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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
Store at -20℃,2 years.(Avoid freeze/thaw cycles)
- 保质期:
Store at -20℃,2 years.(Avoid freeze/thaw cycles)
- 英文名:
Palmitoyl Hexapeptide-12
- 库存:
现询
- 供应商:
北京索莱宝科技有限公司
- 规格:
10mg/5mg/1mg
| 规格: | 10mg | 产品价格: | ¥1540.0 |
|---|---|---|---|
| 规格: | 5mg | 产品价格: | ¥1100.0 |
| 规格: | 1mg | 产品价格: | ¥440.0 |
| 基本信息 | |
| 产品类型 | 多肽 |
| CAS | No.131580-10-4 |
| 单字母序列 | DAEFRHDSGYEVHHQK |
| 三字母序列 | Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys |
| 别名 | Beta-Amyloid (1-16),Human |
| 分子式 | C84H119N27O28 |
| 分子量 | 1955.03 |
| 纯度 | ≥98% |
| 外观(性状) | 冻干粉;Lyophilized powder |
| 盐体系 | TFA盐;Trifluoroacetate salt |
| 来源 | 合成;Synthetic |
| 储存条件 | Store at -20℃,2 years.(Avoid freeze/thaw cycles) |
| 类别/标签 | 淀粉样肽(Amyloid Peptides) |
| 规格 | β-Amyloid (1-16) 是可参与金属结合的β-淀粉样蛋白片段。 β-淀粉样蛋白是在阿尔茨海默病患者的脑中形成淀粉样斑块的肽。β-Amyloid (1-16) is a β-Amyloid protein fragment involved in metal binding. Beta-amyloid is a peptide that forms amyloid plaques in the brains of Alzheimer's disease (AD) patients. |
| In Vitro | 未检测 |
| In Vivo | β-amyloid (1-16) fragment is considered as valid models to examine the contribution of the key histidine residues (His , His in mouse and His , His , His in human fragments) to the Ab–Cu2+ interaction. Oxidation targets for β-Amyloid (1-16) are the histidine residues coordinated to the metal ions. Copper is bound to Aβ in senile plaque of Alzheimer’s disease with β-Amyloid (1-16) taking part in the coordination of the Cu2+ ions. Cu2+ and Zn2+ are linked with the neurotoxicity of -Amyloid and free radical damage. β-amyloid (1-16) is the minimal amino acidic sequence display a Cu coordination mode which involves three Histidines (His6, His13 and His14). β-amyloid (1-16) is supposed to be involved in metal binding. Human β-amyloid interacts with zinc ions through its metal-binding domain 1-16. The C-tails of the two polypeptide chains of the rat Aβ(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Aβ dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat β-Amyloid (1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer's disease. |
| 单位 | 瓶 |
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