Stringent starvation protein B (sspB), Escherichia coli O157:H7, recombinant

Organism: Escherichia coli O157:H7. Source: E.coli. Expression Region: 1-165aa. Protein Length: Full Length. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: MDLSQLTPRR PYLLRAFYEW LLDNQLTPHL VVDVTLPGVQ VPMEYARDGQ IVLNIAPRAV GNLELANDEV RFNARFGGIP RQVSVPLAAV LAIYARENGA GTMFEPEAAY DEDTSIMNDE EASADNETVM SVIDGDKPDH DDDTHPDDEP PQPPRGGRPA LRVVK. 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: Seems to act in concert with SspA in the regulation of several proteins during exponential and stationary-phase growth. The exact function of SspB is not yet known. Reference: "Dual regulatory pathways of flagellar gene expression by ClpXP protease in enterohaemorrhagic Escherichia coli." Kitagawa R., Takaya A., Yamamoto T. Microbiology (Reading, Engl.) 157:3094-3103(2011). Function: Seems to act in concert with SspA in the regulation of several proteins during exponential and stationary-phase growth. The exact function of SspB is not yet known (By similarity).