Maackia amurensis Lectin (MAA/MAL II) - FITC (Fluorescein) – Research Use Only

Maackia amurensis Lectin (MAA/MAL II) - FITC is a fluorescein-conjugated lectin from Maackia amurensis that specifically recognizes α2,3-linked sialic acid residues on glycoproteins and glycolipids. Supplied as a 2 mg liquid, this FITC-labeled lectin enables bright green fluorescence detection for glycan profiling, lectin blotting, histochemistry, and cell surface labeling in cancer, immunology, and developmental biology research.

Scientific Overview

Maackia amurensis Lectin II (MAL II / MAA) is a sialic acid-binding lectin that exhibits high specificity for α2,3-linked sialic acid residues, particularly Neu5Acα2-3Galβ1-4GlcNAc/Glc sequences found on N- and O-glycans. Conjugation to fluorescein (FITC) allows direct green-channel fluorescence detection without secondary reagents, making it a powerful tool for glycan profiling, visualization of sialylated glycoproteins, and investigation of sialylation changes in disease states such as cancer and inflammation.

This MAA/MAL II - FITC conjugate is suitable for:

• Detection of α2,3-linked sialic acids in glycan profiling and lectin blotting
• Fluorescence microscopy and flow cytometry of cell surface sialylation
• Histochemical and immunohistochemical analysis of tissue glycosylation patterns
• Studies of sialylation changes in cancer progression, immune regulation, and developmental biology
• Characterization of sialylated glycoproteins and viral receptors

Usage & Handling Guidance

Store the liquid conjugate at -20 °C. Avoid repeated freeze–thaw cycles by preparing working aliquots. Thaw gently on ice and mix by gentle inversion before use. Dilute in buffer containing divalent cations (Ca²⁺, Mn²⁺) if required for optimal lectin activity and include appropriate blocking agents to reduce non-specific binding.

• Recommended applications: Lectin blotting, immunofluorescence, flow cytometry, histochemistry, and glycan profiling
• Working dilution: Optimize empirically (typical range 1:100 – 1:1,000 depending on application and detection method)
• Excitation / Emission: FITC – Excitation ~495 nm, Emission ~520 nm (green channel)
• Handling: Keep on ice during use; protect from prolonged light exposure

What You Get

• 2 mg Maackia amurensis Lectin (MAA/MAL II) conjugated to FITC as a liquid
• High-specificity lectin for α2,3-linked sialic acid detection
• Ready-to-use fluorescent probe for glycan and cell surface studies
• Biotechnology-grade reagent manufactured with ultrapure water and sterile filtration
• For research use only (RUO)

Why Researchers Choose It

• High specificity for α2,3-linked sialic acid residues
• Direct FITC conjugation for bright green fluorescence detection
• Excellent tool for glycan profiling, sialylation studies, and cancer research
• Supports lectin blotting, flow cytometry, and histochemistry workflows
• High-purity biotechnology-grade formulation

Frequently Asked Questions (FAQ)

• What linkage does MAL II / MAA specifically recognize?
  It preferentially binds α2,3-linked sialic acid (Neu5Acα2-3Gal).
• What are the spectral properties of the FITC conjugate?
  Excitation ~495 nm, emission ~520 nm (standard green/FITC channel).
• What storage conditions are recommended?
  Store at -20 °C. Prepare aliquots to avoid repeated freeze–thaw cycles.
• Is divalent cation required for binding?
  Many lectins perform best with Ca²⁺ and Mn²⁺; include them in the buffer if binding appears weak.
• Is this suitable for flow cytometry?
  Yes. It is commonly used for labeling live or fixed cells to analyze surface sialylation patterns.

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References

• Geisler C, Jarvis DL. Effective glycoanalysis with Maackia amurensis lectins requires a clear understanding of their binding specificities. Glycobiology. 2011;21(8):988-993.
• Putthisen S, et al. Targeting alpha2,3-sialylated glycan in glioma stem-like cells by Maackia amurensis lectin-II: A promising strategy for glioma treatment. Biochem Biophys Res Commun. 2022;587:1-8.
• Wattanavises S, et al. Increase of MAL-II binding alpha2,3-sialylated glycan is associated with 5-FU resistance and short survival of cholangiocarcinoma patients. Medicina (Kaunas). 2019;55(12):761.
• Sata T, et al. Detection of the Neu5Ac (alpha 2,3) Gal (beta 1,4) GlcNAc sequence with the Maackia amurensis lectin-gold complex. Histochemistry. 1989;90(6):441-448.
• Yamamoto K, et al. Sialic acid-binding motif of Maackia amurensis lectins. J Biochem. 1997;121(4):756-761.
• Qin Y, et al. Serum glycopattern and Maackia amurensis lectin-II binding glycoproteins in autism spectrum disorder. Sci Rep. 2017;7:46041.
• Ishigaki H, et al. Detection of sialic acids on the cell surface using flow cytometry with Maackia amurensis lectin II. Methods Mol Biol. 2022;2556:123-134.
• Ohyama C, et al. Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy. Glycobiology. 2004;14(8):671-679.
• Uehara F, et al. Maackia amurensis lectin binding in developing rat retina. Invest Ophthalmol Vis Sci. 1994;35(5):2213-2218.
• Bai X, et al. Enhanced 3-O-sulfation of galactose in Asn-linked glycans and its effect on the binding of Maackia amurensis lectin. Glycobiology. 2001;11(8):621-628.