Tau Monoclonal Antibody (T46) | Invitrogen 13-6400 product information

product summary

company name :

Invitrogen

other brands :

NeoMarkers, Lab Vision, Endogen, Pierce, BioSource International, Zymed Laboratories, Caltag, Molecular Probes, Research Genetics, Life Technologies, Applied Biosystems, GIBCO BRL, ABgene, Dynal, Affinity BioReagents, Nunc, Invitrogen, NatuTec, Oxoid, Richard-Allan Scientific, Arcturus, Perseptive Biosystems, Proxeon, eBioscience

product type :

antibody

product name :

Tau Monoclonal Antibody (T46)

catalog :

13-6400

quantity :

100 µg

price :

US 482

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

T46

reactivity :

human, mouse, rat, chicken, bovine, fruit fly , domestic rabbit

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation, immunohistochemistry - frozen section, western blot knockout validation

more info or order :

Invitrogen product webpage

citations: 35

Published Application/Species/Sample/Dilution	Reference
western blot knockout validation; mouse; 1:1000; loading ...; fig 1b	Hwang A, Trzeciakiewicz H, Friedmann D, Yuan C, Marmorstein R, Lee V, et al. Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members. PLoS ONE. 2016;11:e0168913 pubmed publisher
western blot; fruit fly ; 1:1000; loading ...; fig 3g	Subramanian M, Hyeon S, Das T, Suh Y, Kim Y, Lee J, et al. UBE4B, a microRNA-9 target gene, promotes autophagy-mediated Tau degradation. Nat Commun. 2021;12:3291 pubmed publisher
western blot; mouse; loading ...; fig 4a	Shin M, Vázquez Rosa E, Koh Y, Dhar M, Chaubey K, Cintrón Pérez C, et al. Reducing acetylated tau is neuroprotective in brain injury. Cell. 2021;184:2715-2732.e23 pubmed publisher
immunoprecipitation; human western blot; human; 1:1000; fig 1b	Trzeciakiewicz H, Tseng J, Wander C, Madden V, Tripathy A, Yuan C, et al. A Dual Pathogenic Mechanism Links Tau Acetylation to Sporadic Tauopathy. Sci Rep. 2017;7:44102 pubmed publisher
immunocytochemistry; rat; 1:100; loading ...; fig 4b	Atasoy İ, Dursun E, Gezen Ak D, Metin Armağan D, Ozturk M, Yilmazer S. Both secreted and the cellular levels of BDNF attenuated due to tau hyperphosphorylation in primary cultures of cortical neurons. J Chem Neuroanat. 2017;80:19-26 pubmed publisher
immunocytochemistry; human; 1:200; fig 2c western blot; human; 1:1000; fig 2e	LÃ³pez de Maturana R, Lang V, Zubiarrain A, Sousa A, VÃ¡zquez N, Gorostidi A, et al. Mutations in LRRK2 impair NF-ÎºB pathway in iPSC-derived neurons. J Neuroinflammation. 2016;13:295 pubmed
western blot; mouse; 1:1000; fig 7	Peng Y, Kim M, Hullinger R, O Riordan K, Burger C, Pehar M, et al. Improved proteostasis in the secretory pathway rescues Alzheimer's disease in the mouse. Brain. 2016;139:937-52 pubmed publisher
immunohistochemistry; human; 1:500; fig 6 western blot; human; fig 2	Taniguchi Watanabe S, Arai T, Kametani F, Nonaka T, Masuda Suzukake M, Tarutani A, et al. Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tau. Acta Neuropathol. 2016;131:267-280 pubmed publisher
western blot; human	Corbel C, Zhang B, Le Parc A, Baratte B, Colas P, Couturier C, et al. Tamoxifen inhibits CDK5 kinase activity by interacting with p35/p25 and modulates the pattern of tau phosphorylation. Chem Biol. 2015;22:472-482 pubmed publisher
western blot; human; 1:1000	Takeuchi R, Toyoshima Y, Tada M, Tanaka H, Shimizu H, Shiga A, et al. Globular Glial Mixed Four Repeat Tau and TDP-43 Proteinopathy with Motor Neuron Disease and Frontotemporal Dementia. Brain Pathol. 2016;26:82-94 pubmed publisher
western blot; human; fig 1	Melis V, Zabke C, Stamer K, Magbagbeolu M, Schwab K, Marschall P, et al. Different pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer's disease and frontotemporal lobar degeneration. Cell Mol Life Sci. 2015;72:2199-222 pubmed publisher
	Murie M, Peng Y, Rigby M, Dieterich I, Farrugia M, Endresen A, et al. ATase inhibition rescues age-associated proteotoxicity of the secretory pathway. Commun Biol. 2022;5:173 pubmed publisher
	Wu R, Li L, Shi R, Zhou Y, Jin N, Gu J, et al. Dephosphorylation Passivates the Seeding Activity of Oligomeric Tau Derived From Alzheimer's Brain. Front Mol Neurosci. 2021;14:631833 pubmed publisher
