计算溶液所需的质量、体积或浓度。
免疫原级,天然 级 提供 ≥99%(SDS-PAGE) 纯度,适用于对基线干扰要求严格的色谱和分析工作流程。
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在色谱分析、有机合成和交叉偶联反应领域已被 0 篇同行评审文献引用。
IgG Fc 段不具备抗原结合能力,但可调控抗体依赖性细胞毒性、补体依赖性细胞毒性以及吞噬作用,通过 Fc 受体结合介导免疫功能。
蛋白生物学功能
免疫球蛋白 G 的 Fc(可结晶片段)区域虽不能结合抗原,但具备重要生物学活性与抗原决定簇。该同源二聚体糖蛋白由 CH2、CH3 结构域组成,通过与 Fc 受体、C1q、FcRn 相互作用介导免疫效应功能。Fc 片段调控抗体依赖性细胞毒性(ADCC)、补体依赖性细胞毒性(CDC)与吞噬作用;同时依靠 pH 依赖性结合 FcRn,调控 IgG 在血清中的半衰期。位于 297 位天冬酰胺(Asn-297)的保守 N - 连接糖基化位点,对维持蛋白结构稳定以及受体结合至关重要。
常见研究用途
Fc 糖基化模式改变与类风湿关节炎等自身免疫疾病相关;糖链的半乳糖基化、唾液酸化水平下降提示炎症状态。Fc 受体基因多态性也和自身免疫病发病相关。
常见用途:治疗药物研发、免疫系统研究、流式细胞实验、抗血清制备。
While lacking antigen binding capacity, IgG Fc orchestrates antibody-dependent cytotoxicity, complement-dependent cytotoxicity, and phagocytosis. It mediates immune function through FC-receptor binding.
Role of protein in biology
The Fc (fragment crystallizable) region of immunoglobulin G, while not binding antigen, contains crucial biological activities and antigenic determinants. This homodimeric glycoprotein comprises CH2 and CH3 domains and mediates immune effector functions through interactions with Fc receptors, C1q, and FcRn.
Fc fragments orchestrate antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and phagocytosis while controlling IgG's serum half-life via pH-dependent FcRn binding. The conserved N-linked glycosylation at Asn-297 is essential for structural stability and receptor interactions.
Common research uses
Altered Fc glycosylation patterns correlate with autoimmune conditions including rheumatoid arthritis, where reduced galactosylation and sialylation indicate inflammatory disease states. Fc receptor polymorphisms are also associated with autoimmune disease development.
Common uses include therapeutics research, immune system research, flow cytometry assays, antisera production.