Maackia amurensis Lectin (MAA/MAL II) - Alexa Fluor 647

Maackia amurensis Lectin (MAA/MAL II) is an affinity purified, hemagglutinating lectin and can be used to detect O-linked glycans containing the trisaccharide Siaα2-3Galß1-3GalNAc. This Lectin does not agglutinate one blood type more than another and agglutination can be inhibited by lactose at high concentrations. Although MAL I and MAL II are similar in size and structure, this lectin exhibits more hemagglutinating ability than MAL I.

               This lectin is used in a plethora of research. It has been exhibited that MAA inhibits oral squamous cell carcinoma growth and motility by decreasing activity of the JAK-STAT, TGFβ-SMAD, and Wnt-βCTN signaling pathways. MAA has been used to study Turkey adenovirus 3 activity, leaving evidence that the virus has attachment receptors that are both α2,3-linked and α2,6-linked sialic acids. As a sialic acid binding lectin, MAA has been used to observe content of sialic acid in seminoma testicular tissue, revealing that sialic acids may have roles in seminoma development by promoting invasiveness, as well as cross-talk between cancer-cells and the surrounding stroma and vessels. In novel SARS-CoV-2 research, it has been shown that MAA targets the ACE2 receptor, thus decreasing glycosylation and expression. As a result, the spike protein binding is suppressed, and inflammatory mediators have decreased expression. MAA II was shown to inhibit bluetongue virus infection and growth in sheep cells, showing the key functionality of sialic acid as a receptor for viral entry for the virus that affects domestic animals and has a high economic impact. In cholangiocarcinoma research, MAA II positive staining to sialylated glycans revealed elevated levels of glycans in the carcinomic cells over the hyperplastic/dysplastic and normal bile ducts. The same study used the lectin results to suggest that sialylation is involved in 5-fluorouracil resistance development. This product comes in a lyophilized form.

Maackia amurensis Lectin conjugated with Alexa Fluor™ 647 is a bright, far red fluorescent dye optimized for stable signal generation in imaging and flow cytometry. The excitation wavelength is well-suited for the 633 nm laser line, ensuring effective detection in various applications. This dye is water soluble and pH-insensitive from pH 4 to pH 10, providing dependable performance in different experimental conditions. The Alexa Fluor™ 647 conjugate enhances cellular labeling and detection, making it an excellent choice for advanced research applications.

Recommended usage: Recommended dilutions of 1-10 μg/ml in 1XPBS. 0.5 – 10 μg/ml can agglutinate neuraminidase treated erythrocytes.

Application

Immunohistochemistry, Immunocytochemistry, Immunofluorescence, Blotting, Cell typing, Diagnostic tools, Glycobiology.

References

1.Bum Soo Kim, Kyung Taik Oh,1, Due Hyeon Cho, Yun Jung Kim, Wan Mo Koo, Kwang Hoon Kong, HaHyung Kim. A sialic acid-binding lectin from the legume Maackia fauriei: comparison with lectins from M. amurensis. Plant Science 167 (2004) 315–1321.
2.Knibbs RN, Goldstein IJ, Ratcliffe RM, Shibuya N. Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins. J Biol Chem. 1991 Jan 5;266(1):83-8.
3.Els J.M. Van Damme, Fred Van Leuven and Willy J. Peumans. Isolation, characterization and molecular cloning of the bark lectins from Maackia amurensis. Glycoconjugate Journal (1997) 14: 449—456.
4.Konami Y, Yamamoto K, Osawa T, Irimura T. Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A. FEBS Lett. 1994 Apr 11;342(3):334-8.
5.Kawaguchi T, Matsumoto I, Osawa T. Studies on hemagglutinins from Maackia amurensis seeds. J Biol Chem. 1974 May 10;249(9):2786-92.