	Desale S, Chinnathambi S. α- Linolenic acid modulates phagocytosis and endosomal pathways of extracellular Tau in microglia. Cell Adh Migr. 2021;15:84-100 pubmed publisher
	Das R, Balmik A, Chinnathambi S. Melatonin Reduces GSK3β-Mediated Tau Phosphorylation, Enhances Nrf2 Nuclear Translocation and Anti-Inflammation. ASN Neuro. 2020;12:1759091420981204 pubmed publisher
	Shimonaka S, Matsumoto S, Elahi M, Ishiguro K, Hasegawa M, Hattori N, et al. Asparagine residue 368 is involved in Alzheimer's disease tau strain-specific aggregation. J Biol Chem. 2020;295:13996-14014 pubmed publisher
	Gorantla N, Das R, Chidambaram H, Dubey T, Mulani F, Thulasiram H, et al. Basic Limonoid modulates Chaperone-mediated Proteostasis and dissolve Tau fibrils. Sci Rep. 2020;10:4023 pubmed publisher
	Das R, Balmik A, Chinnathambi S. Phagocytosis of full-length Tau oligomers by Actin-remodeling of activated microglia. J Neuroinflammation. 2020;17:10 pubmed publisher
	Tan R, Lam A, Tan T, Han J, Nowakowski D, Vershinin M, et al. Microtubules gate tau condensation to spatially regulate microtubule functions. Nat Cell Biol. 2019;21:1078-1085 pubmed publisher
	Gao L, Huang S, Zhang H, Hua W, Xin S, Cheng L, et al. Suppression of glioblastoma by a drug cocktail reprogramming tumor cells into neuronal like cells. Sci Rep. 2019;9:3462 pubmed publisher
	Dominy S, LYNCH C, Ermini F, Benedyk M, Marczyk A, Konradi A, et al. Porphyromonas gingivalis in Alzheimer's disease brains: Evidence for disease causation and treatment with small-molecule inhibitors. Sci Adv. 2019;5:eaau3333 pubmed publisher
	Audrain M, Haure Mirande J, Wang M, Kim S, Fanutza T, Chakrabarty P, et al. Integrative approach to sporadic Alzheimer's disease: deficiency of TYROBP in a tauopathy mouse model reduces C1q and normalizes clinical phenotype while increasing spread and state of phosphorylation of tau. Mol Psychiatry. 2018;: pubmed publisher
	Zhang F, Zhong R, Qi H, Li S, Cheng C, Liu X, et al. Impacts of Acute Hypoxia on Alzheimer's Disease-Like Pathologies in APPswe/PS1dE9 Mice and Their Wild Type Littermates. Front Neurosci. 2018;12:314 pubmed publisher
	Zhou Y, Shi J, Chu D, Hu W, Guan Z, Gong C, et al. Relevance of Phosphorylation and Truncation of Tau to the Etiopathogenesis of Alzheimer's Disease. Front Aging Neurosci. 2018;10:27 pubmed publisher
	Wang B, Tanaka K, Ji B, Ono M, Fang Y, Ninomiya Y, et al. Total body 100-mGy X-irradiation does not induce Alzheimer's disease-like pathogenesis or memory impairment in mice. J Radiat Res. 2014;55:84-96 pubmed publisher
	Chatterjee S, Sang T, Lawless G, Jackson G. Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model. Hum Mol Genet. 2009;18:164-77 pubmed publisher
	Guo J, Arai T, Miklossy J, McGeer P. Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease. Proc Natl Acad Sci U S A. 2006;103:1953-8 pubmed
	Mendes S, Henkemeyer M, Liebl D. Multiple Eph receptors and B-class ephrins regulate midline crossing of corpus callosum fibers in the developing mouse forebrain. J Neurosci. 2006;26:882-92 pubmed
	Yu W, Ko M, Yanagisawa K, Michikawa M. Neurodegeneration in heterozygous Niemann-Pick type C1 (NPC1) mouse: implication of heterozygous NPC1 mutations being a risk for tauopathy. J Biol Chem. 2005;280:27296-302 pubmed
	Arai T, Guo J, McGeer P. Proteolysis of non-phosphorylated and phosphorylated tau by thrombin. J Biol Chem. 2005;280:5145-53 pubmed
	Zamora Leon S, Bresnick A, Backer J, Shafit Zagardo B. Fyn phosphorylates human MAP-2c on tyrosine 67. J Biol Chem. 2005;280:1962-70 pubmed
	Rissman R, Poon W, Blurton Jones M, Oddo S, Torp R, Vitek M, et al. Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J Clin Invest. 2004;114:121-30 pubmed
	Clark L, Poorkaj P, Wszolek Z, Geschwind D, Nasreddine Z, Miller B, et al. Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17. Proc Natl Acad Sci U S A. 1998;95:13103-7 pubmed
	Reed L, Schmidt M, Wszolek Z, Balin B, Soontornniyomkij V, Lee V, et al. The neuropathology of a chromosome 17-linked autosomal dominant parkinsonism and dementia ("pallido-ponto-nigral degeneration"). J Neuropathol Exp Neurol. 1998;57:588-601 pubmed
	Lieberman A, Trojanowski J, Lee V, Balin B, Ding X, Greenberg J, et al. Cognitive, neuroimaging, and pathological studies in a patient with Pick's disease. Ann Neurol. 1998;43:259-65 pubmed

