Selenoprotein P (SEPP1) Recombinant Protein | SEPP1 recombinant protein

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

Cat. Num. AAA1065524

• Gene Names: SEPP1; SeP; SELP; SEPP
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Selenoprotein P (SEPP1); Recombinant Human Selenoprotein P (SEPP1) (U59S; U300S; U318S; U330S; U345S; U352S; U367S; U369S; U376S; U378S); SEPP1 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 20-381aa (U59S,U300S,U318S,U330S,U345S,U352S,U367S,U369S,U376S,U378S) ;Full Length of Mature Protein
• Sequence: ESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQASSYLCILQASKLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQEENQTDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGNCSLTTLKDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAPNAPTHPAPPGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLPTDSELAPRSSCCHCRHLIFEKTGSAITSQCKENLPSLCSSQGLRAEENITESCQSRLPPAASQISQQLIPTEASASSRSKNQAKKSESPSN

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to support@mybiosource.com for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Sequence

(There are 10 selenocysteine (U) in the original sequence. The amino acids at multiple sites are ‘U’ in UniProt (yellow highlighted; U59S, U300S, U318S, U330S, U345S, U352S, U367S, U369S, U376S, U378S), reference:: https://www.uniprot.org/uniprot/P49908 ). The ‘U’ at each yellow highlighted site has been mutated to ‘S’ to manufacture the MBS1065524 Recombinant Human Selenoprotein P. 'U' selenocysteine is encoded by UGA and it is normally used as a stop codon in prokaryotic cells, which will lead to early termination of translation, hence the lab mutates this selenocysteine for protein manufacturing. In terms of the formation of selenocysteine, selenocysteine is actually a derivative of serine. Selenocysteine and cysteine as well as serine are all highly similar. This selenocysteine can be regarded as either the 'S' of cysteine replaced by Se, or the 'O' of serine replaced by Se. The selenocysteine can mutated to be either serine or cysteine.Generally, the lab mutates 'U' to serine for protein expression because mutating the 'U' to cysteine may result in the formation of additional disulfide bonds, potentially affecting the expression and structure of the protein.)

SDS-Page

Related Product Information for SEPP1 recombinant protein

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.

References

Conserved nucleotide sequences in the open reading frame and 3' untranslated region of selenoprotein P mRNA.Hill K.E., Lloyd R.S., Burk R.F.Proc. Natl. Acad. Sci. U.S.A. 90:537-541(1993) Hill K.E.NIEHS SNPs programThe DNA sequence and comparative analysis of human chromosome 5.Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.Nature 431:268-274(2004) Purification of selenoprotein P from human plasma.Aakesson B., Bellew T., Burk R.F.Biochim. Biophys. Acta 1204:243-249(1994) A novel method for the purification of selenoprotein P from human plasma.Mostert V., Lombeck I., Abel J.Arch. Biochem. Biophys. 357:326-330(1998) Selenoprotein P properties, functions, and regulation.Mostert V.Arch. Biochem. Biophys. 376:433-438(2000) Selenoprotein P. A selenium-rich extracellular glycoprotein.Burk R.F., Hill K.E.J. Nutr. 124:1891-1897(1994) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) A strategy for precise and large scale identification of core fucosylated glycoproteins.Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.Mol. Cell. Proteomics 8:913-923(2009) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)

NCBI and Uniprot Product Information

• NCBI GI #: 148277018
• NCBI GeneID: 6414
• NCBI Accession #: NP_001078955.1
• NCBI GenBank Nucleotide #: NM_001085486.1
• UniProt Accession #: P49908; Q6PD59; Q6PI43; Q6PI87; Q6PJF9
• Molecular Weight: 42.6 kDa
• NCBI Official Full Name: selenoprotein P isoform 1
• NCBI Official Synonym Full Names: selenoprotein P, plasma, 1
• NCBI Official Symbol: SEPP1
• NCBI Official Synonym Symbols: SeP; SELP; SEPP
• NCBI Protein Information: selenoprotein P
• UniProt Protein Name: Selenoprotein P
• Protein Family: Selenoprotein
• UniProt Gene Name: SEPP1
• UniProt Synonym Gene Names: SELP; SeP
• UniProt Entry Name: SEPP1_HUMAN

NCBI Description

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. [provided by RefSeq, Jul 2008]

Uniprot Description

SEPP1: 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. Belongs to the selenoprotein P family.

Protein type: Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 5q31

Cellular Component: extracellular region; extracellular space

Molecular Function: selenium binding

Biological Process: brain development; growth; locomotory behavior; post-embryonic development; response to oxidative stress; selenium metabolic process; sexual reproduction