Larger Quantities Available Upon Request
- Ultrapure quality
- Sugar spcificity: α-Man, α-Glc
- Mitogen acting, principally on T-lymphocytes
- Reacts with a number of bacterial and animal cells
- Agglutinates neuraminidase treated erythrocytes
Concanavalin A (Con A) lectin is isolated from Jack beans (Canavalia ensiformis) and purified by affinity chromatography. The molecular weight of the lectin is 104 kDa. It has broad applicability and is the most widely used lectin within molecular biology research.
Con A binds specifically to α-Mannose, α-Galactose structures found in sugars, glycoproteins and glycolipids (2). The lectin has been utilized in hormone receptor studies, mitogenic assays and for characterizing normal and malignant cells (cancer cells are readily aggregated by Con A while normal cells are not). Con A can also initiate cell division (mitogenesis) principally acting on T-lymphocytes (3).
Immobilized Con A has been used in affinity chromatography purifications of a wide variety of glycoproteins and cellular structures.
Polyacrylamide gel electrophoresis in SDS of Con A from Jack beans yields three major bands corresponding to molecular weights 27, 13 and 10 kDa. One minor band is visible at 18 kDa. (4).
Medicago’s Con A is supplied as a white lyophilized powder from a buffer containing 0.5 mM MnCl2, 0.5 mM CaCl2, no preservatives are added. The identity is determined by SDS-PAGE (Figure 1) and the protein content by spectrophotometry (Figure 2). The lectin is available in vials containing 250 mg or 100 mg lyophilized powder and the product is to be used for laboratory work only.
- Hormone receptor studies
- Lymphocyte mitogenic studies
- Characterization of certain normal and malignant cells
- Affinity chromatography
Directions for use
The lectin may be reconstituted with 2 ml of deionized water before use. Spin the vial gently until full dissolution. Aggregation is thought to occur in the presence of high concentrations of 2-mercaptoethanol. The solution may be reconstituted in this buffer to desired working concentration. In absence of lactose the lectin will polymerize and storage at pH 8.6–8.8 causes precipitation.
Shipping and storage
The product is shipped at -20°C however for over-the-day transport it may be shipped at ambient temperature. The lyophilized powder is stable for more than five years from production date when stored below -20°C. After reconstitution with deionized water, the solution may be stored frozen in working aliquots for up to 12 months.
Appearance: White lyophilized powder
Source: Jack beans
Molecular weight: 104 kDa
Sugar specificity: a-Man, a-Glc
Activity: Con A reacts with a number of bacterial and animal cells and can distinguish between certain normal and tumour cells. It can initiate cell division (mitogenesis). 0,5-10 μg/ml is required to visibly agglutinate neuraminidase treated erythrocytes.
Microorganisms: < 100 CFU/g
Protein content: > 90 %, OD280nm (ε 1mg/ml = 1.14), > 95%, essentially salt free
Identity: SDS-PAGE, four bands corresponding to the four subunits
Shelf life: Five years when stored at -20°
(1) John L. Wang, Bruce A. Cunningham and Gerald M. Edelman (1971) Unusual Fragments in the Subunit Structure of Concanavalin A (gelelectrophoresis/molecularweights) Proc. Nat. A cad. Sci. USA Vol. 68, No. 6, pp. 1130-1134, JuRm
(2) Ahmed, H.U., Blakeley, M.P., Cianci, M., Cruickshank, D.W.J., Hubbard, J.A., Helliwell, J.R. (2007) The Determination of Protonation States in Proteins. Acta Crystallogr.,Sect.D 63: 906.
(3) Liener I. E., Sharon N., Goldstein I. J., (1986) The Lectins – Properties, Functions and Applications in Biology and Medicine.
(4) Krauss S., Buttgereit F., (1999) Effects of the mitogen concanavalin A on pathways of thymocyte energy metabolism. BrandBiochim Biophys Acta 1412: 129–38.