product information

Product Type :

Antibody

Product Name :

Tau Monoclonal Antibody (T46)

Catalog # :

13-6400

Quantity :

100 µg

Price :

US 482

Clonality :

Monoclonal

Purity :

purified

Host :

Mouse

Reactivity :

Bovine, Chicken, Human, Mouse, Rabbit, Rat, Xenopus laevis

Applications :

ELISA: 0.1-0.5 µg/mL, Immunocytochemistry: 1:250, Immunohistochemistry (Frozen): Assay-dependent, Immunomicroscopy: Assay-dependent, Immunoprecipitation: 2-5 µg, Western Blot: 0.5-1.0 µg/mL

Species :

Bovine, Chicken, Human, Mouse, Rabbit, Rat, Xenopus laevis

Clone :

T46

Isotype :

IgG1

Storage :

-20°C

Description :

Tau is a neuronal microtubule-associated protein found predominantly on axons. The function of Tau is to promote tubulin polymerization and stabilize microtubules. The C-terminus binds axonal microtubules while the N- terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton while the longer isoforms may preferentially play a role in its stabilization. In its hyper-phosphorylated form, Tau is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer's diseases (AD) brain. Hyper-phosphorylation impairs the microtubule binding function of Tau, resulting in the destabilization of microtubules in AD brains, ultimately leading to the degeneration of the affected neurons. Numerous serine/threonine kinases phosphorylate Tau, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II. Hyper-phosphorylated Tau is found in neurofibrillary lesions in a range and other central nervous system disorders such as Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.

Immunogen :

Bovine Tau.

Format :

Liquid

Applications w/Dilutions :

ELISA: 0.1-0.5 µg/mL, Immunocytochemistry: 1:250, Immunohistochemistry (Frozen): Assay-dependent, Immunomicroscopy: Assay-dependent, Immunoprecipitation: 2-5 µg, Western Blot: 0.5-1.0 µg/mL

Aliases :

AI413597; AW045860; DDPAC; FLJ31424; FTDP17; FTDP-17; G protein beta1/gamma2 subunit-interacting factor 1; map tau; Mapt; MAPTL; MGC138549; microtubule associated protein tau; microtubule-associated protein tau; microtubule-associated protein tau, isoform 4; microtubules; MSTD; Mtapt; MTBT1; MTBT2; Neurofibrillary tangle protein; neurofibrillary tangles; Neuronal Marker; paired helical filament-tau; PHFtau; PHF-tau; PPND; PPP1R103; protein phosphatase 1, regulatory subunit 103; pTau; RNPTAU; Tau; Tau microtubule-associated protein; tau protein; Tau-4; Tau5; Unknown (protein for MGC:134287)

more info or order :

Invitrogen product webpage