Macoma Birmanica Lectin Production Service

Macoma birmanica lectin (MBL) is a glycoprotein with a molecular weight of 47 kDa. MBL belongs to the Animal Lectins. MBL interacts well with complex N-linked glycans and medium-high mannose-type N-linked glycans. MBL interacts with Gram-positive bacteria and Gram-negative bacteria by recognizing antigen-containing, surface-exposed GlcNAc from Gram-negative bacteria. Our company provides comprehensive Lectin Production Services, and we hope to be your best assistant!

MBL Extraction and Purification Service at CD BioGlyco

Take the foot muscle of Macoma birmanica and cut it into small pieces. Soak in the buffer for homogenization, and centrifuge the supernatant. Ammonium sulfate is added to precipitate the supernatant and centrifugate the buffer again. Then, collect target fractions and dialysis. An immobilized GlcNAc affinity chromatography column is used for purification and elution. The lectin fractions are detected in real-time and collected tube by tube. Every step is tightly controlled.

Fig. 1 Schematic diagram of MBL production service. (CD BioGlyco)

MBL Analysis Service at CD BioGlyco

We offer a wide range of analytical for purified samples with reliable and highly reproducible data. We have very experienced researchers to meet the needs of our clients. The services we offer are as follows:

Lectin homogeneity assay: We use sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to determine the homogeneity of MBL.
Determination of protein concentration: Determination using the Folin phenol reagent based on bovine serum proteins as standards.
Biological activities: We provide lectin activity assay services. In addition, the extent of binding of MBL to different N- and O-glycans and their derivatives is measured by enzyme-linked lectin adsorption assay (ELLSA). Through ELLSA and growth inhibition studies, we provide quantitative determination of bacterial growth by MBL.

Publication

Paper Title: Purification and characterization of an N-acetylglucosamine-specific lectin from marine bivalve Macoma birmanica

Journal: Fish & Shellfish Immunology

IF: 4.6

Published: 2009

Results: The results showed that MBL bound to a variety of bacteria in a dose-dependent manner, including B. subtilis, S. aureus, E. coli, and V. parahaemolyticus. Among these, the marine bacterium V. parahaemolyticus had the strongest ability to bind to MBL. In addition, E. coli was second only to V. parahaemolyticus in its binding capacity. Studies showed that MBL was a bacterial growth inhibitor.

Fig.2 Chart of analyzed data of HSL. (Nagaraji, et al., 2008) Fig.2 Chart of analyzed data of HSL. (Nagaraji, et al., 2008)

Applications of MBL

MBL plays a crucial role in host defense and is very potent in inhibiting bacterial growth in vitro.
MBL as a specific recognition molecule very well identifies both exposed and internal α-Man and β-GlcNAc/Glc residues.
MBL is part of an immune-like response involved in the recognition and targeting of invading pathogens.
MBL plays an important role in the innate immunity of marine bivalves.

Advantages of Us

We have a team of experienced personnel to designate different production schedules for different projects.
We have an advanced and mature instrumentation platform suitable for providing analytical identification services.

CD BioGlyco provides Natural Lectin Production Services to clients. Our professional and responsible service attitude has been recognized by our clients. Please feel free to contact us if you have any needs in MBL production.

References

Adhya, M.; et al. Purification and characterization of an N-acetylglucosamine specific lectin from marine bivalve Macoma birmanica. Fish Shellfish Immunol. 2009, 27(1): 1-8.
Adhya, M.; et al. Macoma birmanica agglutinin recognizes glycoside clusters of beta-GlcNAc/Glc and alpha-Man. Carbohydr Res. 2009, 344(18): 2489-95.

This service is for Research Use Only, not intended for any clinical use.