*** For pack size 1g or more, please contact us to inquire about pricing

Features 

• Ultrapure quality
• Agglutinates leucocytes, and to a lesser extent erythrocytes
• Sugar specificity: 3’Sialyllactose / Neu5Ac-α2,3-Gal-β1,4-Glc/GlcNAc
• Lyophilized powder

Product description

Maackia amurensis lectin or leucoagglutinin (MAL) is isolated from Maackia amurensis (amur tree) seeds and purified by affinity- and ion exchange chromatography. The lectin consist of two homodimeric subunits connected by disulfide bridges, each with a molecular weight of 75 kDa. MAL has a well studied mitogenic ability on human leucocytes, and a marginal capacity for erythrocyte agglutination (1, 2).

MAL has strong affinity for sialylated glycans, mainly in the form of 3’Sialyllactose, but lactose is tolerated (3).

Hypersialylation of the cell surface is characteristic of many cancerous cells and is thought to be important for immune evasion and migration (4, 5). This provides many opportunities for cancer screening and study using MAL.

Human influenza viruses bind to host cell using sialylated glycans, and specifically binding of 3’Sialic acid instead of 6’ Sialic acid seems to separate human targeting influenza virus from avian viruses (6).

Applications

• Identification of cancerous cells due to hypersialylation.
• Screening for human influenza virus binding sites.

Directions for use

The lectin may be reconstituted in a suitable buffer for your application.

Solubility is ascertained at 1 g/L using PBS, pH 7,4, but higher concentrations and other buffers have not presented issues.

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 PBS, pH 7.4, the solution may be stored frozen in working aliquots for up to 12 months.

Referenses

(1) Imberty A, Gautier C, Lescar J, Pérez S, Wyns L, Loris R. (2000) An Unusual Carbohydrate Binding Site Revealed by the Structures of Two Maackia amurensis Lectins Complexed with Sialic Acid-containing Oligosaccharides. Journal of Biological Chemistry, Volume 275 (23), 17541-17548

(2) Kawaguchi T, Matsumoto I, Osawa T. (1974) Studies on Hemagglutinins from Maackia amurensis Seeds. Journal of Biological Chemistry, Volume 249 (9), 2786-2792

(3) Geisler, C, & Jarvis, DL. (2011). Letter to the Glyco-Forum: Effective glycoanalysis with Maackia amurensis lectins requires a clear understanding of their binding specificities. Glycobiology, Volume 21 (8), 988-993.

(4) Pearce, OM, & Läubli, H. (2016). Sialic acids in cancer biology and immunity. Glycobiology, Volume 26 (2), 111-128.

(5) Tang, W., Mafune, K., Nakata, M., Konishi, T., Kojima, N., Mizuochi, T., & Makuuchi, M. (2003). Association of histochemical expression of Maackia amurensis leukoagglutinin‐positive glycoconjugates with behaviour of human gastric cancer. Histopathology, Volume 42 (3), 239-245.

(6) Yamada S, Suzuki Y, Suzuki T, Le MQ, Nidom CA, Sakai-Tagawa Y, Muramoto Y, Ito M, Kiso M, Horimoto T, Shinya K, Sawada T, Kiso M, Usui T, Murata T, Lin Y, Hay A, Haire LF, Stevens DJ, Russell RJ, Gamblin SJ, Skehel JJ, Kawaoka Y. (2006). Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors. Nature, Volume 444 (7117), 378–382.

Image from the RCSB PDB (RCSB.org) of PDB ID 1BNA (H.R. Drew, R.M. Wing, T. Takano, C. Broka, S. Tanaka, K. Itakura, R.E.Dickerson, Structure of a B-DNA dodecamer: conformation and dynamics (1981) Proc.Natl.Acad.Sci.USA 78: 2179-2183).

MSDS: 

SDS - MAL (Swedish)

SDS - MAL (English)