15 kDa selenoprotein (SEP15), Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

>85% (SDS-PAGE) (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of SEP15 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

17,975 Da

selenoprotein F

Selenoprotein F

The protein encoded by this gene belongs to the SEP15/selenoprotein M family. The exact function of this protein is not known; however, it has been found to associate with UDP-glucose:glycoprotein glucosyltransferase (UGTR), an endoplasmic reticulum(ER)-resident protein, which is involved in the quality control of protein folding. The association with UGTR retains this protein in the ER, where it may play a role in protein folding. It has also been suggested to have a role in cancer etiology. This protein is a selenoprotein, containing the rare amino acid selenocysteine (Sec). Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. [provided by RefSeq, Nov 2016]

May be involved in redox reactions associated with the formation of disulfide bonds. May contribute to the quality control of protein folding in the endoplasmic reticulum ().

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