推荐产品
生物源
rabbit
品質等級
抗體表格
affinity purified immunoglobulin
抗體產品種類
primary antibodies
無性繁殖
polyclonal
純化經由
affinity chromatography
物種活性
human
製造商／商標名
Chemicon®
技術
western blot: suitable
UniProt登錄號
運輸包裝
dry ice
目標翻譯後修改
phosphorylation (pSer396)
基因資訊
human ... MAPT(4137)
一般說明
Tau is a neuronal microtubule-associated protein found predominantly on axons and functions to promote tubulin polymerization and stabilize microtubules. Tau, in its hyperphosphorylated form, is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer′s disease (AD) brain. Hyperphosphorylated Tau is also found in neurofibrillary lesions in a range of other central nervous system disorders. Hyperphosphorylation impairs the microtubule binding function of Tau, resulting in the destabilization of microtubules in AD brains, ultimately leading to the degeneration of the affected neurons. Numerous serine/threonine kinases, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II (CK2), phosphorylate Tau. Serine 396 is phosphorylated by GSK-3beta and cdk5 in vitro and in vivo.
特異性
Tau phosphoSerine 396. The antibody recognizes Tau pSerine 396 in samples of recombinant human Tau treated with GSK-3beta for 45 minutes. The reactivity of the antibody is blocked with the pSerine 396 peptide but not the non-phosphopeptide or a generic phosphoSerine-containing peptide.
The immunogen is conserved in rat, mouse, rhesus monkey, goat, bovine and baboon.
免疫原
Synthetic peptide of amino acids surrounding the phosphoSerine 396 site of human Tau.
應用
Anti-Tau phospho Serine 396 Antibody detects level of Tau phospho Serine 396 & has been published & validated for use in WB.
法律資訊
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 2
Protein kinase C and calcium / calmodulin-dependent protein kinase II phosphorylate three-repeat and four-repeat tau isoforms at different rates.
Singh, T.J., et al.
Molecular and Cellular Biochemistry, 168(1-2), 141-148 (1997)
E Sontag et al.
Neuron, 17(6), 1201-1207 (1996-12-01)
Recently, we reported that a pool of protein phosphatase 2A (PP2A) is associated with microtubules. Here, we demonstrate that specific isoforms of PP2A bind and dephosphorylate the neuronal microtubule-associated protein tau. Coexpression of tau and SV40 small t, a specific
G A Jicha et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 19(17), 7486-7494 (1999-08-25)
To elucidate the role cAMP-dependent protein kinase (PKA) phosphorylations on tau play in Alzheimer's disease, we have generated highly specific monoclonal antibodies, CP-3 and PG-5, which recognize the PKA-dependent phosphorylations of ser214 and ser409 in tau respectively. The present study
Jean C Augustinack et al.
Acta neuropathologica, 103(1), 26-35 (2002-02-12)
Microtubule associated protein tau is abnormally phosphorylated in Alzheimer's disease (AD) and aggregates as paired helical filaments (PHFs) in neurofibrillary tangles (NFTs). We show here that the pattern of tau phosphorylation correlates with the loss of neuronal integrity. Studies using
A D Alonso et al.
The Journal of biological chemistry, 276(41), 37967-37973 (2001-08-10)
The microtubule-associated protein tau is a family of six isoforms that becomes abnormally hyperphosphorylated and accumulates in neurons undergoing neurodegeneration in the brains of patients with Alzheimer disease (AD). We investigated the isoform-specific interaction of normal tau with AD hyperphosphorylated
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