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Description
Lectin are used in a wide variety of applications. Con-A is not a glycoprotein and does not contain cysteine residues. Unlike most other lectins, Con-A is a metalloprotein and requires a transition metal ion, such as manganese, plus calcium ions for binding.
- Con A is not blood group specific but has an affinity for terminal α-D-mannosyl and α-D-glucosyl residues. Con-A binds specifically to mannosyl and glucosyl residues of polysaccharides and glycoproteins.
- Unmodified hydroxyl groups at the C3, C4 and C6 positions of D-glucopyranosyl or D-mannopyranosyl rings may be essential for binding.
- Each subunit of Con A contains one calcium ion and one manganese ion. Removal of these cations by dialysis under acidic conditions abolishes the carbohydrate-binding activity.
- Con A dissociates into dimers at pH 5.6 or below. Between pH 5.8 and pH 7.0, Con A exists as a tetramer. Above pH 7.0 higher aggregates are formed.
- Con A exhibits mitogenic activity which is dependent on its degree of aggregation. Succinylation results in an active dimeric form which remains a dimer above pH 5.6.
Specifications
Specifications
| Quantity | 500 mg |
| Solubility Information | Soluble in water (10mg/mL, slightly hazy, colorless solution). |
| Formula Weight | Monomeric molecular weight of Con-A is 25,500(Lit.) |
| Physical Form | Powder |
Safety and Handling
| Recommended Storage | −20°C |
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