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SEP15 encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. Additionally we are shipping 15 KDa Selenoprotein Proteins (6) and many more products for this protein.
Showing 5 out of 6 products:
Cow (Bovine) Polyclonal SEP15 Primary Antibody for WB - ABIN2783300
Jablonska, Gromadzinska, Sobala, Reszka, Wasowicz: Lung cancer risk associated with selenium status is modified in smoking individuals by Sep15 polymorphism. in European journal of nutrition 2008
Human Polyclonal SEP15 Primary Antibody for ELISA, WB - ABIN564057
Miniard, Middleton, Budiman, Gerber, Driscoll: Nucleolin binds to a subset of selenoprotein mRNAs and regulates their expression. in Nucleic acids research 2010
Genotype variation within the 3'-UTR (show UTS2R Antibodies) of the SEP 15 gene showed no association with breast cancer risk or clinico-pathological parameters in Caucasian women.
Results suggest that SEP15 plays important roles in the regulation of the G1 phase during the cell cycle as well as in cell motility of Chang liver cells offering a novel functional link between the cell cycle and cell motility.
Sep15 in Chang liver cells regulates the pathway that antagonizes RhoA/ROCK/MLC-dependent non-apoptotic bleb formation.
This study provides evidence that SEP15 genetic variation may influence prostate cancer mortality
SEP15, encoding a 15-kDa selenium-containing protein was shown to be downregulated in approximately 60% of MM cell lines and tumor specimens. A SEP15 polymorphic variant, 1125A, resides in the SECIS recognition element
It appears that those with the Sep15 1125 AA genotype may benefit most from a higher Se intake, whereas in those with the GG or GA genotype, a higher Se status may increase the risk for lung cancer.
Studies in mouse show that Sep15 may have redox function.
Considering the variable expression levels of Sep15 and TR1 (show TXNRD1 Antibodies) found within the human population, our results provide insights into new roles of selenoproteins in cancer
Cataracts resulted from an improper folding status of lens proteins caused by Sep15 deficiency.
These data suggest tissue specificity in the cancer-protective effects of Sep15 downregulation, which are mediated, at least in part, by influencing the cell cycle.
Transfecting Sep15 gene did not influence the growth characteristics of BEL (show LHX2 Antibodies)-7402 cell line and Sep15 may have redox function.
The cysteine-rich domain of Sep15 exclusively mediates protein-protein interactions with UDP-glucose:glycoprotein glucosyltransferase (show UGGT1 Antibodies).
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 in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein folding. This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
, 15 kDa selenoprotein
, 15-kDa selenoprotein