Recombinant Human Selenoprotein P (SEPP1) (U59S,U300S,U318S,U330S,U345S,U352S,U367S,U369S,U376S,U378S)

In Stock
Code CSB-EP021018HU
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
Selenoprotein P; Selenoprotein P plasma 1; Selp; SeP; Sepp1; SEPP1_HUMAN
Homo sapiens (Human)
Expression Region
20-381aa(U59S, U300S, U318S, U330S, U345S, U352S, U367S, U369S, U376S, U378S)
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Tris-based buffer,50% glycerol
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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.

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I am interested in your product RPC20084 - Recombinant Human Selenoprotein P (SEPP1).
I am slightly confused by the sequence given on the web page for this protein, as it does not indicate where in the sequence the Selenocysteine units are located; the location in which I expect to see U is denoted with a S. Could you provide the sequence for this product, indicating where the Selenocysteine units lie and how many it contains?

Thanks for your inquiry. This is a in-stock recombinant protein. The product details are confirmed as below.
Code: CSB-EP021018HU
You can view the original sequence on this page.
The original sequence does contain many selenocysteine (U) (10 selenocysteine), and the "U" selenocysteine is encoded by UGA and is normally used as a stop codon in prokaryotic cells, leading to premature
termination of translation. We generally will mutate this selenocysteine. In terms of the formation of selenocysteine, selenocysteine is actually a derivative of serine.
Selenocysteine and cysteine and serine have high similarity. The selenocysteine can be regarded as either cysteine S replaced by Se, or serine O replaced by Se, so mutation to serine and cysteine are both feasible.
In general, we usually mutate it to serine in terms of protein expression (because mutating to cysteine may create additional disulfide bonds that affect protein expression and structure).
The above provided sequences have all replaced "U" with "S". For U in the corresponding position of the original sequence (ie full-length protein), we all mutated to S.

For the purpose of our testing we want to use Se as a marker.
Is it possible to get this protein without the mutation so that the selenocysteine is still present, preferably as a powder?
If so do you have a rough guide on the cost?

Thanks for your response. I'm sorry but we can't provide this protein with Se existing, as we have explained in the last email that Se will lead to premature termination of translation.
We could provide this protein in Lyophilized Powder.

Would you be able to share the concentration of CSB-EP021018HU - Recombinant Human Selenoprotein P(SEPP1)?

Very nice to receive your inquiry. CSB-EP021018HU
We have 12mg inventory of lyophilized powder. If it can pass quality control, then the lead time will be 5-7 working days. As the inventory protein is lyophilized powder, we could satisfy concentration 0.1-1mg/ml.
If it can't pass QC, then the lead time will be 15-20 working days, then the protein concentration will be determined during the experiment process.
If customer has special requirement for protein concentration, please consult with us and remark in your PO.
Note: For Selenium generation of cysteine (U), the Translation code is U, which is Termination codon and can lead to early termination. So we will mutate the selenium generation of cysteine into serine (Ser), and provide the serine mutant.

