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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

Aleuria aurantia lectin (AAL)

Recombinant Aleuria aurantia lectin is produced in E.coli and has an amino acid sequence identical to native Aleuria aurantia lectin. AAL is a dimeric lectin with two identical subunits of approximately 36 kDa. Each subunit has five carbohydrate-binding sites (1). The lectin recognizes and binds specifically to fucose and terminal fucose residues on complex oligo saccharides and glycoconjugates. rAAL has binding affinity for fucose in all binding positions (a1-2, a1-3, a1-4 and a1-6) and in contrast to AAL purified from natural sources, ...

Medicago AB

Catalogue No.DescriptionPack SizePriceQty
MC-05-0134-2Aleuria aurantia lectin (AAL) 2mg £114.00 Quantity Add to Order

Aleuria aurantia lectin (AAL)

Recombinant Aleuria aurantia lectin is produced in E.coli and has an amino acid sequence identical to native Aleuria aurantia lectin. AAL is a dimeric lectin with two identical subunits of approximately 36 kDa. Each subunit has five carbohydrate-binding sites (1). The lectin recognizes and binds specifically to fucose and terminal fucose residues on complex oligo saccharides and glycoconjugates. rAAL has binding affinity for fucose in all binding positions (a1-2, a1-3, a1-4 and a1-6) and in contrast to AAL purified from natural sources, ...

Medicago AB

 ** for pack size 100mg, 1 g or more, please contact us to inquire about pricing

 

AAL Lectin

 

Features 

  • Ultrapure quality
  • Sugar specificity: fucose and terminal fucose residues on complex oligosaccharides and glycoconjugates
  • Binding affinity for fucose in all binding positions (α1-2, α1-3, α1-4 and α1-6)
  • Higher affinity towards fucosylated oligosaccharides than native AaL
  • Not blood group specific 

Product description

Recombinant Aleuria aurantia lectin is produced in E.coli and has an amino acid sequence identical to native Aleuria aurantia lectin. AAL is a dimeric lectin with two identical subunits of approximately 36 kDa. Each subunit has five carbohydrate-binding sites (1). The lectin recognizes and binds specifically to fucose and terminal fucose residues on complex oligo saccharides and glycoconjugates. rAAL has binding affinity for fucose in all binding positions (α1-2, α1-3, α1-4 and α1-6) and in contrast to AAL purified from natural sources, rAAL is not contaminated with free fucose yielding higher affinity towards fucosylated oligosaccharides than native AAL (2).

Recombinant AAL hemagglutinates erythrocytes irrespective of blood type (A, B and 0) at the same titers as AAL isolated from natural sources.

AAL has been widely used for analysis and preparation of oligosaccharides and glycoproteins (3). Diagnostic applications include analysis of disease-associated glycosylation on plasma proteins (4). Furthermore, rAAL can be immobilized and used for affinity chromatography (5).

 

Applications

  • Studies of glycoproteins and glycolipids
  • Purification of membrane proteins
  • Affinity chromatography
  • Agglutination studies

 

Directions for use

The lectin may be reconstituted with 10 mM HEPES, 0.15 M NaCl, pH 7.5, 0.08 % sodium azide, 0.1 mM Ca , 0.01 mM Mn . 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 HEPES buffer, the solution may be stored frozen in working aliquots for up to 12 months.

References

(1) Wimmerova M, Mitchell E, Sanchez JF, Gautier C, Imberty A. Crystal structure of fungal lectin: six-bladed beta-propeller fold and novel fucose recognition mode for Aleuria aurantia lectin. J Biol Chem. 2003; 278:27059-67.

(2) Olausson J, Tibell L, Jonsson BH, Påhlsson P. Detection of a high affinity binding site in recombinant Aleuria aurantia lectin.Glycoconj J. 2008; 25:753-62.

(3) Yazawa S, Kochibe N, Asao T. A simple procedure for isolation of tumor-associated antigens by affinity chromatography using fucose-specific Aleuria aurantia lectin. Immunol Invest. 1990; 19:319-27.

(4) Hashimoto S, Asao T, Takahashi J, Yagihashi Y, Nishimura T, Saniabadi AR, Poland DC, van Dijk W, Kuwano H, Kochibe N, Yazawa S. alpha1-acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis. Cancer. 2004; 101:2825-36.

(5) Bergström M, Aström E, Påhlsson P, Ohlson S. Elucidating the selectivity of recombinant forms of Aleuria aurantia lectin using weak affinity chromatography.  J Chromatogr B Analyt Technol Biomed Life Sci. 2011 [Epub ahead of print]

MSDS: 
application/pdf iconMSDS (AAL)

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