Tau Monoclonal Antibody (BT2) | Invitrogen MN1010 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 (BT2)

catalog :

MN1010

quantity :

100 µg

price :

US 412

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

BT2

reactivity :

human, mouse, rat, bovine

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, western blot knockout validation

more info or order :

Invitrogen product webpage

citations: 24

Published Application/Species/Sample/Dilution	Reference
western blot; mouse western blot knockout validation; human; 1:1000; tbl 1 immunocytochemistry; human; 1:100; tbl 2	Ercan E, Eid S, Weber C, Kowalski A, Bichmann M, Behrendt A, et al. A validated antibody panel for the characterization of tau post-translational modifications. Mol Neurodegener. 2017;12:87 pubmed publisher
ELISA; human; loading ...; fig 5a	Ercan Herbst E, Ehrig J, Schöndorf D, Behrendt A, Klaus B, Gomez Ramos B, et al. A post-translational modification signature defines changes in soluble tau correlating with oligomerization in early stage Alzheimer's disease brain. Acta Neuropathol Commun. 2019;7:192 pubmed publisher
ELISA; mouse; loading ...; fig 4a	Croft C, Wade M, Kurbatskaya K, Mastrandreas P, Hughes M, Phillips E, et al. Membrane association and release of wild-type and pathological tau from organotypic brain slice cultures. Cell Death Dis. 2017;8:e2671 pubmed publisher
ELISA; human	Sankaranarayanan S, Barten D, Vana L, Devidze N, Yang L, Cadelina G, et al. Passive immunization with phospho-tau antibodies reduces tau pathology and functional deficits in two distinct mouse tauopathy models. PLoS ONE. 2015;10:e0125614 pubmed publisher
ELISA; human; fig 7	Song L, Lu S, Ouyang X, Melchor J, Lee J, Terracina G, et al. Analysis of tau post-translational modifications in rTg4510 mice, a model of tau pathology. Mol Neurodegener. 2015;10:14 pubmed publisher
western blot; rat; 1:1000	Santos R, Correia S, Alves M, Oliveira P, Cardoso S, Carvalho C, et al. Insulin therapy modulates mitochondrial dynamics and biogenesis, autophagy and tau protein phosphorylation in the brain of type 1 diabetic rats. Biochim Biophys Acta. 2014;1842:1154-66 pubmed publisher
western blot; rat; 1:2000	Rahman A, Khan K, Al Khaledi G, Khan I, Attur S. Early postnatal lead exposure induces tau phosphorylation in the brain of young rats. Acta Biol Hung. 2012;63:411-25 pubmed publisher
western blot; human	Karch C, Jeng A, Goate A. Calcium phosphatase calcineurin influences tau metabolism. Neurobiol Aging. 2013;34:374-86 pubmed publisher
western blot; rat; 1:2000	Rahman A, Khan K, Al Khaledi G, Khan I, Al Shemary T. Over activation of hippocampal serine/threonine protein phosphatases PP1 and PP2A is involved in lead-induced deficits in learning and memory in young rats. Neurotoxicology. 2012;33:370-83 pubmed publisher
western blot; human western blot; mouse	Yamada K, Cirrito J, Stewart F, Jiang H, Finn M, Holmes B, et al. In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice. J Neurosci. 2011;31:13110-7 pubmed publisher
ELISA; human; 0.1 ug/ml	Wu G, Sankaranarayanan S, Hsieh S, Simon A, Savage M. Decrease in brain soluble amyloid precursor protein ? (sAPP?) in Alzheimer's disease cortex. J Neurosci Res. 2011;89:822-32 pubmed publisher
western blot; mouse; 1:3,000	Koike M, Garcia F, Kitazawa M, Green K, LaFerla F. Long term changes in phospho-APP and tau aggregation in the 3xTg-AD mice following cerebral ischemia. Neurosci Lett. 2011;495:55-9 pubmed publisher