Target Background

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.
Gene References into Functions
  1. When rs13154178 gene polymorphism was compared with AA homozygous individuals, fasting blood glucose levels were significantly higher in carriers of either polymorphism than in those with no polymorphism. We suggest rs13154178 gene polymorphism may lead to gestational diabetes mellitus in the Turkish society. PMID: 29648467
  2. preliminary result indicated the beneficial effect of serine on the expression of SelP and GPx, which suggested that it might be a candidate for combined selenium supplement. PMID: 26944060
  3. Genetic variations in selenoprotein genes modulated both GPX1 and SELENOP selenoprotein gene expression and global gene expression in response to Brazil nut supplementation. PMID: 28696394
  4. 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. PMID: 27524654
  5. We have demonstrated a significant decrease in circulating SeP levels according to MetS status in patients with documented cardiovascular disease. PMID: 28190280
  6. 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. PMID: 29069514
  7. Biomarkers of Se status in clinical research need to be measured by validated assays in order to avoid erroneous data and incorrect interpretations, especially when analyzing young women. The Se content of circulating SELENOP differs between individuals and may provide some important diagnostic information on Se metabolism and status PMID: 28064116
  8. Study suggests the 3' UTR 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. PMID: 27881738
  9. Increased amounts of circulating SeP predicted the ineffectiveness of training on endurance capacity in humans. PMID: 28263310
  10. 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. PMID: 28700468
  11. 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 PMID: 28459371
  12. 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, SELENOF and SBP1. PMID: 27908419
  13. GPX1 and SEPP1 Single Nucleotide Polymorphism were not associated with any changes in the expression of related genes. GPX1 was shown to modulate the expression of unrelated target, SEP15, upon Se supplementation, both alone and in combination with SEPP1. PMID: 26658762
  14. Data show that the cell proliferative ability was inhibited in the cells overexpressing selenoprotein P, plasma 1 (SEPP1), and the colony forming ability of The cell evidently decreased. PMID: 27371843
  15. Selenoprotein P concentrations are not elevated in women with gestational diabetes mellitus but are associated with BMI and HDL cholesterol. PMID: 26514640
  16. Studied gene-specific regulation of hepatic selenoprotein expression by interleukin-6; by testing human hepatocytes in culture, found IL-6 reduced the concentrations of SePP mRNA and secreted SePP in a dose-dependent manner. PMID: 26399395
  17. Impaired renal function is positively correlated with serum concentrations of SePP. PMID: 26348725
  18. women who carry the SEPP1 rs3877899 A allele are better able to maintain selenium status during pregnancy, and their GPx3 activity increases more with supplementation, which suggests better protection from low selenium status. PMID: 26675765
  19. this study provide preliminary genetic evidence that the SEPP1 functional variants contribute to the AAA risk. PMID: 25395084
  20. Elevated SeP concentrations are independently associated with a reduced risk of MetS in children PMID: 24638201
  21. These results demonstrate that SEPP1 represents a previously unrecognized regulator of Polychlorinated biphenyl-induced biological effects. PMID: 23770201
  22. Selenium, selenoenzymes, oxidative stress and risk of neoplastic progression from Barrett's esophagus: results from biomarkers and genetic variants. PMID: 22715394
  23. These results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A). PMID: 24914767
  24. data suggest that SEPP1 alters breast cancer risk among women with higher levels of NA ancestry PMID: 24278290
  25. The histidine-rich domain of selenoprotein P is capable of binding Cu ions in both oxidation states of Cu(+) and Cu(2+) with high affinity and of modulating Cu(+) and Cu(2+)-mediated ABETA aggregation, reactive oxygen species production, neurotoxicity. PMID: 24437729
  26. Data suggest that plasma SEPP1 level can be up-regulated by dietary factors; here, significantly higher plasma SEPP1 is observed in women at risk of pre-eclampsia treated with dietary supplement of selenium-enriched yeast started in first trimester. PMID: 24708917
  27. SEPP1 rs7579 was found to be associated with lower risk of advanced prostate cancer. PMID: 24563517
  28. This study demonistrated that Sepp1 in midbrain was expressed in neurons of the substantia nigra (SN), and expression was concentrated within the centers of Lewy bodies, the pathological hallmark of Parkinson disease PMID: 23268326
  29. The data provide evidence that single nucleotide polymorphisms in SEPP1 and GPX1 modulate risk of breast cancer. PMID: 24039907
  30. SePP is not only involved in Selenium transport to testes supporting GPX4 biosynthesis but it also becomes secreted into seminal plasma. PMID: 24361887
  31. metformin decreases binding of FoxO3a, a direct target of AMPK, to the SEPP1 promoter. PMID: 24257750
  32. Sepp1 secreted from epithelial cells may support the intestinal immune system by providing immune cells (including plasma cells) with selenium PMID: 24157689
  33. We speculate that there could be a feedback regulation between hepatic Sepp1 and pancreatic insulin and that increased circulating Sepp1 might be the result rather than the cause of abnormal glucose metabolism.[Review] PMID: 23760059
  34. Genetic variants in selenoprotein P plasma 1 gene (SEPP1) are associated with fasting insulin and first phase insulin response in Hispanics PMID: 24161883
  35. SEPP1 genetic variation was associated with prostate cancer incidence; replication of these results in an independent dataset is necessary. PMID: 23129481
  36. Higher tumor grade and tumor stage at diagnosis correlated to lower SePP and Se concentrations. PMID: 23056383
  37. hepatocellular SAM-dependent protein methylation is required for both SEPP1 and gluconeogenic enzyme expression and that inhibition of protein arginine methylation might provide a route to therapeutic interventions in type II diabetes. PMID: 22932905
  38. Circulating selenoprotein P levels were positively correlated with fasting plasma glucose and negatively associated with both total and high-molecular adiponectin in type 2 diabetics. PMID: 22496878
  39. Circulating SeP concentrations were elevated in patients with glucose metabolism dysregulation and were related to various cardiometabolic parameters including insulin resistance, inflammation, and atherosclerosis. PMID: 21677040
  40. The glucocorticoid receptor inhibits selenoprotein P transactivation via response elements; the finding provides insight into a potential mechanism of selenium redistribution during development. PMID: 19513589
  41. Selenoprotein P levels in prostate cells determine basal reactive-oxygen-species levels and H2O2-induced cytotoxicity. Deregulation of selenoprotein P during prostate carcinogenesis may increase free radicals, thus promoting tumor development. PMID: 21456065
  42. Using serial analysis of gene expression and DNA chip methods, the study found that hepatic SeP mRNA levels correlated with insulin resistance in humans. PMID: 21035759
  43. tear SeP is a key molecule to protect the ocular surface cells against environmental oxidative stress PMID: 20360971
  44. Inflammation of the intestinal mucosa causes a decline in locally produced selenoprotein P in the colon that eventually may contribute to the emergence of inflammatory bowel disease-related colorectal cancer. PMID: 20542496
  45. The present results show no significant difference in genotype and allele distribution of SNP r25191g/a between individuals with Kashin-Beck disease and controls. PMID: 20565998
  46. These findings suggest an association between the individual selenoprotein concentration and the presence of diabetes. PMID: 20875901
  47. Our findings demonstrate that Selenoprotein P protects neuronal cells from amyloid beta-induced toxicity, suggesting a neuroprotective role for SelP in preventing neurodegenerative disorders. PMID: 20521393
  48. Early decrease in Sel-P plasma concentrations was specifically observed in septic shock and was similar in SIRS patients whereas GPx activity remained unchanged. PMID: 19779296
  49. A DNA-repeat structure within the promoter contains a functionally relevant polymorphism and is genetically unstable under conditions of mismatch repair deficiency PMID: 12173025
  50. selenoprotein P functions as a Se-supply protein, delivering Se to the cells PMID: 12423375

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Subcellular Location
Protein Families
Selenoprotein P family
Tissue Specificity
Made in the liver and heart and secreted into the plasma. It is also found in the kidney.
Database Links

HGNC: 10751

OMIM: 601484

KEGG: hsa:6414

STRING: 9606.ENSP00000420939

UniGene: Hs.275775

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