Purity
Greater than 85% as determined by SDS-PAGE.
Research Area
Tags & Cell Markers
Expression Region
1-304aa
Target Protein Sequence
METAVAYYKDGVPYDDKGQVIITLLNGTPDGSGSGGGGGKGGSKSESSAAIHATAKWSTAQLKKTQAEQAARAKAAAEAQAKAKANRDALTQRLKDIVNEALRHNASRTPSATELAHANNAAMQAEDERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLQNRPFFEATRRRVGAGKIREEKQKQVTASETRINRINAD
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Tag Info
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Form
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.
Description
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.
