Anti-Tau (phospho S202) 抗体 [EPR2402] (ab108387)
Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- Rabbit monoclonal [EPR2402] to Tau (phospho S202)
- Suitable for: WB, Dot blot
- Reacts with: Mouse, Rat, Human
Related conjugates and formulations
製品の概要
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製品名
Anti-Tau (phospho S202) antibody [EPR2402]
Tau 一次抗体 製品一覧 -
製品の詳細
Rabbit monoclonal [EPR2402] to Tau (phospho S202) -
由来種
Rabbit -
特異性
Stimulation may be required to allow detection of the phosphorylated protein. Please see images below for recommended treatment conditions and positive controls.
The specificity of this antibody refers to P10636-8.
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アプリケーション
適用あり: WB, Dot blotmore details
適用なし: Flow Cyt,ICC/IF or IHC-P -
種交差性
交差種: Mouse, Rat, Human -
免疫原
Synthetic peptide. This information is proprietary to Abcam and/or its suppliers.
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ポジティブ・コントロール
- WB: Human brain lysate, mouse hippocampus, rat hippocampus and cerebral cortex lysates.
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特記事項
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
製品の特性
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製品の状態
Liquid -
保存方法
Shipped at 4°C. Store at -20°C. Stable for 12 months at -20°C. -
解離定数(KD 値)
KD = 4.13 x 10 -12 M Learn more about KD -
バッファー
pH: 7.20
Preservative: 0.01% Sodium azide
Constituents: 0.05% BSA, 40% Glycerol (glycerin, glycerine), 59% PBS -
Concentration information loading...
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精製度
Protein A purified -
ポリ/モノ
モノクローナル -
クローン名
EPR2402 -
アイソタイプ
IgG -
研究分野
関連製品
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Alternative Versions
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Isotype control
アプリケーション
The Abpromise guarantee
Abpromise保証は、 次のテスト済みアプリケーションにおけるab108387の使用に適用されます
アプリケーションノートには、推奨の開始希釈率がありますが、適切な希釈率につきましてはご検討ください。
アプリケーション | Abreviews | 特記事項 |
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WB |
1/5000 - 1/10000. Predicted molecular weight: 79 kDa.
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Dot blot |
1/1000.
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特記事項 |
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WB
1/5000 - 1/10000. Predicted molecular weight: 79 kDa. |
Dot blot
1/1000. |
ターゲット情報
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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
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参照データベース
- Entrez Gene: 4137 Human
- Entrez Gene: 17762 Mouse
- Entrez Gene: 29477 Rat
- Omim: 157140 Human
- SwissProt: P10636 Human
- SwissProt: P10637 Mouse
- SwissProt: P19332 Rat
- Unigene: 101174 Human
see all -
製品の状態
There are 9 isoforms produced by alternative splicing. -
別名
- AI413597 antibody
- AW045860 antibody
- DDPAC antibody
see all
画像
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All lanes : Anti-Tau (phospho S202) antibody [EPR2402] (ab108387) at 1/1000 dilution
Lane 1 : Rat hippocampus lysate
Lane 2 : Rat hippocampus lysate then the membrane treated with Alkaline Phosphatase for 1 hour
Lane 3 : Rat cerebral cortex lysate
Lane 4 : Rat cerebral cortex lysate then the membrane treated with Alkaline Phosphatase for 1 hour
Lane 5 : Mouse hippocampus lysate
Lane 6 : Mouse hippocampus lysate then the membrane treated with Alkaline Phosphatase for 1 hour
Lysates/proteins at 15 µg per lane.
Secondary
All lanes : Goat Anti-Rabbit IgG (HRP) with minimal cross-reactivity with human IgG at 1/2000 dilution
Predicted band size: 79 kDa
Observed band size: 32-72 kDa why is the actual band size different from the predicted?
Exposure time: 3 secondsThe molecular weight observed is consistent with what has been described in the literature (PMID: 28382304, 32692785 and 30120733).
Blocking and diluting buffer: 5% NFDM/TBST
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All lanes : Anti-Tau (phospho S202) antibody [EPR2402] (ab108387) at 1/1000 dilution
Lane 1 : Human brain lysate
Lane 2 : Human brain lysate then the membrane treated with Alkaline Phosphatase for 1 hour
Lysates/proteins at 15 µg per lane.
Secondary
All lanes : Goat Anti-Rabbit IgG (HRP) with minimal cross-reactivity with human IgG at 1/2000 dilution
Predicted band size: 79 kDa
Observed band size: 32-72 kDa why is the actual band size different from the predicted?
Exposure time: 5 secondsThe molecular weight observed is consistent with what has been described in the literature (PMID: 28382304, 32692785 and 30120733).
Blocking and diluting buffer: 5% NFDM/TBST
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Dot blot analysis using 1/1000 dilution ab108387 and Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated (ab97051) secondary at 1/100000 dilution.
Blocking and diluting buffer: 5% NFDM/TBST
Lane 1: Tau non-phospho peptide
Lane 2: Tau S199 phospho peptide
Lane 3: Tau S202 phospho peptide
Lane 4: Tau S199+S202 phospho peptide
Exposure time: 3 minutes
データシートおよび資料
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SDS download
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Datasheet download
参考文献 (12)
ab108387 は 12 報の論文で使用されています。
- Xie Z et al. Microglial cathepsin E plays a role in neuroinflammation and amyloid β production in Alzheimer's disease. Aging Cell 21:e13565 (2022). PubMed: 35181976
- Siddik MAB et al. Branched-Chain Amino Acids Are Linked with Alzheimer's Disease-Related Pathology and Cognitive Deficits. Cells 11:N/A (2022). PubMed: 36359919
- Wu Y et al. Berberine Reduces Aβ42 Deposition and Tau Hyperphosphorylation via Ameliorating Endoplasmic Reticulum Stress. Front Pharmacol 12:640758 (2021). PubMed: 34349640
- Sun F et al. Upregulation of Prickle2 Ameliorates Alzheimer's Disease-Like Pathology in a Transgenic Mouse Model of Alzheimer's Disease. Front Cell Dev Biol 8:565020 (2020). PubMed: 33015060
- Neddens J et al. Constant Levels of Tau Phosphorylation in the Brain of htau Mice. Front Mol Neurosci 13:136 (2020). PubMed: 32982685