CD BioGlyco offers a complete production solution for the Production of Lectins. BanLec is a dimer formed from two subunits. It has mannose-specific binding sites, including binding to those membrane proteins that contain glycosylation. It may therefore inhibit HIV-1 invasion by binding to the envelope protein gp120. The researchers found that it also induced apoptosis in cancer cell lines. To meet the different research needs of our clients for the production of different Plant Lectins such as BanLec, we provide one-stop BanLec production services.
Fig.1 Process of BanLec production. (CD BioGlyco)
We extract lectins from the pulp of M. paradisiaca. Based on the reported extraction and purification methods, we carry out optimization and moderate modifications. M. paradisiaca fruits are cut into thin slices and soaked in phosphate-buffered saline for some time. After centrifugation to remove impurities ammonium sulfate is added for precipitation. After that, we use Affinity Chromatography for further purification. Finally, purified BanLec is obtained by dialysis and freeze-drying.
BanLec has mannose or glucose binding specificity. The nature of its sugar-specific binding site and some biochemical functions are investigated. After extracting the purified BanLec, we also provide its biochemical characterization services. Molecular weight, product purity, amino acid composition, sugar-binding specificity, agglutination activity, etc., are all examined.
Based on optimized extraction methods, we improve the yield and purity of BanLec. We offer a wide range of BanLec products, including unconjugated BanLec, biotin conjugate, ferritin conjugate, rhodamine conjugate, etc. BanLec-related genes have been cloned. We obtain recombinant BanLec after transfecting the gene into Escherichia coli for Expression. In addition to BanLec and its conjugates, we also provide recombinant BanLec products.
| Cat. No. | Product Name | Cat. No. | Product Name |
|---|---|---|---|
| XLC-92-01Q | BanLec, Unconjugate | XLC-92-14Q | BanLec, Peroxidase Conjugate |
| XLC-92-03Q | BanLec, Alkaline Phosphatase Conjugate | XLC-92-15Q | BanLec, Rhodamine Conjugate |
| XLC-92-04Q | BanLec, Biotin Conjugate | XLC-92-16Q | BanLec, Cy3 Conjugate |
| XLC-92-05Q | BanLec, Colloidal Gold Conjugate | XLC-92-17Q | BanLec, Cy5 Conjugate |
| XLC-92-11Q | BanLec, Ferritin Conjugate | XLC-92-18Q | BanLec, Texas Red Conjugate |
| XLC-92-12Q | BanLec, FITC Conjugate | XLC-103-22Q | BanLec, E. coli, Recombinant |
Technology: Affinity Chromatography
Journal: The Protein Journal
IF:1.317
Published: 2018
Results: In the present study, affinity chromatography was used to purify the crude extract of BanLec obtained from M. paradisiaca pulp. The purified natural BanLec was finally obtained. Preliminary mass spectrometry analysis of it showed the presence of proteins of different molecular weights. The molecular masses of the monomers ranged from 14.4-14.8 kDa, indicating the presence of isoforms of the protein. The three main isoforms for which acetylation at the N-terminus was present were identified by top-down and bottom-up analysis.
Fig.2 Fragmentation of unique peptides belonging to isoforms present in native BanLec. (Gnanesh Kumar & Surolia, 2018)
CD BioGlyco is a modern enterprise integrating lectin research and development, production, and sales services. We have a perfect project management system to ensure real-time updates of experimental progress and make timely adjustments. Please feel free to contact us for information about BanLec's offer, production process, and biochemical properties of the assay. We are at your service.
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