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Lab Reagents

Lab Reagents: Absolute Lectins

Absolute Lectins, perfect for Glycoscience Medicago is a primary manufacturer of a wide variety of exceptionally pure lectins purified by affinity chromatography. Lectins are non-enzymatic proteins of non-immunoglobulin origin that bind specifically and reversibly to carbohydrate moieties without altering the covalent structure of the glycosyl ligands. The term ‘lectin’ is derived from the latin word legere, meaning ‘to select’. The specificity of a lectin is usually defined by the monosaccharides or oligosaccharides that are best at inhibiting the agglutination or precipitation caused by the lectin. Lectins are usually of plant origin but do occur in many types of organism; some are glycoproteins and may be soluble or membrane-bound.

The biological function of lectins is far from fully explored. Their specificity enables binding to glycoproteins and polysaccharides as well as agglutination of erythrocytes and stimulation of blood lymphocytes. Because of their ability to distinguish glycosyl ligands on human red blood cells, lectins can be used for blood typing.Immobilized lectins can be used in affinity chromatography to purify and isolate glycoproteins, glycolipids, polysaccharides, viruses and cells.

Carbohydrate-containing substances bound to the lectin may be eluted with a competitive binding substance. Medicago offers lectins as a freeze-dried powder or as a solution manufactured under aseptic conditions. If you don’t find the lectin you are looking for, we can certainly produce it for you. Furthermore, we offer different custom lectin conjugates on request.

•Ultrapure quality

•High activity

•Wide range

•Lyophilized powder

•Custom lectins and conjugates

Concanavalin A (Con A)

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.

Medicago AB

Catalogue No.DescriptionPack SizePriceQty
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  • £
MC-05-0106-100Concanavalin A (Con A) 100 mg €168.00 Quantity Add to Order
MC-05-0106-1000Concanavalin A (Con A) 1g €289.20 Quantity Add to Order
MC-05-0106-250Concanavalin A (Con A) 250 mg €182.40 Quantity Add to Order

Description

Product description

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.


Features 

  • Ultrapure quality
  • Sugar specificity: α-Man, α-Glc
  • Mitogen acting, principally on T-lymphocytes
  • Reacts with a number of bacterial and animal cells
  • Agglutinates neuraminidase treated erythrocytes

If you cannot find the answer to your problem then please contact us or telephone +44 (0)1954 210 200

References

References

(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.

If you cannot find the answer to your problem then please contact us or telephone +44 (0)1954 210 200

Notes

Specifications

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°

If you cannot find the answer to your problem then please contact us or telephone +44 (0)1954 210 200

Applications & Benefits

Applications

  • Hormone receptor studies
  • Lymphocyte mitogenic studies
  • Characterization of certain normal and malignant cells
  • Affinity chromatography

If you cannot find the answer to your problem then please contact us or telephone +44 (0)1954 210 200