Aleuria aurantia lectin (AaL) (100 mg)

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Aleuria aurantia lectin (AaL) (100 mg)
Code: A05-0134-100mg
Manufacturer’s Part Number: 05-0134-100mg
Shipping Weight: 1.00 pounds
Quantity in Basket: None

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

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].

Information

SKU ID# Packaging Website Links
A05-0134-100mg 100 mg www.buffer-solutions.com
 
Features Specifications Applications
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.
Appearance: White to pale yellow lyophilized powder or flocculate.
Source: E.coli.
Molecular weight: Two identical subunits of 36 kDa.
Sugar specificity: Fucose α1-2, α1-3, α1-4 and α1-6.
Activity: Agglutinates human erythrocytes irrespective of blood type (A, B and 0).
Microorganisms: < 100 CFU/g.
Protein content: > 80%.
Identity: SDS-PAGE, 4 mg/ml, staining with coomassie R-350, one band between 30 and 45 kDa.
Shelf life: > Five years when stored at -20°.
Studies of glycoproteins and glycolipids.
Purification of membrane proteins.
Affinity chromatography.
Agglutination studies.

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