Anti-Tau (phospho-T205) Antibody (A27476)

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Rabbit polyclonal antibody to Tau (phospho-T205) for WB.

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Anti-Tau Antibody [5B10]

Mouse monoclonal (5B10) antibody to Tau for WB and ICC/IF.

Specifications

Name

Anti-Tau (phospho-T205) Antibody

Description

Rabbit polyclonal antibody to Tau (phospho-T205)

Specificity

p-Tau (T205) pAb detects endogenous levels of Tau only when phosphorylated at Thr522, isoforms Tau-3 and isoforms Tau-4 phosphorylated at Thr205, and other isoforms phosphorylated at the corresponding Site.

Applications

Reactivity

Human, Mouse, Rat

Immunogen

Synthetic phosphopeptide derived from human isoforms Tau-4 around the phosphorylation site of Threonine 205.

Host

Rabbit

Clonality

Polyclonal

Conjugate

Unconjugated

Molecular Weight

50 to 80 kDa

Purity

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Product Form

1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.

Synonyms

AI413597, AW045860, DDPAC, FLJ31424, FTDP 17, G protein beta1/gamma2 subunit interacting factor 1, MAPT, MAPTL, MGC134287, MGC138549, MGC156663, Microtubule associated protein tau, Microtubule associated protein tau isoform 4, Microtubule-associated protein tau, MSTD, Mtapt, MTBT1, MTBT2, Neurofibrillary tangle protein, Paired helical filament tau, Paired helical filament-tau, PHF tau, PHF-tau, PPND, PPP1R103, Protein phosphatase 1, regulatory subunit 103, pTau, RNPTAU, Tauopathy and respiratory failure, included, TAU_HUMAN

Suitable Secondaries

Disclaimer

This product is for research use only. It is not intended for diagnostic or therapeutic use.

Scientific Validation Data (2)

Figure 1: Anti-Tau (phospho-T205) Antibody (A27476)

For details please refer to datasheet.

Figure 2: Anti-Tau (phospho-T205) Antibody (A27476)

For details please refer to datasheet.

Citations (5)

SCM-198 inhibits microglial overactivation and attenuates Aβ(1-40)-induced cognitive impairments in rats via JNK and NF-кB pathways.

(2)

References: Anti-Tau (phospho-T205) Antibody (A27476)

Abstract:

BACKGROUND:

Neuroinflammation mediated by overactivated microglia plays a key role in many neurodegenerative diseases, including Alzheimer's disease (AD). In this study, we investigated for the first time the anti-neuroinflammatory effects and possible mechanisms of SCM-198 (an alkaloid extracted from Herbaleonuri), which was previously found highly cardioprotective, both in vitro and in vivo.

METHODS:

For in vitro experiments, lipopolysaccharide (LPS) or β-amyloid(1-40) (Aβ(1-40)) was applied to induce microglial overactivation. Proinflammatory mediators were measured and activations of NF-κB and mitogen-activated protein kinases' (MAPKs) pathways were investigated. Further protective effect of SCM-198 was evaluated in microglia-neuron co-culture assay and Sprague-Dawley (SD) rats intrahippocampally-injected with Aβ(1-40).

RESULTS:

SCM-198 reduced expressions of nitric oxide (NO), TNF-α, IL-1β and IL-6 possibly via, at least partially, inhibiting c-Jun N-terminal kinase (JNK) and NF-κB signaling pathways in microglia. Co-culture assay showed that activated microglia pretreated with SCM-198 led to less neuron loss and decreased phosphorylation of tau and extracellular signal-regulated kinase (ERK) in neurons. Besides, SCM-198 also directly protected against Aβ(1-40)-induced neuronal death and lactate dehydrogenase (LDH) release in primary cortical neurons. For in vivo studies, SCM-198 significantly enhanced cognitive performances of rats 12 days after intrahippocampal injections of aged Aβ(1-40) peptides in the Morris water maze (MWM), accompanied by less hippocampal microglial activation, decreased synaptophysin loss and phosphorylation of ERK and tau. Co-administration of donepezil and SCM-198 resulted in a slight cognitive improvement in SD rats 50 days after intrahippocampal injections of aged Aβ(1-40) peptides as compared to only donepezil or SCM-198 treated group.

CONCLUSIONS:

Our findings are the first to report that SCM-198 has considerable anti-neuroinflammatory effects on inhibiting microglial overactivation and might become a new potential drug candidate for AD therapy in the future.

UCH-L1 Inhibition Decreases the Microtubule-Binding Function of Tau Protein.

References: Anti-Tau (phospho-T205) Antibody (A27476)

Abstract:

Ubiquitin C-terminal hydrolase L1 (UCH-L1) is critical for protein degradation and free ubiquitin recycling. In Alzheimer's disease brains, UCH-L1 is negatively related to neurofibrillary tangles whose major component is hyperphosphorylated tau protein, but the direct action of UCH-L1 on tau has not been reported. In the current study, mouse neuroblastoma Neuro2a (N2a) cells were treated by the different concentrations of UCH-L1 inhibitor LDN (2.5, 5 and 10 μM) to inhibit the hydrolase activity of UCH-L1. In addition, we also used UCH-L1 siRNA to treat the HEK293/tau441 cells to decrease the expression of UCH-L1. After LDN and UCH-L1 siRNA treatment, we used immunofluorescence, immunoprecipitation, and tau-microtubule binding assay to measure the microtubule-binding ability and post-translational modifications of tau protein. All the results presented that both inhibition of the activity and expression of UCH-L1 induced the decreased microtubule-binding ability and increased phosphorylation of tau protein. Abnormal aggregation and ubiquitination of tau protein was also observed after UCH-L1 inhibition. The above results suggested that aggregation of tau protein might be devoted to the abnormal post-translational modifications of tau protein. Our study first indicates that dysfunction of UCH-L1 most likely affected normal biological function of tau protein through decreasing degradation of ubiquitinated and hyperphosphorylated tau.

