FAD-linked sulfhydryl oxidase ALR (Gfer), rat, recombinant

Organism: Rattus norvegicus (Rat). Source: E.coli. Expression Region: 1-198aa. Protein Length: Full Length. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: MAAPSEPAGF PRGSRFSFLP GGAHSEMTDD LVTDARGRGA RHRKDNAPAA APAPKGLEHG KRPCRACVDF KSWMRTQQKR DIKFREDCPQ DREELGRNTW AFLHTLAAYY PDMPTPEQQQ DMAQFIHIFS KFYPCEECAE DIRKRIDRSQ PDTSTRVSFS QWLCRLHNEV NRKLGKPDFD CSRVDERWRD GWKDGSCD. Purity: Greater than 90% 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 regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. May have a function in liver regeneration and spermatogenesis. Reference: "The crystal structure of augmenter of liver regeneration: a mammalian FAD-dependent sulfhydryl oxidase." Wu C.-K., Dailey T.A., Dailey H.A., Wang B.-C., Rose J.P. Protein Sci. 12:1109-1118(2003). Function: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. May have a function in liver regeneration and spermatogenesis.