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Peptide Competition. Human recombinant Tau untreated (1) or treated with GSK-3ß (1 µg per µg Tau) for 45 minutes (2-5) was added to background extracts, resolved by SDS-PAGE on a 10% Tris-glycine gel and transferred to PVDF. The membrane was blocked with a 5% BSA-TBST buffer for one hour at room temperature, then incubated with the Tau [pS396] antibody in a 1% BSA-TBST buffer for two hours at room temperature, following prior incubation with: no peptide (1, 2), the non-phosphopeptide corresponding to the phosphopeptide immunogen (3), a generic phosphoserine-containing peptide (4), or the phosphopeptide immunogen (5). After washing, the membrane was incubated with goat F(ab"e;)2 anti-rabbit IgG HRP conjugate (Cat. no. ALI4404) and signals were detected using the Pierce SuperSignal™ method. The data show that only the peptide corresponding to Tau [pS396] blocks the antibody signal, demonstrating the specificity of the antibody. The data also show up-regulation of Tau [pS396] upon GSK-3ß treatment.
|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Tag, Rat, Bovine, Mouse, Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of human Tau that contains serine 396. The sequence is conserved in many species including mouse, rat, rhesus monkey, baboon, cow and goat.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 1mg/ml BSA, 50% glycerol|
|Contains||0.05% sodium azide|
|Tested Applications||Dilution *|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. 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 whereas the longer isoforms may preferentially play a role in its stabilization.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Fyn inhibition rescues established memory and synapse loss in Alzheimer mice.
44-752G was used in western blot to assess the Src family kinase inhibitor, AZD0530, for treatment of Alzheimer's disease.
|Kaufman AC,Salazar SV,Haas LT,Yang J,Kostylev MA,Jeng AT,Robinson SA,Gunther EC,van Dyck CH,Nygaard HB,Strittmatter SM||Annals of neurology (77:953)||2015|
GSK-3β-dependent downregulation of γ-taxilin and αNAC merge to regulate ER stress responses.
44-752G was used in western blot to provide evidence that GSK-3beta-dependent downregulation of gamma-taxilin and alphaNAC regulate hypoxia-induced ER stress responses
|Hotokezaka Y,Katayama I,van Leyen K,Nakamura T||Cell death & disease (6:null)||2015|
The choice of general anesthetics may not affect neuroinflammation and impairment of learning and memory after surgery in elderly rats.
44-752G was used in western blot to test if anesthetic choice affects cognitive impairment and neuroinflammation in elderly rat
|Zhang J,Tan H,Jiang W,Zuo Z||Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology (10:179)||2015|
Amyloid and tau pathology of familial Alzheimer's disease APP/PS1 mouse model in a senescence phenotype background (SAMP8).
44-752G was used in western blot to characterize cognitive and neuropathological Alzheimer's disease markers in a novel mouse model
|Porquet D,Andrés-Benito P,Griñán-Ferré C,Camins A,Ferrer I,Canudas AM,Del Valle J,Pallàs M||Age (Dordrecht, Netherlands) (37:null)||2015|
Cross talk between PI3K-AKT-GSK-3β and PP2A pathways determines tau hyperphosphorylation.
44-752G was used in western blot to study the role of glycogen synthase kinase-3beta and protein phosphatase 2A in regulation of tau hyperphosphorylation
|Wang Y,Yang R,Gu J,Yin X,Jin N,Xie S,Wang Y,Chang H,Qian W,Shi J,Iqbal K,Gong CX,Cheng C,Liu F||Neurobiology of aging (36:188)||2015|
Impairment of glymphatic pathway function promotes tau pathology after traumatic brain injury.
44-752G was used in western blot to study how extracellular proteins are cleared from the brain
|Iliff JJ,Chen MJ,Plog BA,Zeppenfeld DM,Soltero M,Yang L,Singh I,Deane R,Nedergaard M||The Journal of neuroscience : the official journal of the Society for Neuroscience (34:16180)||2014|
Early alterations in energy metabolism in the hippocampus of APPswe/PS1dE9 mouse model of Alzheimer's disease.
44-752G was used in western blot to investigate the abnormalites in hippocampal energy metabolism in the pathogenesis of Alzheimer disease.
|Pedrós I,Petrov D,Allgaier M,Sureda F,Barroso E,Beas-Zarate C,Auladell C,Pallàs M,Vázquez-Carrera M,Casadesús G,Folch J,Camins A||Biochimica et biophysica acta (1842:1556)||2014|
Terminal hypothermic Tau.P301L mice have increased Tau phosphorylation independently of glycogen synthase kinase 3α/β.
44-752G was used in western blot to study the lack of involvementof GSK3-alpha/beta in the elevated tau phosphorylation observed in Tau.P30L hypothermic mice
|Maurin H,Lechat B,Borghgraef P,Devijver H,Jaworski T,Van Leuven F||The European journal of neuroscience (40:2442)||2014|
Microtubule-associated protein tau in bovine retinal photoreceptor rod outer segments: comparison with brain tau.
44-752G was used in western blot to characterize tau in the rod outer segment of bovine retinal photoreceptors.
|Yamazaki A,Nishizawa Y,Matsuura I,Hayashi F,Usukura J,Bondarenko VA||Biochimica et biophysica acta (1832:1549)||2013|
|Rat||Not Cited||A proteomic analysis of MCLR-induced neurotoxicity: implications for Alzheimer's disease.||Li G,Cai F,Yan W,Li C,Wang J||Toxicological sciences : an official journal of the Society of Toxicology (127:485)||2012|
|Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases.||Yu Y,Run X,Liang Z,Li Y,Liu F,Liu Y,Iqbal K,Grundke-Iqbal I,Gong CX||Journal of neurochemistry (108:1480)||2009|
|Pseudophosphorylation of tau protein alters its ability for self-aggregation.||Haase C,Stieler JT,Arendt T,Holzer M||Journal of neurochemistry (88:1509)||2004|
G protein beta1/gamma2 subunit-interacting factor 1; MAPT; Microtubule-associated protein tau; microtubule-associated protein tau, isoform 4; MTBT1; Neurofibrillary tangle protein; Paired helical filament-tau; PHF-tau; protein phosphatase 1, regulatory subunit 103; Tau microtubule-associated protein
AI413597; AW045860; DDPAC; FTDP-17; MAPT; MAPTL; MSTD; Mtapt; MTBT1; MTBT2; PPND; PPP1R103; pTau; RNPTAU; TAU