UCH-L1 inhibition involved in CREB dephosphorylation in hippocampal slices.

References: Anti-Tau (phospho-T205) Antibody (A27476)

Abstract:

Ubiquitin C-terminal hydrolase L1 (UCH-L1) is abundantly expressed in the brain and is critical for the normal function of synapses. cAMP response element binding protein (CREB) is a transcription factor which initiates the expression of proteins that related to the regulation of synaptic plasticity and memory function. Studies have shown that UCH-L1 can influence the expression and activity of CREB, but the underlying mechanisms remain unclear. In this study, we used UCH-L1 inhibitor LDN to treat mice hippocampal slices and found that UCH-L1 inhibition caused the dephosphorylation of CREB at Ser133 site. Meanwhile, hyperphosphorylation of microtubule-associated protein tau; increased expression of synaptic protein components of PSD-95 and synapsin-1, and decreased activity of tyrosine kinase Fyn were observed after UCH-L1 inhibition. Moreover, all these alternations have an influence on the normal function of N-methyl-D-aspartate (NMDA) receptor NR2B subunit which is likely to result in the dephosphorylation of CREB. We also found that LDN treatment mediated protein kinase A (PKA) deactivation was involved in the dephosphorylation of CREB. Thus, our study introduces a novel possible mechanism for elaborating the effects of UCH-L1 inhibition on the CREB activity and the implicated signaling pathways.

Self-assembling nanofibers alter the processing of amyloid precursor protein in a transgenic mouse model of Alzheimer's disease.

References: Anti-Tau (phospho-T205) Antibody (A27476)

Abstract:

BACKGROUND:

Alzheimer's disease (AD) is one of the most common dementia, which is not effectively cured to date. Amyloid-beta (Abeta) deposition cascade and disintegrity of brain extracellular matrix (ECM) scaffold attribute to the progress of AD. Thus, it maybe an effective way to treat AD by altering the processing of amyloid precursor protein (APP) and regaining the integrity of ECM. The peptide amphiphile (PA) with a laminin epitope isoleucine-lysine-valine-alanine-valine (IKVAV) (IKVAV-PA) can be trigged into ECM in vivo. In addition, IKVAV-PA could significantly improve cognitive impairment with remarkable increase of endoneurogensis in the hippocampus, as well as reduction of burden of amyloid plaque in the brain.

METHODS:

We used heterozygous AbetaPPswe/PS1dE9 double transgenic mice as the animal model of AD. After 1 week of initial stereotaxic administration into bilateral hippocampus, the mice were subjected to the Morris Water Maze (MWM) test. At the end of MWM test, immunohistochemical staining, Western blot and real-time polymerase chain reaction (PCR) were performed in mice.

RESULTS:

Here we showed that IKVAV-PA significantly improved cognitive impairment accompanying with reducing the burden of Abeta plaques, as well as the levels of soluble Abeta1-40 and Abeta1-42 in the cortex and hippocampus after 2 weeks of initial administration into bilateral hippocampus. Further examination demonstrated that IKVAV-PA also altered the processing of APP via inhibiting the gene expression of beta-secretase (BACE1), as well as improving the gene expression of insulin-degrading enzyme (IDE) and neprilysin (NEP).

CONCLUSION:

Our data suggest that IKVAV-PA may serve as an alternative therapeutic intervention for treating the learning and memory losses in AD.

Effect of chronic noise exposure on expression of N-methyl-D-aspartic acid receptor 2B and Tau phosphorylation in hippocampus of rats.

References: Anti-Tau (phospho-T205) Antibody (A27476)

Abstract:

OBJECTIVE:

To study the effect of chronic noise exposure on expression of N-methyl-D-aspartic acid receptor 2B (NR2B) and tau phosphorylation in hippocampus of rats.

METHODS:

Twenty-four male SD rats were divided in control group and chronic noise exposure group. NR2B expression and tau phosphorylation in hippocampus of rats were detected after chronic noise exposure (100 dB SPL white noise, 4 h/d×30d) and their mechanisms underlying neuronal apoptosis in hippocampus of rats with TUNEL staining.

RESULTS:

The NR2B expression decreased significantly after chronic noise exposure which resulted in tau hyperphosphorylation and neural apoptosis in hippocampus of rats. Immunohistochemistry showed that the tau hyperphosphorylation was most prominent in dentate gyrus (DG) and CA1 region of rat hippocampus.

CONCLUSION:

The abnormality of neurotransmitter system, especially Glu and NR2B containing NMDA receptor, and tau hyperphosphorylation in hippocampus of rats, may play a role in chronic noise-induced neural apoptosis and cognition impairment.