Recombinant Human Selenoprotein P (SELENOP) Protein (His)

Name: Recombinant Human Selenoprotein P (SELENOP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03296P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Selenoprotein P (SELENOP) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P49908
Target Symbol	SELENOP
Synonyms	Selenoprotein P; Selenoprotein P plasma 1; Selp; SeP; Sepp1; SEPP1_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	ESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQASSYLCILQASKLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQEENQTDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGNCSLTTLKDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAPNAPTHPAPPGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLPTDSELAPRSSCCHCRHLIFEKTGSAITSQCKENLPSLCSSQGLRAEENITESCQSRLPPAASQISQQLIPTEASASSRSKNQAKKSESPSN
Expression Range	20-381aa(U59S,U300S,U318S,U330S,U345S,U352S,U367S,U369S,U376S,U378S)
Protein Length	Full Length of Mature Protein
Mol. Weight	44.6kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

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.
Subcellular Location	Secreted.
Protein Families	Selenoprotein P family
Database References	HGNC: 10751 OMIM: 601484 KEGG: hsa:6414 STRING: 9606.ENSP00000420939 UniGene: Hs.275775
Tissue Specificity	Made in the liver and heart and secreted into the plasma. It is also found in the kidney.

Gene Functions References

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
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
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
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
We have demonstrated a significant decrease in circulating SeP levels according to MetS status in patients with documented cardiovascular disease. PMID: 28190280
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
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
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
Increased amounts of circulating SeP predicted the ineffectiveness of training on endurance capacity in humans. PMID: 28263310
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
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
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
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
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
Selenoprotein P concentrations are not elevated in women with gestational diabetes mellitus but are associated with BMI and HDL cholesterol. PMID: 26514640
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
Impaired renal function is positively correlated with serum concentrations of SePP. PMID: 26348725
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
this study provide preliminary genetic evidence that the SEPP1 functional variants contribute to the AAA risk. PMID: 25395084
Elevated SeP concentrations are independently associated with a reduced risk of MetS in children PMID: 24638201
These results demonstrate that SEPP1 represents a previously unrecognized regulator of Polychlorinated biphenyl-induced biological effects. PMID: 23770201
Selenium, selenoenzymes, oxidative stress and risk of neoplastic progression from Barrett's esophagus: results from biomarkers and genetic variants. PMID: 22715394
These results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A). PMID: 24914767
data suggest that SEPP1 alters breast cancer risk among women with higher levels of NA ancestry PMID: 24278290
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
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
SEPP1 rs7579 was found to be associated with lower risk of advanced prostate cancer. PMID: 24563517
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
The data provide evidence that single nucleotide polymorphisms in SEPP1 and GPX1 modulate risk of breast cancer. PMID: 24039907
SePP is not only involved in Selenium transport to testes supporting GPX4 biosynthesis but it also becomes secreted into seminal plasma. PMID: 24361887
metformin decreases binding of FoxO3a, a direct target of AMPK, to the SEPP1 promoter. PMID: 24257750
Sepp1 secreted from epithelial cells may support the intestinal immune system by providing immune cells (including plasma cells) with selenium PMID: 24157689
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
Genetic variants in selenoprotein P plasma 1 gene (SEPP1) are associated with fasting insulin and first phase insulin response in Hispanics PMID: 24161883
SEPP1 genetic variation was associated with prostate cancer incidence; replication of these results in an independent dataset is necessary. PMID: 23129481
Higher tumor grade and tumor stage at diagnosis correlated to lower SePP and Se concentrations. PMID: 23056383
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
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
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
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
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
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
tear SeP is a key molecule to protect the ocular surface cells against environmental oxidative stress PMID: 20360971
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
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
These findings suggest an association between the individual selenoprotein concentration and the presence of diabetes. PMID: 20875901
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
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
A DNA-repeat structure within the promoter contains a functionally relevant polymorphism and is genetically unstable under conditions of mismatch repair deficiency PMID: 12173025
selenoprotein P functions as a Se-supply protein, delivering Se to the cells PMID: 12423375

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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