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Selenoprotein P Proteins (SEPP1)

SEPP1 encodes a selenoprotein containing multiple selenocysteine (Sec) residues, which are encoded by the UGA codon that normally signals translation termination. Additionally we are shipping Selenoprotein P Antibodies (39) and Selenoprotein P Kits (12) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
SEPP1 6414 P49908
SEPP1 20363 P70274
SEPP1 29360 P25236
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Top Selenoprotein P Proteins at antibodies-online.com

Showing 8 out of 9 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Human His tag 50 μg Log in to see 21 to 26 Days
$341.00
Details
HOST_Escherichia coli (E. coli) Cow GST tag 50 μg Log in to see 21 to 26 Days
$341.00
Details
Yeast Human His tag 50 μg Log in to see 31 to 36 Days
$341.00
Details
Yeast Rat His tag   1 mg Log in to see 56 to 66 Days
$3,001.17
Details
Yeast Cow His tag   1 mg Log in to see 56 to 66 Days
$3,054.33
Details
HOST_Escherichia coli (E. coli) Human Un-conjugated   50 μg Log in to see 16 to 21 Days
$314.29
Details

SEPP1 Proteins by Origin and Source

Origin Expressed in Conjugate
Human ,

Mouse (Murine)

Rat (Rattus)

More Proteins for Selenoprotein P (SEPP1) Interaction Partners

Human Selenoprotein P (SEPP1) interaction partners

  1. Selenoprotein P concentrations are not elevated in women with gestational diabetes mellitus but are associated with BMI and HDL (show HSD11B1 Proteins) cholesterol.

  2. Studied gene-specific regulation of hepatic selenoprotein expression by interleukin-6 (show IL6 Proteins); by testing human hepatocytes in culture, found IL-6 (show IL6 Proteins) reduced the concentrations of SePP mRNA and secreted SePP in a dose-dependent manner.

  3. women who carry the SEPP1 rs3877899 A allele are better able to maintain selenium status during pregnancy, and their GPx3 (show GPX3 Proteins) activity increases more with supplementation, which suggests better protection from low selenium status.

  4. this study provide preliminary genetic evidence that the SEPP1 functional variants contribute to the AAA (show APP Proteins) risk.

  5. Elevated SeP concentrations are independently associated with a reduced risk of MetS in children

  6. These results demonstrate that SEPP1 represents a previously unrecognized regulator of Polychlorinated biphenyl-induced biological effects.

  7. These results demonstrated that SelP interacts with tubulin (show TUBB Proteins), alpha 1a (TUBA1A (show Tuba1a Proteins)).

  8. data suggest that SEPP1 alters breast cancer risk among women with higher levels of NA ancestry

  9. 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 (show APP Proteins) aggregation, reactive oxygen species production, neurotoxicity.

  10. 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.

Mouse (Murine) Selenoprotein P (SEPP1) interaction partners

  1. This study showed that Male mice lacking two key genes involved in Se metabolism (Scly (show SCLY Proteins)(-/-)Sepp1(-/-) mice), selenoprotein P (Sepp1) and Sec lyase (Scly (show SCLY Proteins)), develop severe neurological dysfunction, neurodegeneration, and audiogenic seizures.

  2. Results indicate that selenoprotein P (Sepp1) is important for this transport in selenium-replete mice but that glutathione peroxidase-3 (Gpx3 (show GPX3 Proteins)) is not.

  3. 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

  4. plasma Sepp1(UF) and small selenium-containing proteins are filtered by the glomerulus and taken up by PCT (show UROD Proteins) cells via megalin (show LRP2 Proteins)-mediated endocytosis.

  5. Tandem Sepp1-apoER2 (show LRP8 Proteins) 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 (show LRP8 Proteins), concentrating brain selenium in them.

  6. These findings provide the first in vivo evidence that Scly (show SCLY Proteins) and Sepp1 work cooperatively to maintain selenoprotein function in the mammalian brain.

  7. longer isoforms of Sepp1 with high selenium content interact with a binding site distinct from the ligand-binding domain of apoER2 (show LRP8 Proteins) for selenium delivery

  8. metformin decreases binding of FoxO3a (show FOXO3 Proteins), a direct target of AMPK (show PRKAA1 Proteins), to the SEPP1 promoter.

  9. Data indicate that uptake of Sepp1 and Gpx3 (show GPX3 Proteins) by d-13 visceral yolk sac (show ADCY10 Proteins) was independent of apoER2 (show LRP8 Proteins) and megalin (show LRP2 Proteins).

  10. 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

Selenoprotein P (SEPP1) Protein Profile

Protein Summary

This gene encodes a selenoprotein containing multiple selenocysteine (Sec) residues, which are 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), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This selenoprotein is an extracellular glycoprotein, and is unusual in that it contains 10 Sec residues per polypeptide. It is a heparin-binding protein that appears to be associated with endothelial cells, and has been implicated to function as an antioxidant in the extracellular space. Several transcript variants, encoding either the same or different isoform, have been found for this gene.

Gene names and symbols associated with Selenoprotein P Proteins (SEPP1)

  • selenoprotein P, plasma, 1 (SEPP1)
  • selenoprotein P, plasma, 1 (sepp1)
  • selenoprotein P (SEPP1)
  • selenoprotein P (SeP)
  • selenoprotein P, plasma, 1 (Sepp1)
  • AU018766 protein
  • D15Ucla1 protein
  • DKFZp459B039 protein
  • MGC88974 protein
  • Se-P protein
  • selp protein
  • SeP protein
  • SEPP1 protein

Protein level used designations for Selenoprotein P Proteins (SEPP1)

selenoprotein P , plasma selenoprotein P , seP , selenoprotein P-like protein

GENE ID SPECIES
431587 Gallus gallus
448755 Xenopus (Silurana) tropicalis
461897 Pan troglodytes
479346 Canis lupus familiaris
698917 Macaca mulatta
100037964 Sus scrofa
100052968 Equus caballus
100174535 Pongo abelii
100329002 Saccoglossus kowalevskii
6414 Homo sapiens
20363 Mus musculus
282066 Bos taurus
29360 Rattus norvegicus
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