Purity
Greater than 90% as determined by SDS-PAGE.
Species
Unknown prokaryotic organism
Expression Region
1-376aa
Target Protein Sequence
DINGGGATLPQKLYLTPDVLTAGFAPYIGVGSGKGKIAFLENKYNQFGTDTTKNVHWAGSDSKLTATELATYAADKEPGWGKLIQVPSVATSVAIPFRKAGANAVDLSVKELCGVFSGRIADWSGITGAGRSGPIQVVYRAESSGTTELFTRFLNAKCTTEPGTFAVTTTFANSYSLGLTPLAGAVAATGSDGVMAALNDTTVAEGRITYISPDFAAPTLAGLDDATKVARVGKGVVNGVAVEGKSPAAANVSAAISVVPLPAAADRGNPDVWVPVFGATTGGGVVAYPDSGYPILGFTNLIFSQCYANATQTGQVRDFFTKHYGTSANNDAAIEANAFVPLPSNWKAAVRASFLTASNALSIGNTNVCNGKGRPQ
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Protein Length
Full Length
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
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℃/-80℃. 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
In order to produce the recombinant unknown prokaryotic organism phosphate-binding protein, the gene fragment encompassing the full-length protein (amino acids 1-376) and an N-terminal 10xHis-tag and C-terminal Myc-tag is cloned into a suitable expression vector. The cloning process involves inserting the gene fragment downstream of the appropriate promoter and regulatory elements. The resulting expression construct is then introduced into E. coli host cells through a transformation method. The transformed cells are selected to confirm the presence of the recombinant plasmid. Large-scale culture of the transformed E. coli cells is subsequently established in a growth medium optimized for protein expression. The presence of an N-terminal 10xHis-tag and C-terminal Myc-tag enables easy purification and detection of the recombinant phosphate-binding protein. Following cell lysis, the recombinant phosphate-binding protein is extracted and purified from the cell lysate. The purity of the recombinant phosphate-binding protein is evaluated through SDS-PAGE analysis, demonstrating a purity level of up to 90%. On the gel, the purified protein appears as a distinct band with an approximate molecular weight of 45 kDa.