Concanavalin A (ConA) Conjugates

Concanavalin A (ConA) is a carbohydrate-binding lectin originally isolated from the jack bean (Canavalia ensiformis), known for its high affinity for mannose and glucose residues typically found on glycoproteins and glycolipids of cell membranes. This selective binding makes ConA an invaluable tool for investigating cell surface glycosylation patterns, analyzing glycoprotein structure, and studying membrane dynamics. Beyond its role in glycoprotein research, ConA is a potent T cell mitogen that activates the immune system, recruits lymphocytes, stimulates cytokine production, and induces programmed cell death through apoptosis and autophagy pathways. It also activates NFAT (nuclear factor of activated T cells), a key transcription factor involved in T cell receptor (TCR) signaling and immune response modulation.

Fluorescent ConA conjugates, particularly those labeled with iFluor® or XFD dyes, offer bright and photostable options for fluorescence microscopy, flow cytometry, and biochemical assays. iFluor®-ConA conjugates enable precise labeling and visualization of cell surface and intracellular glycoproteins, making them essential for detecting, characterizing, and quantifying glycosylated proteins in a wide range of biological and immunological applications.

 

Properties of Concanavalin A

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Concanavalin A (ConA) selectively binds to α-D-mannosyl and α-D-glucosyl residues found in a variety of glycoproteins and polysaccharides present on the cell surface and within extracellular matrices. The presence and distribution of these sugar moieties can vary significantly among different cell types and tissues, making ConA a useful probe for examining glycosylation patterns and studying membrane-associated glycoproteins. ConA is a water-soluble protein that exists as a tetramer with a molecular weight of ~104 kDa under physiological conditions. It is slightly acidic (pI ≈ 4.5-5.5) and can readily agglutinate erythrocytes and other cell types by cross-linking glycosylated surface proteins.

ConA binding is calcium- and manganese-dependent, with optimal activity at neutral to slightly basic pH. Unlike some other lectins, ConA can penetrate live cells, making it ideal for both live-cell and fixed-cell labeling experiments. When conjugated to fluorescent dyes or enzymes, ConA can be used to label, visualize, and analyze glycoproteins and glycolipids in various applications such as fluorescence microscopy, flow cytometry, and Western blotting. Additionally, its ability to induce mitogenesis in lymphocytes and its interaction with insulin receptors have made ConA an important tool for investigating cell signaling pathways and studying the immune response.

Fluorescent iFluor®-ConA Conjugates

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AAT Bioquest proudly offers iFluor® ConA conjugates in a spectrum of vibrant fluorescence colors. Our lineup includes the popular green-fluorescent iFluor® 488, bright red-fluorescent iFluor® 594, and far-red iFluor® 647-ConA conjugates. These innovative conjugates not only match the spectra of traditional FITC, Texas Red, and Cy5 dyes, but also deliver substantially brighter and more photostable signals across a broader pH range (pH 4 to 10).

The longer-wavelength iFluor® 647-ConA, which emits at a maximum of 670 nm, is particularly advantageous for multicolor imaging or when working with complex samples that exhibit high levels of intrinsic autofluorescence, such as tissue sections. Its emission profile is well-separated from commonly used blue- and green-fluorescent dyes, significantly reducing the need for signal compensation and simplifying your experimental design.

We also offer a variety of ConA conjugates labeled with our XFD dye equivalents, including popular options like XFD488 and XFD594. Our XFD dyes share the same chemical structure as the original Alexa Fluor® dyes, but with enhanced performance and higher purity—delivering superior results at an exceptional value.

Products

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