阿尔茨海默病、帕金森病等神经退行性疾病呈快速增长趋势，已成为严重的社会问题。近年来，肌萎缩性侧索硬化症(ALS)等顽固性神经系统疾病的致病基因被发现，为研究其发病机制开辟了新的途径。已有研究表明，特定蛋白质的聚集和积累导致神经毒性和病变的形成，但发病和进展机制尚不清楚。神经病理诊断和实验模型生物标志物是药物构建、药物发现和治疗发展所必需的。
α -突触核蛋白是一种在突触前末端大量表达的140个氨基酸蛋白质，是帕金森病(PD)、路易体痴呆(DLB)和多系统萎缩(MSA)病例中观察到的神经元内或胶质包体的组成部分。虽然α -突触核蛋白是一种天然的未折叠蛋白，但α -突触核蛋白的纤维化或构象变化对α -突触核蛋白病的发病机制至关重要。α -突触核蛋白的氨基末端区域由7个不完全重复序列组成，每个重复序列长度为11个氨基酸，一致序列为KTKEGV。重复序列部分重叠于疏水区域(氨基酸61-95)。羧基末端(96-140氨基酸)带负电荷。这些抗体是神经退行性疾病的生化和免疫组化分析以及α -突触核蛋白构象变化评估的有力工具。
Cosmo Bio抗体,Anti Alpha Synuclein (Amino Acids 75-91) pAb (Rabbit, Antiserum),CAC-TIP-SN-P08
Application: IHC, WB, ELISA
Clonality: Polyclonal
Host: Rabbit
Purification: Serum
Reactivity: Human, Mouse
Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.
Alpha-Synuclein, a 140-amino acid protein abundantly expressed in presynaptic terminals, is a component of intraneuronal or glial inclusions observed in cases of Parkinson’s disease (PD), Dementia with Lewy bodies (DLB) and Multiple system atrophy (MSA). Although alpha-synuclein is a natively unfolded protein, fibrillization or conformational change(s) of alpha-synuclein is central to the pathogenesis of alpha-synucleinopathies. The amino-terminal region of alpha-synuclein consists of seven imperfect repeats, each 11 amino acids in length, with the consensus sequence KTKEGV. The repeats partially overlap with a hydrophobic region (amino acids 61-95). The carboxy-terminal region (amino acids 96-140) is negatively charged. These antibodies are powerful tools for biochemical and IHC analyses of neurodegenerative diseases and for evaluation of conformational changes of alpha-synuclein.