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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

Galanthus nivalis lectin (GNA)

alanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. Is has a molecular weight of 50 kDa and consists of four identical subunits. The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes (1). It binds specifically to murine IgM immunoglobulin and human a2-macroglobulin. Structures containing (a-1,3) mannose residues are preferred for binding

Medicago AB

Catalogue No.DescriptionPack SizePriceQty
MC-05-0120-5Galanthus nivalis lectin (GNA) 5 mg £66.00 Quantity Add to Order

Galanthus nivalis lectin (GNA)

alanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. Is has a molecular weight of 50 kDa and consists of four identical subunits. The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes (1). It binds specifically to murine IgM immunoglobulin and human a2-macroglobulin. Structures containing (a-1,3) mannose residues are preferred for binding

Medicago AB

Product description

Galanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. Is has a molecular weight of 50 kDa and consists of four identical subunits (1). The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes (1). It binds specifically to murine IgM immunoglobulin and human α2-macroglobulin. Structures containing (α-1,3) mannose residues are preferred for binding (2). It contains little or no carbohydrate and does not need Ca2 or Mn2 for binding, since unlike most mannose-specific lectins it is not a metalloprotein. Unlike the majority of mannose-binding lectins, GNA does not bind alpha-linked glucose. GNA has been useful in HIV research (3). It is also applicable for blood cell agglutination studies but also as a model system to help understand the molecular basis of how proteins recognize carbohydrates.

Medicago’s GNA lectin is supplied as a white to cream coloured lyophilized powder. The purity of GNA lectin is determined by SDS- electrophoresis, which generates one single band at 13 kDa corresponding to the four identical polypeptide chains. The lectin is available in vials containing 5 mg powder and is to be used for laboratory work only.

  Features 

  • Ultrapure quality
  • Agglutinates rabbit erythrocytes
  • Sugar specificity: (α-1,3) mannose residues
  • Binds to serum IgM and α2- macroglobulin
  • Lyophilized powder

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.

 

 


References

(1) Naoto Shibuya, Irwin J. Goldstein, Els J. M. Van Damme and Willy J. Peumans. (1988) Binding Properties of a Mannose-specific Lectin from the Snowdrop (Galanthus nivalis) Bulb* J. Mol. Biol. Vol. 263, No. 2, Issue of January 15, pp. 728-734

(2) Christine S. Wright, Hanae Kaku and Irwin J. Goldstein (1990). Crystallization and Preliminary X-ray Diffraction Results of Snowdrop (Galanthus nivalis) Lectin. J.Mol.Biol. Vol. 265, No. 3, Issue of January 25, pp. 1676-1677

(3) Gilljam, G. AIDS Reserach and Human Retroviruses. May 1993; 9(5): 431–8.

(4) The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 A and 3.0 A resolution. Hester, G., Wright, C.S. (1996) J.Mol.Biol. 262: 516–31.

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

Galanthus nivalis lectin (GNA)

alanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. Is has a molecular weight of 50 kDa and consists of four identical subunits. The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes (1). It binds specifically to murine IgM immunoglobulin and human a2-macroglobulin. Structures containing (a-1,3) mannose residues are preferred for binding

Medicago AB

References

(1) Naoto Shibuya, Irwin J. Goldstein, Els J. M. Van Damme and Willy J. Peumans. (1988) Binding Properties of a Mannose-specific Lectin from the Snowdrop (Galanthus nivalis) Bulb* J. Mol. Biol. Vol. 263, No. 2, Issue of January 15, pp. 728-734

(2) Christine S. Wright, Hanae Kaku and Irwin J. Goldstein (1990). Crystallization and Preliminary X-ray Diffraction Results of Snowdrop (Galanthus nivalis) Lectin. J.Mol.Biol. Vol. 265, No. 3, Issue of January 25, pp. 1676-1677

(3) Gilljam, G. AIDS Reserach and Human Retroviruses. May 1993; 9(5): 431–8.

(4) The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 A and 3.0 A resolution. Hester, G., Wright, C.S. (1996) J.Mol.Biol. 262: 516–31.

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

Galanthus nivalis lectin (GNA)

alanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. Is has a molecular weight of 50 kDa and consists of four identical subunits. The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes (1). It binds specifically to murine IgM immunoglobulin and human a2-macroglobulin. Structures containing (a-1,3) mannose residues are preferred for binding

Medicago AB

Specifications

Appearance: White to cream coloured lyophilized powder                              

Source: Snowdrop bulbs

Molecular weight: 52 kDa

Sugar specificity: (α-1,3) Man residues

Activity: Blood group non-specific

Microorganisms: < 100 CFU/g

Protein content: > 85 %, OD280nm (ε 1mg/ml = 1.14), >95%, essentially salt free

Identity: SDS-PAGE, one band at 13 kDa

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

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

Galanthus nivalis lectin (GNA)

alanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. Is has a molecular weight of 50 kDa and consists of four identical subunits. The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes (1). It binds specifically to murine IgM immunoglobulin and human a2-macroglobulin. Structures containing (a-1,3) mannose residues are preferred for binding

Medicago AB

Applications

  • Blood cell agglutination studies
  • Model systems to help understand the molecular basis of how proteins recognize carbohydrates
  • HIV research

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