磷酸化APP淀粉樣肽前體蛋白抗體（）

英文名稱：Anti-phospho-APP/ABPP（Thr668）                               濃度： 1mg/1ml 

抗體來源：Rabbit

克隆類型：polyclonal          

 交叉反應： Human, Mouse, Rat, Chicken, Dog, Pig, Cow, Horse, Rabbit,      

產品類型: 一抗  

性    狀:Lyophilized or Liquid 

保存條件： Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. 

產品介紹 ：Amyloid Precursor Protein （APP） functions as a cell surface kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. APP is important for neurite growth, neuronal adhesion and axonogenesis. Immature APP （N-glycosylated in the endoplasmic reticulum） moves to the Golgi complex where complete maturation occurs （O-glycosylated and sulfated）. After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP is expressed in the brain, kidney, heart and spleen of fetal tissues; it is induced during neuronal differentiation. In adult brain, highest expression of APP is found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Defects in APP are a cause of autosomal dominant Alzheimer's disease （AD）. Phosphorylation of APP at Tyr757 and 762 is important for MAPK8IP1, APBA1, shcA/shcC and DAB1 binding. Binding interactions regulated by phosphorylation determine the localisation and the function of APP. Therefore Amyloid Precursor Protein （phospho Y757） antibody will be a useful tool in tracing the processing, distribution and interaction of APP

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