CLP1185 Palmitoyl Hexapeptide-12 化妆品肽 171263-26-6

CLP1185 Palmitoyl Hexapeptide-

12 化妆品肽 171263-26-6
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  • ¥440 - 1540
  • Solarbio|ActivAb
  • 北京
  • CLP1185
  • 2025年07月29日
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    • 详细信息
    • 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
    CASNo.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 Vivoβ-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

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