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Recombinant Escherichia coli cea protein is an E.coli-expressed partial protein. Molecularly, this cea protein is characterized by N-terminal 10xHis tag and C-terminal Myc tag, internal Escherichia coli cea DNA fragment (1-304aa). Standard methods for recombinant cea protein expression comprise transfecting cells with DNA vectors that consist of specific templates and then cultures cells to translate and transcribe the cea protein production process. Typically, these cells are lysed to extract expressed proteins for more purification. The purity of this recombinant cea protein is 85%+ measured by SDS-PAGE.cea, also known as colicin E1, is a bacteriocin produced by E. coli that acts against bacteria by forming a pore in the bacterial membrane, leading to membrane depolarization and cell death. The cobalamin translocator BtuB binds to the colicin E1, initiating the import of colicin E1. The drug-export protein TolC is essential for the import of colicin E1 across the outer membrane and periplasmic space. Treatment of cells harboring the plasmid ColE1 with chemicals that damage DNA or interfere with DNA synthesis can result in the production of colicin E1.
|Purity||Greater than 85% as determined by SDS-PAGE.|
|Research Area||Tags & Cell Markers|
|Target Protein Sequence||METAVAYYKDGVPYDDKGQVIITLLNGTPDGSGSGGGGGKGGSKSESSAAIHATAKWSTAQLKKTQAEQAARAKAAAEAQAKAKANRDALTQRLKDIVNEALRHNASRTPSATELAHANNAAMQAEDERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLQNRPFFEATRRRVGAGKIREEKQKQVTASETRINRINAD
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
|Mol. Weight||38.2 kDa
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
|Buffer||Tris-based buffer，50% glycerol|
|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 Condition||Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.|
|Shelf Life||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.
|Lead Time||3-7 business days|
|Notes||Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.|
|Datasheet & COA||Please contact us to get it.|
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This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.; Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
|Subcellular Location||Cell membrane; Multi-pass membrane protein.|
|Protein Families||Channel forming colicin family|