Musa paradisiaca Lectin Production Service

Musa paradisiaca Lectin Production Service

Musa paradisiaca Lectin (BanLec) Production Service at CD BioGlyco

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.

Process of BanLec production. (CD BioGlyco) Fig.1 Process of BanLec production. (CD BioGlyco)

  • BanLec production service

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.

  • BanLec products

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.

Publication

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.

Fragmentation of unique peptides belonging to isoforms present in native BanLec. Fig.2 Fragmentation of unique peptides belonging to isoforms present in native BanLec. (Gnanesh Kumar & Surolia, 2018)

Applications of BanLec Production

  • BanLec is found to have better anti-HIV activity. The BanLec we produce is used in the development of antiviral drugs.
  • Our BanLec is used for affinity chromatography purification of glycoligands bound to lectins.
  • The BanLec we produce is used to quantify sugar conjugates that react with lectins in enzyme-linked lectin binding assays.

Advantages of Us

  • With our rich experience in plant lectin research, we are confident that excel in BanLec production services.
  • We have a wide range of BanLec-related products, including biotin conjugate, rhodamine conjugate, ferritin conjugate, and so on. We also have recombinant BanLec products.

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.

Reference:

  1. Gnanesh Kumar, B.S.; Surolia, A. Identification of banana lectin isoforms and differential acetylation through mass spectrometry approaches. The Protein Journal. 2018, 37: 38-46.
This service is for Research Use Only, not intended for any clinical use.

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