400-998-5282
专注多肽 服务科研
400-998-5282
专注多肽 服务科研
淀粉样蛋白具有神经营养和神经毒性作用的生物活性结构域位于β（25-35）序列GSNKGAIGLM中，该序列与速激肽家族肽中的一个区域同源。
编号：155032
CAS号：131602-53-4
单字母：H2N-GSNKGAIIGLM-OH
β-Amyloid (25-35)是阿尔茨海默氏淀粉样蛋白β肽的Aβ(25-35)片段。
The biologically active domain of the amyloid β-protein for neurotrophic and neurotoxic effects is located in the β (25-35) sequence GSNKGAIIGLM, which is homologous to a region in peptides of the tachykinin family.
β-淀粉样蛋白通常存在于阿尔茨海默病(AD) 患者的大脑中，是老年痴呆症淀粉样斑块的主要组成部分。人大脑中β-淀粉样蛋白的主要存在形式是Aβ (1-40) 和Aβ (1-42)。然而研究发现存在于老年人脑中的Aβ(25 - 35)片段由于其特有的聚合性，毒性更大，与阿尔茨海默病(AD)息息相关。
Aβ(25-35) 由于其神经毒害作用被认为是Aβ的功能域，它是β-淀粉样蛋白的生物活性区域。研究表明小鼠侧脑室注射Aβ(25-35)片段可导致小鼠失忆，引起小鼠空间学习记忆能力障碍，并伴随被动回避反应的衰退。
在体内，Aβ (25-35)存在于阿尔茨海默病(AD)患者脑中下托及内嗅皮质神经元中[7]，也存在于包涵体肌炎(IBM)患者的肌肉中。
"Amyloid beta-protein (Aβ) is a protein that is a major component of amyloid plaques in the brains of people with Alzheimers disease. Aβ-Protein (25-35) trifluoroacetate salt, also known as Aβ(25-35), is an amyloid beta protein fragment that has been shown to inhibit neuronal death and increase antioxidative properties in human serum. It has been shown to have anti-apoptotic effects by inhibiting the activation of caspases and the release of cytochrome C from mitochondria. This drug may have physiological effects on the central nervous system due to its ability to induce apoptosis through mitochondrial membrane depolarization and cytosolic calcium levels. It has been shown to be active against Chinese herb Pueraria lobata and cell lysis, as well as granule neurons in culture. It may also stimulate phosphorylation of p38mapk and induce logarithmic growth"
"Amyloid beta-Protein (Human, 25-35) is the shortest amyloid fragment that forms β-sheet fibrils, while retaining toxicity, and may also induce the aggregation of N-tau protein and N-tau peptide 1/2R. Consequently this peptide may play a role in the pathogenesis of Alzheimers disease, a neurodegenerative disorder that affects memory and cognitive function.\nThis product is available as a trifluoroacetate salt and as a 0.5mg vial."
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