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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

Triticum vulgaris lectin (WGA)

Triticum vulgaris lectin or Weat germ agglutinin (WGA) is isolated from Triticum vulgaris (Weat germ) and purified by affinity chromatography. The lectin has two subunits and a molecular weight of 36 kDa. WGA selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids

Medicago AB

Catalogue No.DescriptionPack SizePriceQty
MC-05-0102-10Triticum vulgaris lectin (WGA) 10 mg £64.00 Quantity Add to Order
MC-05-0102-100Triticum vulgaris lectin (WGA) 100 mg £371.00 Quantity Add to Order

Triticum vulgaris lectin (WGA)

Triticum vulgaris lectin or Weat germ agglutinin (WGA) is isolated from Triticum vulgaris (Weat germ) and purified by affinity chromatography. The lectin has two subunits and a molecular weight of 36 kDa. WGA selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids

Medicago AB

 Product description

Triticum vulgaris lectin or Weat germ agglutinin (WGA) is isolated from Triticum vulgaris (Weat germ) and purified by affinity chromatography. The lectin has two subunits and a molecular weight of 36 kDa. WGA selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids (1).

The WGA lectin agglutinates erythrocytes and most types of malignant cells. It agglutinates rabbit erythrocytes at < 0.1 µg/ml following trypsin treatment of the cells. Adding 300 mM N-Acetyle-D-Glucosamine gives an inhibition with a titer that is at least 8-fold lower than the control.

Wheat germ agglutinin inhibits the C5a receptor interaction, which has implications in studies of receptor micro-heterogeneity and ligand binding sites (1).

WGA together with Con A is the lectin most widely used as an analytical and preparative agent when studying glycoproteins and cell surface proteins. The immobilized lectin can be used for affinity chromatography of cells and sub-cellular particles.

Medicago’s WGA is supplied as a white to pale yellow lyophilized powder from a buffer containing 10 mM CH3COONH4. No preservatives are added. The purity of WGA is determined by SDS- electrophoresis which generates three bands, corresponding to the three isolectins of WGA. Protein content is verified in spectrophotmetry The lectin is available in vials containing 100 mg, 25 mg or 10 mg powder and the product is to be used for laboratory work only.


Features 

  • Ultrapure quality
  • Sugar specificity: N-acetylglucosamine and N-acetylneuraminic acid residues
  • Agglutinates erythrocytes and most types of malignant cells
  • Agglutinates rabbit erythrocytes at ≤0.1 µg/ml after treating the cells with trypsin
  • Not blood group specific 


 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.

 

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 three 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.

 

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

Triticum vulgaris lectin (WGA)

Triticum vulgaris lectin or Weat germ agglutinin (WGA) is isolated from Triticum vulgaris (Weat germ) and purified by affinity chromatography. The lectin has two subunits and a molecular weight of 36 kDa. WGA selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids

Medicago AB

References

(1) Johnson R. J., Simpson S., Van Epps D. E., Chenoweth D. E. (1992) Wheat germ agglutinin inhibits the C5a receptor interaction: implications for receptor microheterogeneity and ligand binding site. Journal of Leukocyte Biology Vol 52, Issue 1, 3–10.

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

Triticum vulgaris lectin (WGA)

Triticum vulgaris lectin or Weat germ agglutinin (WGA) is isolated from Triticum vulgaris (Weat germ) and purified by affinity chromatography. The lectin has two subunits and a molecular weight of 36 kDa. WGA selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids

Medicago AB

Specifications

Appearance: White to pale yellow lyophilized powder or flocculate

Source: Weat germ

Molecular weight: 36 kDa

Sugar specificity: GlcNAc

Activity: N-Acetyle-D-Glucose amine at a concentration of of 100mM gives a hemaglutination/inhibition with a titer which is at least 8 times more dilute than the control. The control must have a titer of at least 32. Agglutinates erythrocytes and most types of malignant cells more readily than corresponding cells from normal tissues. Less than 4 μg/ml will agglutinate human type 0 erythrocytes.

Microorganisms: < 100 CFU/g

Protein content: > 85 %, OD280nm (ε 1.6 = 1 mg/mL)

Identity: SDS-PAGE, three bands – the three isolectins

Shelf life: > Three years when stored at -20°

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

Triticum vulgaris lectin (WGA)

Triticum vulgaris lectin or Weat germ agglutinin (WGA) is isolated from Triticum vulgaris (Weat germ) and purified by affinity chromatography. The lectin has two subunits and a molecular weight of 36 kDa. WGA selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids

Medicago AB

Applications

  • Studies of glycoproteins and glycolipids
  • Purification of membrane proteins
  • Affinity chromatography of cells and sub-cellular particles
  • Agglutination studies

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200