Phospho-Tau (Ser199) Polyclonal Antibody | Invitrogen 44-734G 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 :

Phospho-Tau (Ser199) Polyclonal Antibody

catalog :

44-734G

quantity :

100 µL

price :

US 446

clonality :

polyclonal

host :

domestic rabbit

conjugate :

nonconjugated

antigen modification :

phosphorylated

reactivity :

human, mouse, rat, dogs

application :

western blot, immunohistochemistry, immunocytochemistry, immunohistochemistry - paraffin section

more info or order :

Invitrogen product webpage

citations: 26

Published Application/Species/Sample/Dilution	Reference
western blot; rat; 1:2000; loading ...; fig 2a	Zheng J, Tian N, Liu F, Zhang Y, Su J, Gao Y, et al. A novel dephosphorylation targeting chimera selectively promoting tau removal in tauopathies. Signal Transduct Target Ther. 2021;6:269 pubmed publisher
western blot; mouse; loading ...; fig 1a	Wu D, Gao D, Yu H, Pi G, Xiong R, Lei H, et al. Medial septum tau accumulation induces spatial memory deficit via disrupting medial septum-hippocampus cholinergic pathway. Clin Transl Med. 2021;11:e428 pubmed publisher
immunocytochemistry; human; loading ...; fig 1d western blot; human; 1:1000; loading ...; fig s5b	Tseng J, Xie L, Song S, Xie Y, Allen L, Ajit D, et al. The Deacetylase HDAC6 Mediates Endogenous Neuritic Tau Pathology. Cell Rep. 2017;20:2169-2183 pubmed publisher
western blot; mouse; loading ...; fig 3a	Zimova I, Brezovakova V, Hromádka T, Weisová P, Cubinkova V, Valachova B, et al. Human Truncated Tau Induces Mature Neurofibrillary Pathology in a Mouse Model of Human Tauopathy. J Alzheimers Dis. 2016;54:831-43 pubmed publisher
western blot; mouse; fig 8	Winston C, NoÃ«l A, Neustadtl A, Parsadanian M, Barton D, Chellappa D, et al. Dendritic Spine Loss and Chronic White Matter Inflammation in a Mouse Model of Highly Repetitive Head Trauma. Am J Pathol. 2016;186:552-67 pubmed publisher
western blot; dogs; 1:1000; fig 7 western blot; mouse western blot; human western blot; rat	Smolek T, Madari A, Farbáková J, Kandrac O, Jadhav S, Cente M, et al. Tau hyperphosphorylation in synaptosomes and neuroinflammation are associated with canine cognitive impairment. J Comp Neurol. 2016;524:874-95 pubmed publisher
	Lei L, Feng J, Wu G, Wei Z, Wang J, Zhang B, et al. HIF-1α Causes LCMT1/PP2A Deficiency and Mediates Tau Hyperphosphorylation and Cognitive Dysfunction during Chronic Hypoxia. Int J Mol Sci. 2022;23: pubmed publisher
	Li L, Miao J, Chu D, Jin N, Tung Y, Dai C, et al. Tau antibody 77G7 targeting microtubule binding domain suppresses proteopathic tau to seed tau aggregation. CNS Neurosci Ther. 2022;28:2245-2259 pubmed publisher
	Alpaugh M, Masnata M, de Rus Jacquet A, Lepinay E, Denis H, Saint Pierre M, et al. Passive immunization against phosphorylated tau improves features of Huntington's disease pathology. Mol Ther. 2022;30:1500-1522 pubmed publisher
	Zhao D, Zhou Y, Huo Y, Meng J, Xiao X, Han L, et al. RPS23RG1 modulates tau phosphorylation and axon outgrowth through regulating p35 proteasomal degradation. Cell Death Differ. 2021;28:337-348 pubmed publisher
	Egervári G, Akpoyibo D, Rahman T, Fullard J, Callens J, Landry J, et al. Chromatin accessibility mapping of the striatum identifies tyrosine kinase FYN as a therapeutic target for heroin use disorder. Nat Commun. 2020;11:4634 pubmed publisher
	Gu J, Xu W, Jin N, Li L, Zhou Y, Chu D, et al. Truncation of Tau selectively facilitates its pathological activities. J Biol Chem. 2020;295:13812-13828 pubmed publisher
	Miao J, Shi R, Li L, Chen F, Zhou Y, Tung Y, et al. Pathological Tau From Alzheimer's Brain Induces Site-Specific Hyperphosphorylation and SDS- and Reducing Agent-Resistant Aggregation of Tau in vivo. Front Aging Neurosci. 2019;11:34 pubmed publisher
