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MABN388
Sigma-AldrichAnti-phospho Tau (Thr181), clone 1E7 Antibody
Anti-phospho Tau (Thr181) antibody, clone 1E7 is an antibody against phospho Tau (Thr181) for use in western blotting.
More>>Anti-phospho Tau (Thr181) antibody, clone 1E7 is an antibody against phospho Tau (Thr181) for use in western blotting. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
The protein named Tau, or more completely microtubule-associated protein tau, and when associated with disease, neurofibrillary tangle protein, or paired helical filament tau (PHF-tau) and encoded by the human gene MAPT/MAPTL/MTBT1/TAU is an important protein involved in microtubule synthesis and stabilization. The protein is expressed in neurons and it plays a critical role in linking microtubules to the plasma membrane and in microtubule transport and signaling. Tau’s expression is largely confined to the cytosol and axons in neurons and is often highly phosphorylated particularly during cytokinesis in developing neurons and under neurological disease states such as Alzheimer’s. Phosphorylation causes detachment from microtubules and their destabilization. Phosphorylated Tau at Threonine 181, or Tau phsopho-Thr-181, is a phosphorylated form of Tau that is often associated with neuropathological disease. Its levels in CSF increase with age and phosphorylated Tau Thr181 is one of the many biomarkers used to track neurological disease progression.
LRRK2 phosphorylates Tau at Thr181, which only occurs when tubulin is associated with Tau otherwise there is no LRRK2-Tau interaction and subsequentTau phosphorylation. The LRRK2 mutant, G2019S, that shows higher PD causes elevated phosphorylation at 181 suggesting a link between the phosphorylation at this site and PD.
References
Product Information
Format
Affinity Purified
Presentation
Purified mouse monoclonal in buffer containing PBS without preservatives.
Anti-phospho Tau (Thr181) antibody, clone 1E7 is an antibody against phospho Tau (Thr181) for use in western blotting.
Key Applications
Western Blotting
Application Notes
Western Blotting Analysis: A representative lot from an independent laboratory detected phospho Tau (Thr181) in SH-SY5Y cell lysate (Kawakami, F., et al. (2012). PLoS One 7(1):e30834.).
Biological Information
Immunogen
Linear peptide corresponding to human Tau phosphorylated at Thr181.
Epitope
Phosphorylated Thr181
Clone
clone 1E7
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Species Reactivity
Mouse
Human
Species Reactivity Note
Demonstrated to react with Mouse. Predicted to react with Human based on 100% sequence homology.
~50 kDa observed. 301L transgene mice have human 0N4R isoform of TAU (383 amino acids). In SDS-PAGE, it is found as band of ~ 50 kDa. Another band of ~ 25 kDa seen could be proteolysis product of phospho Tau (Thr181) (Kawakami, F., et al. (2012). PLoS One 7(1):e30834.). Uncharacterized band(s) may be observed in some cell lysates.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in wild type and P301L transgenic mouse brain tissue lysate.
Western Blotting Analysis: 1.4 µg/mL of this antibody detected phospho Tau (Thr181) in P301L transgenic mouse brain tissue lysate, and not in wild type mouse brain tissue lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth. Kawakami, Fumitaka, et al. PLoS ONE, 7: e30834 (2012)
2011
Leucine-rich repeat kinase 2 (LRRK2), a large protein kinase containing multi-functional domains, has been identified as the causal molecule for autosomal-dominant Parkinson's disease (PD). In the present study, we demonstrated for the first time that (i) LRRK2 interacts with tau in a tubulin-dependent manner; (ii) LRRK2 directly phosphorylates tubulin-associated tau, but not free tau; (iii) LRRK2 phosphorylates tau at Thr181 as one of the target sites; and (iv) The PD-associated LRRK2 mutations, G2019S and I2020T, elevated the degree of tau-phosphorylation. These results provide direct proof that tau is a physiological substrate for LRRK2. Furthermore, we revealed that LRRK2-mediated phosphorylation of tau reduces its tubulin-binding ability. Our results suggest that LRRK2 plays an important role as a physiological regulator for phosphorylation-mediated dissociation of tau from microtubules, which is an integral aspect of microtubule dynamics essential for neurite outgrowth and axonal transport.
