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Type II collagen is composed of a triple helix of three identical α chains. These molecules associate to form a fibril that is stabilized by intermolecular crosslinks1. Damage to the fibrillar meshwork, made up of primarily type II collagen (z 90–95%), maybe a critical event in the pathology of many arthritides, due in part to the very slow rate of collagen turnover within the cartilage2.
Type II collagen is composed of a triple helix of three identical α chains. These molecules associate to form a fibril that is stabilized by intermolecular crosslinks1. Damage to the fibrillar meshwork, made up of primarily type II collagen (z 90–95%), maybe a critical event in the pathology of many arthritides, due in part to the very slow rate of collagen turnover within the cartilage2.
规格 | 价格 | 库存 | 数量 |
---|---|---|---|
1 mg | ¥ 483 | 期货 | |
5 mg | ¥ 1,383 | 期货 | |
10 mg | ¥ 2,283 | 期货 | |
25 mg | ¥ 3,183 | 期货 |
产品描述 | Type II collagen is composed of a triple helix of three identical α chains. These molecules associate to form a fibril that is stabilized by intermolecular crosslinks1. Damage to the fibrillar meshwork, made up of primarily type II collagen (z 90–95%), maybe a critical event in the pathology of many arthritides, due in part to the very slow rate of collagen turnover within the cartilage2. |
体外活性 | Type II collagen and aggrecan (a large, aggregating proteoglycan) are the two major components of the extracellular matrix of cartilage. The collagen, which is present in a fibrillar form, provides tensile strength whereas the aggrecan is responsible for compressive stiffness of cartilage3-5. Early damage to type II collagen is predominantly pericellular/ territorial suggests that in the majority of cases collagen damage was mediated by the chondrocyte. |
分子量 | 1471.61 |
分子式 | C65H102N18O21 |
密度 | 1.31g/cm3 |
存储 | keep away from moisture | Powder: -20°C for 3 years | In solvent: -80°C for 1 year | Shipping with blue ice. |
溶解度信息 | DMSO: ≥147.1 mg/mL |
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