Microbiology Recombinant Proteins
E.Coli MBP (27-396) Recombinant Protein (RPPB3941)
- SKU:
- RPPB3941
- Product Type:
- Recombinant Protein
- Species:
- Escherichia coli
- Uniprot:
- P0AEX9
- Research Area:
- Microbiology
Description
Product Name: | E.Coli MBP (27-396) Recombinant Protein |
Product Code: | RPPB3941 |
Size: | 20µg |
Species: | E.Coli |
Target: | MBP (27-396) |
Synonyms: | Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994. |
Source: | Escherichia Coli |
Physical Appearance: | Sterile Filtered colorless solution. |
Formulation: | MBP protein solution (1mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol. |
Stability: | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
Purity: | Greater than 95.0% as determined by SDS-PAGE. |
Amino Acid Sequence: | MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIA VEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTRIT K |
UniProt Code: | P0AEX9 |
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.
Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (27-396 a.a) and having a molecular mass of 40.8kDa. MBP protein was purified by proprietary chromatographic techniques.