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A construct encoding NH2-terminally 6xHis-tagged human selenoprotein P (SEPP1) was expressed in the E.coli cells. The resulting protein is the recombinant full-length of mature SEPP1 protein containing amino acid sequence 20-381 of mouse SEPP1. The purity of this SEPP1 protein is greater than 90% determined by SDS-PAGE. A molecular mass band range from 40 kDa was presented on the SDS-PAGE gel under reducing conditions. In-stock SEPP1 proteins are offered now. In addition to being used to immunize animals for specific antibody synthesis, this recombinant SEPP1 protein may also find use int he studies of selenium-metabolism or SEPP1-related diseases. SEPP1 is a major selenium-containing protein in human plasma and is primarily expressed in the liver and secreted into the extracellular fluid. As a selenium-transporter, SEPP1 sustains antioxidative selenoenzymes in several tissues such as the brain and testis and plays an important role in selenium-metabolism and antioxidative defense. The reduction of SEPP1 and other selenoproteins leads to various dysfunctions associated with oxidative stress. Recent studies have shown that overexpressed SEPP1 exacerbates glucose metabolism and promotes type II diabetes.
A construct encoding NH2-terminally 6xHis-tagged human selenoprotein P (SEPP1) was expressed in the E.coli cells. The resulting protein is the recombinant full-length of mature SEPP1 protein containing amino acid sequence 20-381 of mouse SEPP1. The purity of this SEPP1 protein is greater than 90% determined by SDS-PAGE. A molecular mass band range from 40 kDa was presented on the SDS-PAGE gel under reducing conditions. In-stock SEPP1 proteins are offered now. In addition to being used to immunize animals for specific antibody synthesis, this recombinant SEPP1 protein may also find use int he studies of selenium-metabolism or SEPP1-related diseases.
SEPP1 is a major selenium-containing protein in human plasma and is primarily expressed in the liver and secreted into the extracellular fluid. As a selenium-transporter, SEPP1 sustains antioxidative selenoenzymes in several tissues such as the brain and testis and plays an important role in selenium-metabolism and antioxidative defense. The reduction of SEPP1 and other selenoproteins leads to various dysfunctions associated with oxidative stress. Recent studies have shown that overexpressed SEPP1 exacerbates glucose metabolism and promotes type II diabetes.
| Cat.No | ACP02548 | Target Name | SELENOP |
|---|---|---|---|
| Target Synonyms | Selenoprotein P; Selenoprotein P plasma 1; Selp; SeP; Sepp1; SEPP1_HUMAN | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 20-381aa(U59S, U300S, U318S, U330S, U345S, U352S, U367S, U369S, U376S, U378S) |
| Mol Weight | 44.6kDa | Protein Length | Full Length of Mature Protein |
| Purity | Greater than 90% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P49908 |
|---|
Uniprot Id
P49908
Target Species
Human
Target Name
SELENOP
Target Full Name
Selenoprotein P
Target Function
Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis.
Target Subcellular Location
Secreted.
Target Protein Families
Selenoprotein P family
Target Tissue Specificity
Made in the liver and heart and secreted into the plasma. It is also found in the kidney.
Target Research Area
Others
Target Synonyms
Selenoprotein P; Selenoprotein P plasma 1; Selp; SeP; Sepp1; SEPP1_HUMAN
Target Background
This gene encodes a selenoprotein that is predominantly expressed in the liver and secreted into the plasma. This selenoprotein is unique in that it contains multiple selenocysteine (Sec) residues per polypeptide (10 in human), and accounts for most of the selenium in plasma. It has been implicated as an extracellular antioxidant, and in the transport of selenium to extra-hepatic tissues via apolipoprotein E receptor-2 (apoER2). Mice lacking this gene exhibit neurological dysfunction, suggesting its importance in normal brain function. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. The mRNA for this selenoprotein contains two SECIS elements. The use of alternative polyadenylation sites, one located in between the two SECIS elements, results in two populations of mRNAs containing either both (predominant) or just the upstream SECIS element (PMID:27881738). Alternatively spliced transcript variants have also been found for this gene.
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