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Concanavalin A (Con A) is a carbohydrate-binding protein that binding to the mannose residues of various glycoproteins, which can be extensively applied for diverse investigations. With Ph.D. level scientists and cutting-edge technology platforms in glycoprotein-related research, Creative Biolabs is able to offer the first-rate services on Con A glycoproteins profiling with perfect strategies and competitive quote.

What Is Con A?

Structure of Con A.Fig.1 Structure of Con A.

Con A, a member of the legume lectin family, is a plant lectin that extracted from jack beans. It can bind to the mannose residues of various glycoproteins and stimulate lymphocytes. ConA is a commercial lectin that widely used in biology and biochemistry to characterize glycoproteins, as well as used as lectin affinity chromatography to purify glycosylated macromolecules. ConA is molecular with diverse biological activities:

  • As a lectin, ConA can interact with a wide range of receptors containing mannose carbohydrates, particularly rhodopsin, blood group markers, insulin-receptor, the immunoglobulins, and the carcino-embryonary antigen.
  • As a plant mitogen, ConA directly stimulates mouse T-cell subsets and induces several T cell populations increase.
  • ConA shows the potential therapeutic effect of against experimental hepatoma.
  • ConA-glycoenzyme couplings have proved to be a useful method in glycoenzymes solid-phase immobilization, especially those difficult to immobilize by traditional covalent coupling.

Con A-Binding Glycoproteins Profiling

As a plant lectin, Con A was reported that the widely used model for acute immune-mediated hepatitis in mice, which was driven by the activation and recruitment of T cells to the liver. However, Con A was also demonstrated to be effective on anti-hepatoma due to its autophagic cytotoxicity and immunomodulation dual properties via the specific carbohydrate binding. Con A binding glycoproteins may serve as male infertility marker proteins human seminal plasma.

Due to its significantly biological activities and diverse applications, profiles of ConA-binding glycoproteins based on modern biological technology have been well performed. Creative Biolabs has rich experience in Con A-binding glycoproteins profiling. Based on our powerful Technologies, we can offer our clients high-quality service in glycoproteins profiling.

Con A-bound serum glycoproteins digested with trypsin prior to MALDI-TOF Fig.2 Con A-bound serum glycoproteins digested with trypsin prior to MALDI-TOF (Drake, 2006).

Creative Biolabs is more than happy to share our extensive experience in glycoproteins profiling. If you are interested in our glycoproteins profiling service, please feel free to contact us for more detailed information.


  1. Drake, R.R.; et al. Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers. Molecular & Cellular Proteomics. 2006, 5(10): 1957-1967.
For Research Use Only.

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