Maackia amurensis Lectin (MAA/MAL I) - Pure
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Product Description
Maackia amurensis Lectin (MAA/MAL I) is a leukoagglutinating lectin isolated from Maackia amurensis seeds and purified by affinity chromatography. MAA I can be used to detect N-linked glycans containing the trisaccharide Siaα2-3Galß1-4GlcNAc. MAA detects sialic acid α2,3-position. This Lectin does not agglutinate one blood type more than another and agglutination can be inhibited by sialyllactose or lactose at higher concentrations. Although MAA I and MAA II are similar in size and structure, this Lectin is a more potent mitogen and exhibits less hemagglutinating ability than MAA II.
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. This product comes in a lyophilized form.
Recommended Usage: Recommended dilutions of 0.5 – 10 ug/ml in 1XPBS pH 7.4. 5 – 20 ug/ml can agglutinate leukocytes (human, rabbit, porcine).
Technical Specifications
| Abbreviation | : | MAA/MAL I |
| Material Source: | : | Amur maackia |
| Conjugate: | : | None |
| Concentration: | : | 2 mg, 5 mg |
| Molecular Weight: | : | 130 kDa |
| Purity: | : | High Purity Grade |
| Shelf Life: | : | 2 years |
| Blood Group Specificity: | : | Non-specific |
| Preferred Sugar Specificity: | : | Sialic Acid, Lactose |
| Inhibiting or Eluting Sugar: | : | Neu5Acα2-3Galβ1-4GlcNAc |
| Divalent Ions: | : | None Required |
| Mitogenic Activity: | : | Yes |
| Lyophilized or Liquid | : | Lyophilized |
| Storage Temperature: | : | -20°C |
| Hazardous Shipping: | : | Non-hazardous |
Applications
Immunohistochemistry, Immunocytochemistry, Bioconjugation, Cancer biomarker, Neu5Acα2,3Galβ1,4GlcNA detection/sialic acid / sialyltransferases/ profiling, Cell typing, Targeted drug delivery, therapeutic agent, ELISA, Blotting, Glycobiology.
References
- 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) 1315–1321.
- 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.
- Els J.M. Van Damme, Fred Van Leuven and Willy J. Peumans. Isolation, characterizationand molecularcloningof the bark lectins from Maackia amurensis. Glycoconjugate Journal (1997) 14: 449—456.
- 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.
- Kawaguchi T, Matsumoto I, Osawa T. Studies on hemagglutinins from Maackia amurensis seeds. J Biol Chem. 1974 May 10;249(9):2786-92.
