Mitochondrial FAD-linked sulfhydryl oxidase ERV1 (ERV1), Saccharomyces cerevisiae, recombinant

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). Source: Yeast. Expression Region: 1-189aa. Protein Length: Full Length of Mature Protein. Tag Info: C-terminal 6xHis-tagged. Target Protein Sequence: MKAIDKMTDN PPQEGLSGRK IIYDEDGKPC RSCNTLLDFQ YVTGKISNGL KNLSSNGKLA GTGALTGEAS ELMPGSRTYR KVDPPDVEQL GRSSWTLLHS VAASYPAQPT DQQKGEMKQF LNIFSHIYPC NWCAKDFEKY IRENAPQVES REELGRWMCE AHNKVNKKLR KPKFDCNFWE KRWKDGWDE. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is 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 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: 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. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins. Reference: "The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre." Hofhaus G., Lee J.E., Tews I., Rosenberg B., Lisowsky T. Eur. J. Biochem. 270:1528-1535(2003). Function: nan