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天然蛋白检测试剂
您的位置:首页 > 产品中心 > 细胞生物学 > 细胞培养 > 天然蛋白
Human Complement Component C3c

Human Complement Component C3c

Human Complement Component C3c

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中文名称:
Human Complement Component C3c
英文名称:
Human Complement Component C3c
品牌:
AAA Biotech
品牌介绍:
AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具,核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
货号:
AAA38513
规格:
0.2 mg|1 mg|10 mg|2x10 mg|3x10 mg
保存建议:
Human C3c although stable at room temperature for 3 weeks, should be stored between 2-8 degree C.
货期:
6-8周
纯度:
Greater than 96.0%.
产品形式:
The Human Complement C3c was lyophilized in a sodium phosphate buffer, pH 7.2, containing 0.15M NaCl.
Sterile Filtered White lyophilized (freeze-dried) powder.
免责声明:
*本产品仅供科研实验使用,不得用于临床诊断。*
说明书:
Description: Human C3c produced in Human Plasma having a molecular mass of 137 KDa.

Introduction: The C3c component is central in both complement activation pathways, with different specific proteolytic systems cleaving it to form C3 convertase. Cleavage of C3 releases C3a and the C3b fragment which is part of the alternative C3 convertase. C3 levels can be low because of decreased synthesis or due to consumption. High C3 levels are seen in highly acute or chronic inflammation, hepatic cholestasis and during the third trimester of pregnancy.Unwanted complement activation is a major cause of tissue damage in various pathological conditions and contributes to quite a few immune complex diseases. Compstatin is an effective inhibitor of the activation of complement component C3 and thus blocks a central and essential step in the complement cascade. The specific binding site on C3, the configuration in the bound form, and the exact mode of action of compstatin are unknown. The crystal structure of compstatin in complex with C3c reveals that the compstatin-binding site is formed by the macroglobulin (MG) domains 4 and 5. This binding site is part of the structurally stable MG-ring created by domains MG16 and is distant from any other known binding site on C3. Compstatin does not modify the conformation of C3c, while compstatin itself undergoes a large conformational alteration upon binding.

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