Skip to Content
Merck
CN
All Photos(1)

Documents

MABN388

Sigma-Aldrich

Anti-phospho Tau (Thr181), clone 1E7 Antibody

clone 1E7, from mouse, purified by affinity chromatography

Synonym(s):

Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, F-tau

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

1E7, monoclonal

purified by

affinity chromatography

species reactivity

mouse

species reactivity (predicted by homology)

human (based on 100% sequence homology)

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

phosphorylation (pThr181)

Gene Information

human ... MAPT(4137)

Related Categories

General description

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.

Immunogen

Epitope: Phosphorylated Thr181
Linear peptide corresponding to human Tau phosphorylated at Thr181.

Application

Anti-phospho Tau (Thr181) antibody, clone 1E7 is an antibody against phospho Tau (Thr181) for use in western blotting.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
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.).

Quality

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.

Target description

~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.

Physical form

Affinity purified
Purified mouse monoclonal in buffer containing PBS without preservatives.

Storage and Stability

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.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

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.

Not finding the right product?  

Try our Product Selector Tool.

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Lucia Buccarello et al.
Oncotarget, 8(47), 83038-83051 (2017-11-16)
Recently a range of ocular manifestations such as retinal and lens amyloid-beta accumulation and retinal nerve fiber layer loss have been proposed as potential biomarkers in Alzheimer disease (AD). The TgCRND8 mouse model of AD exhibits age-dependent amyloid β (Aβ)
Nongnuch Singrang et al.
International journal of molecular sciences, 25(10) (2024-05-25)
Stroke and Alzheimer's disease (AD) are prevalent age-related diseases; however, the relationship between these two diseases remains unclear. In this study, we aimed to investigate the ability of melatonin, a hormone produced by the pineal gland, to alleviate the effects
Beatrice Terni et al.
Journal of Alzheimer's disease : JAD, 46(2), 461-469 (2015-09-25)
Previous studies have shown that metalloproteinases (MMPs) participate in the clearance of amyloid-β (Aβ) in Alzheimer's disease (AD); MMP2 and MMP3 cleave soluble Aβ, and both MMP9 and MT1-MMP are able to degrade soluble and fibrillar forms of Aβ. The

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service