Chaperone protein htpG (htpG), partial, Bacteroides fragilis, recombinant

Organism: Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343). Source: E.coli. Expression Region: 1-326aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged. Target Protein Sequence: MQKGNIGVTT ENIFPIIKKF LYSDHEIFLR ELVSNAVDAT QKLNTLASIS EFKGELGDLT VHVSLGKDTI TISDRGIGLT AEEIDKYINQ IAFSGANDFL EKYKNDANAI IGHFGLGFYS AFMVSKKVEI ITKSYKEGAQ AVKWTCDGSP EFTLEEVEKA DRGTDIVLYI DDDCKEFLEE SRISALLKKY CSFLPVPIAF GKKKEWKDGK QVETAEDNVI NDTIPLWTKK PSELSDEDYK KFYRELYPMS DEPLFWIHLN VDYPFHLTGI LYFPKVKSNI DLNKNKIQLY CNQVYVTDSV EGIVPDFLTL LHGVLDSPDI PLNVSR. 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: Molecular chaperone. Has ATPase activity. Reference: "Extensive DNA inversions in the B. fragilis genome control variable gene expression." Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.Parkhill J. Science 307:1463-1465(2005). Function: Molecular chaperone. Has ATPase activity.