T9450
Anti-Tau antibody, Mouse monoclonal
clone Tau46, purified from hybridoma cell culture
Synonyme(s) :
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
Produits recommandés
Source biologique
mouse
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
purified immunoglobulin
Type de produit anticorps
primary antibodies
Clone
Tau46, monoclonal
Forme
buffered aqueous solution
Espèces réactives
bovine, rat, human, mouse
Conditionnement
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
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)
Description générale
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.
Spécificité
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.
Immunogène
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)
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.
Actions biochimiques/physiologiques
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.
Forme physique
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Clause de non-responsabilité
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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Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Les clients ont également consulté
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
Lina Adwan et al.
Journal of neurochemistry, 133(2), 266-272 (2014-10-04)
Tau and its aggregates are linked to the pathology of Alzheimer's disease (AD) and other tauopathies and, therefore, are explored as therapeutic targets for such disorders. Tau belongs to a family of microtubule-associated proteins that promote microtubule assembly. When hyperphosphorylated
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
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
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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