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. 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.
GlycoBindTM Buffer is for maximized adsorption of MAA/MAL I lectin. GlycoBindTM is utilized for separation and purification of glycoproteins or glycoconjugates with lectin-specific carbohydrate residues.
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- Source: Maackia amurensis (Amur maackia)
- Activity: Non-specific
- Carbohydrate Specificity: Siaα2-3Galß1-4GlcNAc
- Molecular Weight: 130 kDa
- Inhibitory Carbohydrate: Lactose
- Divalent Ions Required: None
- Mitogenic Activity: Yes
- Conjugation: Binding Buffer
Storage and Stability:
Store at 2-8°C.