western blot; mouse; 1:100 western blot; human; 1:100	Perreault S, Bousquet O, Lauzon M, Paiement J, Leclerc N. Increased association between rough endoplasmic reticulum membranes and mitochondria in transgenic mice that express P301L tau. J Neuropathol Exp Neurol. 2009;68:503-14 pubmed publisher
immunohistochemistry; mouse; 1:200	Mastrangelo M, Bowers W. Detailed immunohistochemical characterization of temporal and spatial progression of Alzheimer's disease-related pathologies in male triple-transgenic mice. BMC Neurosci. 2008;9:81 pubmed publisher
immunohistochemistry; mouse; 1:500	Menendez J, Rodriguez Navarro J, Solano R, Casarejos M, Rodal I, Guerrero R, et al. Suppression of Parkin enhances nigrostriatal and motor neuron lesion in mice over-expressing human-mutated tau protein. Hum Mol Genet. 2006;15:2045-58 pubmed
	Latina V, Giacovazzo G, Cordella F, Balzamino B, Micera A, Varano M, et al. Systemic delivery of a specific antibody targeting the pathological N-terminal truncated tau peptide reduces retinal degeneration in a mouse model of Alzheimer's Disease. Acta Neuropathol Commun. 2021;9:38 pubmed publisher
	Triana Baltzer G, Van Kolen K, Theunis C, Moughadam S, Slemmon R, Mercken M, et al. Development and Validation of a High Sensitivity Assay for Measuring p217 + tau in Cerebrospinal Fluid. J Alzheimers Dis. 2020;77:1417-1430 pubmed publisher
	Lin Y, Rajamohamedsait H, Sandusky Beltran L, Gamallo Lana B, Mar A, Sigurdsson E. Chronic PD-1 Checkpoint Blockade Does Not Affect Cognition or Promote Tau Clearance in a Tauopathy Mouse Model. Front Aging Neurosci. 2019;11:377 pubmed publisher
	Chan H, Xu D, Ho S, He D, Wong M, Li H. Highly sensitive quantification of Alzheimer's disease biomarkers by aptamer-assisted amplification. Theranostics. 2019;9:2939-2949 pubmed publisher
	Guix F, Corbett G, Cha D, Mustapic M, Liu W, Mengel D, et al. Detection of Aggregation-Competent Tau in Neuron-Derived Extracellular Vesicles. Int J Mol Sci. 2018;19: pubmed publisher
	Piccardo P, King D, Brown D, Barron R. Variable tau accumulation in murine models with abnormal prion protein deposits. J Neurol Sci. 2017;383:142-150 pubmed publisher
	Huang R, Iacob R, Sankaranarayanan S, Yang L, Ahlijanian M, Tao L, et al. Probing Conformational Dynamics of Tau Protein by Hydrogen/Deuterium Exchange Mass Spectrometry. J Am Soc Mass Spectrom. 2018;29:174-182 pubmed publisher
	Meredith J, Sankaranarayanan S, Guss V, Lanzetti A, Berisha F, Neely R, et al. Characterization of novel CSF Tau and ptau biomarkers for Alzheimer's disease. PLoS ONE. 2013;8:e76523 pubmed publisher
	Nashmi R, Dickinson M, McKinney S, Jareb M, Labarca C, Fraser S, et al. Assembly of alpha4beta2 nicotinic acetylcholine receptors assessed with functional fluorescently labeled subunits: effects of localization, trafficking, and nicotine-induced upregulation in clonal mammalian cells and in cultured midbrain neurons. J Neurosci. 2003;23:11554-67 pubmed

product information

Product Type :

Antibody

Product Name :

Tau Monoclonal Antibody (BT2)

Catalog # :

MN1010

Quantity :

100 µg

Price :

US 412

Clonality :

Monoclonal

Purity :

protein A

Host :

Mouse

Reactivity :

Bovine, Human, Non-human primate, Rat

Applications :

ELISA: 2-10 µg/mL, Western Blot: 1:500

Species :

Bovine, Human, Non-human primate, Rat

Clone :

BT2

Isotype :

IgG1, kappa

Storage :

-20° C, Avoid Freeze/Thaw Cycles

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 :

Purified bovine Tau

Format :

Liquid

Applications w/Dilutions :

ELISA: 2-10 µg/mL, Western Blot: 1:500

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