isoform, have been found for this gene.
, membrane metallo-endopeptidase-like 2
, neprilysin II
, soluble secreted endopeptidase
, zinc metallopeptidase
, selenoprotein P
, plasma selenoprotein P
, selenoprotein P-like protein