刀豆蛋白A（Concanavalin A，Con A），来源于Canavalia ensiformis洋刀豆（刀豆），是一种凝集素蛋白（Mw 104kDa）。pH≥7.0条件下，Con A以同质四聚体结构形式存在，由四个分子量为26kDa的亚基构成。酸性条件（pH 4.5-5.5）下，Con A解离为活化的二聚体结构（52kDa）。每一个单体，不管pH值或分子结构如何，都包含2个金属离子结合位点。金属离子（Ca2+ 和 Mn2+ ）必须结合到这两个位点上Con A才能发挥活性。乙酰化、琥珀酰化或其他衍生物也能产生稳定的二聚体结构形式。
刀豆蛋白A（Concanavalin A，Con A）无血型特异性，但选择性结合各种糖蛋白、糖脂和糖类分子上的α-甘露糖基（α-mannosyl residues）和α-葡糖基残基（α-glucosyl residues）。我们提供多种刀豆蛋白A偶联物，用于荧光检测含有α-D-甘露糖或α-D-葡萄糖的糖蛋白。
使用说明
1.根据检测需求使用相应浓度，一般5‑200 µg/mL可满足大部分免疫荧光检测需求。
2.伴刀豆凝集素(Concanavalin A, Con A)由四个相同亚基组成四聚体蛋白，每个亚基在结合糖时需要Ca2+和Mn2+参与。虽然这些二价金属离子可牢固地结合多肽结构，但是应该避免使用含磷酸盐等可与Ca2+结合的缓冲液稀释伴刀豆凝集素(Concanavalin A, Con A)，因为这将导致伴刀豆凝集素(Concanavalin A, Con A)的活性降低。
Concanavalin A (ConA) lectin is isolated from Jack beans (Canavalia ensiformis) and purified by affinity chromatography. The molecular weight of the lectin is 104 kDa. The lectin has broad applicability and is the most widely used lectin within molecular biology research. ConA binds specifically to α-Mannose, α-Galactose structures found in sugars, glycoproteins and glycolipids.
We offer a broad selection of concanavalin A conjugates for the fluorescent detection of glycoproteins containing α−D-mannose or α−D-glucose. Biotinylated Concanavalin A has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins.
Guideline for Use
1.Training protocols vary with application. The appropriate dilution of concanavalin A conjugate should be determined empirically. A final concentration of 5‑200 µg/mL is typically satisfactory for immunohistochemical applications.
2.Con A requires calcium or manganese ions at each of its four saccharide binding sites. Although these divalent metal ions are bound tightly to the polypeptide structure, buffers which can bind calcium (such as phosphate) generally should be avoided in diluting Con A, since a gradual loss in activity may occur.
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