Key features and details
- Rabbit polyclonal to Tau (phospho T205)
- Suitable for: Flow Cyt, WB
- Reacts with: Mouse, Human
- Isotype: IgG
製品名Anti-Tau (phospho T205) antibody
Tau 一次抗体 製品一覧
製品の詳細Rabbit polyclonal to Tau (phospho T205)
アプリケーション適用あり: Flow Cyt, WBmore details
種交差性交差種: Mouse, Human
Synthetic peptide (Human) derived from the region of human tau that contains threonine 205.
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保存方法Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: 0.05% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.1% BSA
Concentration information loading...
精製度Immunogen affinity purified
特記事項（精製）Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated tau. The final product is generated by affinity chromatography using a tau-derived peptide that is phosphorylated at threonine 205.
Our Abpromise guarantee covers the use of ab4841 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: 1/1000. Predicted molecular weight: 62 kDa. Can be blocked with Tau peptide - phospho T205 (phospho and non-phospho pair).
Not tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
機能Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
組織特異性Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.
関連疾患Note=In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU).
Defects in MAPT are a cause of frontotemporal dementia (FTD) [MIM:600274]; also called frontotemporal dementia (FTD), pallido-ponto-nigral degeneration (PPND) or historically termed Pick complex. This form of frontotemporal dementia is characterized by presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons.
Defects in MAPT are a cause of Pick disease of the brain (PIDB) [MIM:172700]. It is a rare form of dementia pathologically defined by severe atrophy, neuronal loss and gliosis. It is characterized by the occurrence of tau-positive inclusions, swollen neurons (Pick cells) and argentophilic neuronal inclusions known as Pick bodies that disproportionally affect the frontal and temporal cortical regions. Clinical features include aphasia, apraxia, confusion, anomia, memory loss and personality deterioration.
Note=Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease.
Defects in MAPT are a cause of progressive supranuclear palsy type 1 (PSNP1) [MIM:601104, 260540]; also abbreviated as PSP and also known as Steele-Richardson-Olszewski syndrome. PSNP1 is characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613.
配列類似性Contains 4 Tau/MAP repeats.
発生段階Four-repeat (type II) tau is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau is found in both adult and fetal brain.
ドメインThe tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.
翻訳後修飾Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK: CDK1, CDK5, GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in PHF-tau), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK) in Alzheimer diseased brains. Phosphorylation decreases with age. Phosphorylation within tau's repeat domain or in flanking regions seems to reduce tau's interaction with, respectively, microtubules or plasma membrane components. Phosphorylation on Ser-610, Ser-622, Ser-641 and Ser-673 in several isoforms during mitosis.
Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur.
Glycation of PHF-tau, but not normal brain tau. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD.
細胞内局在Cytoplasm > cytosol. Cell membrane. Cytoplasm > cytoskeleton. Cell projection > axon. Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.
- Information by UniProt
製品の状態There are 9 isoforms produced by alternative splicing.
- AI413597 antibody
- AW045860 antibody
- DDPAC antibody
WB using Ab4841. The peptide corresponding to tau [pT205] blocks the antibody signal, thereby demonstrating the specificity of the antibody.
Flow cytometric analysis of 70% ethanol-fixed SH-SY5Y (human neuroblastoma cell line from bone marrow) cell line labeling Tau (phospho T205) with ab4841 at 5 μg/million cells (red) compared with a rabbit Isotype control details (pink),an unlabelled control (purple) and a secondary only control (green). Alexa Fluor® 488 Goat Anti-Rabbit, at 1/400 dilution was used as the secondary antibody.
ab4841 は 9 報の論文で使用されています。
- Bathini P et al. Progressive signaling changes in the olfactory nerve of patients with Alzheimer's disease. Neurobiol Aging 76:80-95 (2019). PubMed: 30708185
- Moosecker S et al. Activated PPAR? Abrogates Misprocessing of Amyloid Precursor Protein, Tau Missorting and Synaptotoxicity. Front Cell Neurosci 13:239 (2019). PubMed: 31263400
- Liu Z et al. Amyloid ß and tau are involved in sleep disorder in Alzheimer's disease by orexin A and adenosine A(1) receptor. Int J Mol Med 43:435-442 (2019). PubMed: 30365112
- Tong M et al. T3D-959: A Multi-Faceted Disease Remedial Drug Candidate for the Treatment of Alzheimer's Disease. J Alzheimers Dis 51:123-38 (2016). PubMed: 26836193
- Brai E et al. Notch1 hallmarks fibrillary depositions in sporadic Alzheimer's disease. Acta Neuropathol Commun 4:64 (2016). PubMed: 27364742
- Hamm M et al. Physiologically relevant factors influence tau phosphorylation by leucine-rich repeat kinase 2. J Neurosci Res 93:1567-80 (2015). PubMed: 26123245
- Krstic D et al. Systemic immune challenges trigger and drive Alzheimer-like neuropathology in mice. J Neuroinflammation 9:151 (2012). WB, IHC-FrFl ; Mouse . PubMed: 22747753
- Kocherhans S et al. Reduced Reelin expression accelerates amyloid-beta plaque formation and tau pathology in transgenic Alzheimer's disease mice. J Neurosci 30:9228-40 (2010). IHC-FoFr . PubMed: 20610758
- Nathan C et al. Protection from Alzheimer's-like disease in the mouse by genetic ablation of inducible nitric oxide synthase. J Exp Med 202:1163-9 (2005). PubMed: 16260491