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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 (Thr205) Polyclonal Antibody
catalog :
44-738G
quantity :
100 µL
price :
US 446
clonality :
polyclonal
host :
domestic rabbit
conjugate :
nonconjugated
antigen modification :
phosphorylated
reactivity :
human, mouse, rat, dogs, cat
application :
western blot, immunohistochemistry, immunocytochemistry, immunohistochemistry - paraffin section
more info or order :
citations: 28
Published Application/Species/Sample/DilutionReference
  • immunohistochemistry - paraffin section; cat; 1:1000; loading ...; fig 3b
Fiock K, Smith J, Crary J, Hefti M. β-amyloid and tau pathology in the aging feline brain. J Comp Neurol. 2020;528:108-113 pubmed publisher
  • immunohistochemistry; mouse; 1:250; loading ...; fig s5d
Wang A, Jensen E, Rexach J, Vinters H, Hsieh Wilson L. Loss of O-GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration. Proc Natl Acad Sci U S A. 2016;113:15120-15125 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, Noël 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; human
  • western blot; mouse
  • immunohistochemistry - paraffin section; dogs
  • western blot; dogs; 1:1000; fig 7
  • 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
Salgado B, Sastre I, Bullido M, Aldudo J. Herpes Simplex Virus Type 1 Induces AD-like Neurodegeneration Markers in Human Progenitor and Differentiated ReNcell VM Cells. Microorganisms. 2023;11: pubmed publisher
Pan A, Audrain M, Sakakibara E, Joshi R, Zhu X, Wang Q, et al. Dual-Specificity Protein Phosphatase 4 (DUSP4) Overexpression Improves Learning Behavior Selectively in Female 5xFAD Mice, and Reduces β-Amyloid Load in Males and Females. Cells. 2022;11: pubmed publisher
Levert S, Pilliod J, Aumont x, Armanville S, Tremblay C, Calon F, et al. Direct and Indirect Effects of Filamin A on Tau Pathology in Neuronal Cells. Mol Neurobiol. 2022;: pubmed publisher
Siddik M, Mullins C, Kramer A, Shah H, Gannaban R, Zabet Moghaddam M, et al. Branched-Chain Amino Acids Are Linked with Alzheimer's Disease-Related Pathology and Cognitive Deficits. Cells. 2022;11: pubmed publisher
Hochmair J, Exner C, Franck M, Dominguez Baquero A, Diez L, Brognaro H, et al. Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates. EMBO J. 2022;41:e108882 pubmed publisher
Lester E, Ooi F, Bakkar N, Ayers J, Woerman A, Wheeler J, et al. Tau aggregates are RNA-protein assemblies that mislocalize multiple nuclear speckle components. Neuron. 2021;109:1675-1691.e9 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
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
Ko H, Chiou S, Wong Y, Wang Y, Lai Y, Chou C, et al. GSKIP-Mediated Anchoring Increases Phosphorylation of Tau by PKA but Not by GSK3beta via cAMP/PKA/GSKIP/GSK3/Tau Axis Signaling in Cerebrospinal Fluid and iPS Cells in Alzheimer Disease. J Clin Med. 2019;8: pubmed publisher
Beyrent E, Gomez G. Oxidative stress differentially induces tau dissociation from neuronal microtubules in neurites of neurons cultured from different regions of the embryonic Gallus domesticus brain. J Neurosci Res. 2020;98:734-747 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
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
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
Shen X, Luo T, Li S, Ting O, He F, Xu J, et al. Quercetin inhibits okadaic acid-induced tau protein hyperphosphorylation through the Ca2+?calpain?p25?CDK5 pathway in HT22 cells. Int J Mol Med. 2017;: 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
O Hare Doig R, Chiha W, Giacci M, Yates N, Bartlett C, Smith N, et al. Specific ion channels contribute to key elements of pathology during secondary degeneration following neurotrauma. BMC Neurosci. 2017;18:62 pubmed publisher
Mohamed N, Desjardins A, Leclerc N. Tau secretion is correlated to an increase of Golgi dynamics. PLoS ONE. 2017;12:e0178288 pubmed publisher
Grant N, Coates P, Woods Y, Bray S, Morrice N, Hastie C, et al. Phosphorylation of a splice variant of collapsin response mediator protein 2 in the nucleus of tumour cells links cyclin dependent kinase-5 to oncogenesis. BMC Cancer. 2015;15:885 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
Porquet D, Andrés Benito P, Griñán Ferré 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-3β and PP2A pathways determines tau hyperphosphorylation. Neurobiol Aging. 2015;36:188-200 pubmed publisher
product information
Product Type :
Antibody
Product Name :
Phospho-Tau (Thr205) Polyclonal Antibody
Catalog # :
44-738G
Quantity :
100 µL
Price :
US 446
Clonality :
Polyclonal
Purity :
Antigen affinity chromatography
Host :
Rabbit
Reactivity :
Human, Mouse, Rat
Applications :
Immunocytochemistry: 1-2 µg/mL, Immunohistochemistry: Assay-dependent, 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 threonine 205. The sequence is conserved in mouse and rat.
Format :
Liquid
Applications w/Dilutions :
Immunocytochemistry: 1-2 µg/mL, Immunohistochemistry: Assay-dependent, 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 :
company information
Invitrogen
Thermo Fisher Scientific
81 Wyman Street
Waltham, MA USA 02451
https://www.thermofisher.com
800-678-5599
headquarters: USA