Recombinant Mouse Selenoprotein P (Selenop)

Code CSB-YP021018MO
MSDS
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Source Yeast
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Code CSB-EP021018MO
MSDS
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Source E.coli
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Code CSB-EP021018MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP021018MO
MSDS
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Source Baculovirus
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Code CSB-MP021018MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Selenop
Uniprot No.
Alternative Names
Selenop; Selp; Sepp1; Selenoprotein P; SeP; Plasma selenoprotein P
Species
Mus musculus (Mouse)
Expression Region
20-380
Target Protein Sequence
E SQGQSSACYK APEWYIGDQN PMLNSEGKVT VVALLQASUY LCLLQASRLE DLRIKLESQG YFNISYIVVN HQGSPSQLKH SHLKKQVSEH IAVYRQEEDG IDVWTLLNGN KDDFLIYDRC GRLVYHLGLP YSFLTFPYVE EAIKIAYCEE RCGNCNLTSL EDEDFCKTVT SATANKTAEP SEAHSHHKHH NKHGQEHLGS SKPSENQQPG PSETTLPPSG LHHHHRHRGQ HRQGHLESUD TTASEGLHLS LAQRKLURRG CINQLLCKLS KESEAAPSSC CCHCRHLIFE KSGSAIAUQC AENLPSLCSU QGLFAEEKVT ESCQCRSPPA AUQNQPMNPM EANPNUSUDN QTRKUKUHSN
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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.
Gene References into Functions
  1. In this study, the role of SeP in ischemia/reperfusion (I/R) injury has been investigated. PMID: 29547524
  2. 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
  3. 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
  4. SeP causes exercise resistance through its muscle receptor low-density lipoprotein receptor-related protein 1 (LRP1). SeP-deficient mice showed a 'super-endurance' phenotype after exercise training, as well as enhanced reactive oxygen species production, AMPK phosphorylation and Ppargc-1alpha expression in skeletal muscle. PMID: 28263310
  5. Through correlational analysis, it was determined that the effects of Se-supplement were closely related to SelP expression, inflammatory cytokines, and apoptosis molecule production. PMID: 27334433
  6. This study showed that Male mice lacking two key genes involved in Se metabolism (Scly(-/-)Sepp1(-/-) mice), selenoprotein P (Sepp1) and Sec lyase (Scly), develop severe neurological dysfunction, neurodegeneration, and audiogenic seizures. PMID: 26586820
  7. Results indicate that selenoprotein P (Sepp1) is important for this transport in selenium-replete mice but that glutathione peroxidase-3 (Gpx3) is not. PMID: 25068390
  8. 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 PMID: 26053663
  9. data highlight SePP as the essential Se transporter to bones, and suggest a novel feedback mechanism for preferential uptake of Se in Se-deprived bones PMID: 24626785
  10. plasma Sepp1(UF) and small selenium-containing proteins are filtered by the glomerulus and taken up by PCT cells via megalin-mediated endocytosis. PMID: 24434121
  11. Tandem Sepp1-apoER2 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, concentrating brain selenium in them. PMID: 24760755
  12. These findings provide the first in vivo evidence that Scly and Sepp1 work cooperatively to maintain selenoprotein function in the mammalian brain. PMID: 24519931
  13. longer isoforms of Sepp1 with high selenium content interact with a binding site distinct from the ligand-binding domain of apoER2 for selenium delivery PMID: 24532792
  14. metformin decreases binding of FoxO3a, a direct target of AMPK, to the SEPP1 promoter. PMID: 24257750
  15. Data indicate that uptake of Sepp1 and Gpx3 by d-13 visceral yolk sac was independent of apoER2 and megalin. PMID: 23651543
  16. results emphasize the importance of non-coding transcript variations as a regulatory means for Sepp1 expression in different tissues and stages of development; presence of a variant localized in the hippocampus and regulated by a microRNA may have implications for deficits in synaptic function caused by genetic deletion of Sepp1 PMID: 23064117
  17. study shows that pancreatic islets express relatively high levels of Sepp1 that may fulfill a function in antioxidant protection of beta-cells. Downregulation of Sepp1 expression by high glucose might thus contribute to glucotoxicity in beta-cells PMID: 23125459
  18. Sepp1(-/-) mice have impairments in fear extinction, latent inhibition, and sensorimotor gating, showing the important supporting role of Sepp1 on ApoER2-expressing parvalbumin interneurons. PMID: 22640876
  19. Sepp1 production by hepatocytes retains selenium in the organism and distributes it from the liver to peripheral tissues. PMID: 23038251
  20. the neurological phenotype caused by the absence of Sepp1 is exacerbated in male vs. female mice. PMID: 22487427
  21. apoER2-mediated uptake of long isoform Sepp1 is responsible for selenium distribution to tissues throughout the body. PMID: 22761431
  22. Deletion of Sepp1 (and presumably selenium deficiency in the brain) produce both neuronal and axonal degeneration as well as more moderate and potentially reversible neurite changes in the developing brain. PMID: 21636077
  23. Both genetic deletion and RNA interference-mediated knockdown of selenoprotein P improved systemic insulin sensitivity and glucose tolerance in mice. PMID: 21035759
  24. investigation of role of Sepp1 expression in adipocytes during adipogenesis and oxidative stress in models of obesity and insulin resistance PMID: 20959537
  25. Selenoprotein biosynthesis becomes redirected in hepatocytes during the acute-phase response at the expense of dispensable selenoproteins (e.g., SepP) and in favor of SepS expression, thereby causing declining serum selenium and improving liver function. PMID: 20370716
  26. Se-P from liver provides selenium to several tissues, especially testis and brain PMID: 12574155
  27. Selenoprotein P is required for development of functional spermatozoa and is an essential component of the selenium delivery pathway for developing germ cells. PMID: 15744015
  28. Brainstem axonal degeneration was found in mice with deletion of Sepp1. PMID: 16105800
  29. absence of selenoprotein P synthesis in the liver makes more selenium available for urinary metabolite synthesis, increasing loss of selenium from the organism and causing the decrease in whole-body selenium PMID: 17014962
  30. C terminus of Sepp1 is critical for the maintenance of selenium in brain and testis but not for the maintenance of whole body selenium PMID: 17311913
  31. Sepp1 is more important for maintaining selenium in the hippocampus than in other brain regions. PMID: 17311961
  32. Sertoli cell ApoER2 is a Sepp1 receptor and a component of the selenium delivery pathway to spermatogenic cells PMID: 17314095
  33. Thus, age represents another important modifier of the dynamic sex- and tissue-specific selenoprotein expression patterns. PMID: 17937617
  34. local Sepp expression is required to maintain selenium content in selenium-privileged tissues such as brain and testis during dietary selenium restriction PMID: 17961124
  35. Neurodegeneration in mice resulting from loss of functional selenoprotein P. PMID: 18172410
  36. kidney selenium homeostasis is mediated by a megalin-dependent Sepp1 uptake pathway in the proximal tubule PMID: 18174160
  37. Alternatively activated myeloid cells limit pathogenicity associated with African trypanosomiasis through the IL-10 inducible gene selenoprotein P. PMID: 18424738
  38. Spatiotemporal expression of the Se-P gene in postimplantational mouse embryos is reported. PMID: 18956332
  39. Data suggest that hepatic translation of Sepp1 mRNA is specifically impaired during the acute-phase response. PMID: 19136613

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Subcellular Location
Secreted.
Protein Families
Selenoprotein P family
Tissue Specificity
In the kidney, expressed in the cortex with no expression observed in the medulla (at protein level). Expressed by the liver and secreted in plasma.
Database Links
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