	Zhang Y, Wu F, Iqbal K, Gong C, Hu W, Liu F. Subacute to chronic Alzheimer-like alterations after controlled cortical impact in human tau transgenic mice. Sci Rep. 2019;9:3789 pubmed publisher
	Salissou M, Mahaman Y, Zhu F, Huang F, Wang Y, Xu Z, et al. Methanolic extract of Tamarix Gallica attenuates hyperhomocysteinemia induced AD-like pathology and cognitive impairments in rats. Aging (Albany NY). 2018;10:3229-3248 pubmed publisher
	Neddens J, Temmel M, Flunkert S, Kerschbaumer B, Hoeller C, Loeffler T, et al. Phosphorylation of different tau sites during progression of Alzheimer's disease. Acta Neuropathol Commun. 2018;6:52 pubmed publisher
	Hu W, Tung Y, Zhang Y, Liu F, Iqbal K. Involvement of Activation of Asparaginyl Endopeptidase in Tau Hyperphosphorylation in Repetitive Mild Traumatic Brain Injury. J Alzheimers Dis. 2018;64:709-722 pubmed publisher
	Mahaman Y, Huang F, Wu M, Wang Y, Wei Z, Bao J, et al. Moringa Oleifera Alleviates Homocysteine-Induced Alzheimer's Disease-Like Pathology and Cognitive Impairments. J Alzheimers Dis. 2018;63:1141-1159 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
	Hu W, Wu F, Zhang Y, Gong C, Iqbal K, Liu F. Expression of Tau Pathology-Related Proteins in Different Brain Regions: A Molecular Basis of Tau Pathogenesis. Front Aging Neurosci. 2017;9:311 pubmed publisher
	Wang Y, Ma Q, Ma X, Zhang Z, Liu N, Wang M. Role of mammalian target of rapamycin signaling in autophagy and the neurodegenerative process using a senescence accelerated mouse-prone 8 model. Exp Ther Med. 2017;14:1051-1057 pubmed publisher
	Wang Y, Zhang Y, Hu W, Xie S, Gong C, Iqbal K, et al. Rapid alteration of protein phosphorylation during postmortem: implication in the study of protein phosphorylation. Sci Rep. 2015;5:15709 pubmed publisher
	Takeda S, Wegmann S, Cho H, DeVos S, Commins C, Roe A, et al. Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer's disease brain. Nat Commun. 2015;6:8490 pubmed publisher
	Sottejeau Y, Bretteville A, Cantrelle F, Malmanche N, Demiaute F, Mendes T, et al. Tau phosphorylation regulates the interaction between BIN1's SH3 domain and Tau's proline-rich domain. Acta Neuropathol Commun. 2015;3:58 pubmed publisher
	Porquet D, AndrÃ©s Benito P, GriÃ±Ã¡n FerrÃ© C, Camins A, Ferrer I, Canudas A, et al. Amyloid and tau pathology of familial Alzheimer's disease APP/PS1 mouse model in a senescence phenotype background (SAMP8). Age (Dordr). 2015;37:9747 pubmed publisher
	Wang Y, Yang R, Gu J, Yin X, Jin N, Xie S, et al. Cross talk between PI3K-AKT-GSK-3Î² and PP2A pathways determines tau hyperphosphorylation. Neurobiol Aging. 2015;36:188-200 pubmed publisher

product information

Product Type :

Antibody

Product Name :

Phospho-Tau (Ser199) Polyclonal Antibody

Catalog # :

44-734G

Quantity :

100 µL

Price :

US 446

Clonality :

Polyclonal

Purity :

Antigen affinity chromatography

Host :

Rabbit

Reactivity :

Human, Mouse, Rat

Applications :

Functional Assay: Assay-dependent, Immunocytochemistry: 1 µg/mL, Immunohistochemistry (Paraffin): 1:20-1:200, Western Blot: 1:1,000

Species :

Human, Mouse, Rat

Isotype :

IgG

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 :

The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of human Tau that contains serine 199. The sequence is conserved in mouse and rat.

Format :

Liquid

Applications w/Dilutions :

Functional Assay: Assay-dependent, Immunocytochemistry: 1 µg/mL, Immunohistochemistry (Paraffin): 1:20-1:200, Western Blot: 1:1,000

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