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Merck

T9450

Sigma-Aldrich

Anti-Tau antibody, Mouse monoclonal

clone Tau46, purified from hybridoma cell culture

Sinónimos:

Anti-DDPAC, Anti-FTDP-17, Anti-MAPTL, Anti-MSTD, Anti-MTBT1, Anti-MTBT2, Anti-PPND, Anti-PPP1R103, Anti-TAU, Anti-tau-40

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

Tau46, monoclonal

form

buffered aqueous solution

species reactivity

bovine, rat, human, mouse

packaging

antibody small pack of 25 μL

concentration

~2 mg/mL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.5-1 μg/mL using mouse brain extract

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)

General description

Tau (τ), also known as MAPT (microtubule associated protein tau), is encoded by the gene mapped to human chromosome 17q21.3. It is highly expressed in neurons, but is most prominent in axons.
Tau is a family of microtubule-associated proteins thought to regulate the stability and organization of microtubules in neuronal cells. The tau protein family is derived from alternative mRNA splice variants that originate from a single gene, and result in mature proteins that vary in size from 352 to 441 amino acids (45 to 60 kDa). Tau loses microtubule-binding activity and aggregates into paired helical filaments (PHFs) in neurodegenerative disorders. PHFs are the basic structural components of neurofibrillary tangles (NFTs). NFT accumulation correlates with the clinical progression of Alzheimer′s disease. Phosphorylation can affect the functional properties of tau and hyperphosphorylation of tau may result in the loss of tau′s microtubule binding activity and the formation of the insoluble aggregates. Hyperphosphorylation and nonenzymatic glycosylation are posttranslational modifications detected in PHF-tau, and numerous sites of hyperphosphorylation of both normal and PHF-tau have been identified.

Specificity

Mouse monoclonal clone Tau46 anti-Tau antibody recognizes bovine, rat, human, and mouse Tau (approx. 45 to 60 kDa). The antibody recognizes a phosphorylation-independent epitope in amino acids 404-441 (human). The antibody recognizes all six isoforms of Tau and may cross react with MAP2 protein.

Immunogen

bovine Tau.

Application

Anti-Tau antibody, Mouse monoclonal has been used in western blotting.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Mouse monoclonal clone Tau46 anti-Tau antibody is useful in ELISA, immunoblotting, immunogold labeling, immunopreciptation as well as immunohistochemistry. It is used as a probe to determine the presence and roles of Tau protein in the regulation of the stability and organization of microtubules in neuronal cells.

Biochem/physiol Actions

Tau (τ) plays an essential role in the assembly and maintenance of microtubule structure. Deletion of tau (τ) results in developmental delay and learning disability. The gene expression is associated with the development of Alzheimer′s disease (AD). Genetic variation in τ gene increases the risk of susceptibility to the sporadic tauopathies, progressive supranuclear palsy (PSP) and corticobasal degeneration.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Ming-Jang Chiu et al.
Frontiers in aging neuroscience, 9, 51-51 (2017-03-23)
Using an ultra-sensitive technique, an immunomagnetic reduction assay, the plasma tau level can be measured to a limit of quantification of pg/ml. In total 126 cognitively normal middle-aged and older adults (45-95 years old) were recruited. The plasma tau levels
Jeffrey J Iliff et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 34(49), 16180-16193 (2014-12-05)
Traumatic brain injury (TBI) is an established risk factor for the early development of dementia, including Alzheimer's disease, and the post-traumatic brain frequently exhibits neurofibrillary tangles comprised of aggregates of the protein tau. We have recently defined a brain-wide network
Shieh-Yueh Yang et al.
Scientific reports, 7(1), 9304-9304 (2017-08-26)
Immunomagnetic reduction (IMR), which involves the use of antibody-functionalized magnetic nanoparticles to specifically label target biomarkers, was utilized to develop an assay for total tau protein in human plasma. The analytic properties of the IMR assay on tau protein were
Lih-Fen Lue et al.
Neurology and therapy, 6(Suppl 1), 25-36 (2017-07-25)
The utility of the levels of amyloid beta (Aβ) peptide and tau in blood for diagnosis, drug development, and assessment of clinical trials for Alzheimer's disease (AD) has not been established. The lack of availability of ultra-sensitive assays is one
Ling-Yun Fan et al.
Frontiers in aging neuroscience, 10, 175-175 (2018-07-04)
Background: Neuritic plaques and neurofibrillary tangles are the pathological hallmarks of Alzheimer's disease (AD), while the role of brain amyloid deposition in the clinical manifestation or brain atrophy remains unresolved. We aimed to explore the relation between brain amyloid deposition

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