Alternative Name(s):

Species: (Organism)

Escherichia coli (strain K12)

Gene Names:

sapA

Tag info:

N-terminal 10xHis-tagged and C-terminal Myc-tagged

Target Protein AA Sequence:

APESPPHADIRDSGFVYCVSGQVNTFNPSKASSGLIVDTLAAQFYDRLLDVDPYTYRLMPELAESWEVLDNGATYRFHLRRDVPFQKTDWFTPTRKMNADDVVFTFQRIFDRNNPWHNVNGSNFPYFDSLQFADNVKSVRKLDNHTVEFRLAQPDASFLWHLATHYASVMSAEYARKLEKEDRQEQLDRQPVGTGPYQLSEYRAGQFIRLQRHDDFWRGKPLMPQVVVDLGSGGTGRLSKLLTGECDVLAWPAASQLSILRDDPRLRLTLRPGMNVAYLAFNTAKPPLNNPAVRHALALAINNQRLMQSIYYGTAETAASILPRASWAYDNEAKITEYNPAKSREQLKSLGLENLTLKLWVPTRSQAWNPSPLKTAELIQADMAQVGVKVVIVPVEGRFQEARLMDMSHDLTLSGWATDSNDPDSFFRPLLSCAAIHSQTNLAHWCDPKFDSVLRKALSSQQLAARIEAYDEAQSILAQELPILPLASSLRLQAYRYDIKGLVLSPFGNASFAGVYREKQDEVKKP

Expression Region:

22-547aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Full Length of Mature Protein

Pathway:

Mol. Weight:

66.9 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

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.

Research Areas:

Others

Function:

Involvement in disease:

Relevance:

Not part of a putrescine export system. Very similar to a S.typhimurium protein implicated in antimicrobial peptide resistance, but the SapBCDF operon in E.coli is implicated in putrescine export.

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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Reference:

"A novel putrescine exporter SapBCDF of Escherichia coli." Sugiyama Y., Nakamura A., Matsumoto M., Kanbe A., Sakanaka M., Higashi K., Igarashi K., Katayama T., Suzuki H., Kurihara S. J. Biol. Chem. 291:26343-26351(2016)