Up-regulation and Antibody-Peptide Competition. Human recombinant Tau stimulated with GSK-3β (1 µg per µg Tau) for 45 minutes 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 and either left untreated (1-4) or treated with lambda phosphatase (5), then incubated with the Tau [pS422] antibody in a 3% BSA-TBST buffer for two hours at room temperature, following prior incubation with: no peptide (1,5), the non-phosphopeptide corresponding to the phosphopeptide immunogen (2), a generic phosphoserine-containing peptide (3), or the phosphopeptide immunogen (4). After washing, the membrane was incubated with goat F(ab')2 anti-rabbit IgG HRP conjugate (Cat. no. ALI4404) and signals were detected using the Pierce SuperSignal™ method.The data show that only the phosphopeptide corresponding to Tau [pS422] blocks the antibody signal, demonstrating the specificity of the antibody. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific. (Cat. No. 44764G)
|Tested species reactivity||Human|
|Published species reactivity||Tag, Mouse, Human, Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of human Tau that contains serine 422. The sequence is conserved in mouse and rat.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 50% glycerol, 1mg/ml BSA|
|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.
The neuritic plaque facilitates pathological conversion of tau in an Alzheimer's disease mouse model.
44-764G was used in immunohistochemistry - paraffin section to elucidate the pathological conversion of tau facilitated by the neuritic plaque in an Alzheimer's disease mouse model
|Li T,Braunstein KE,Zhang J,Lau A,Sibener L,Deeble C,Wong PC||Nature communications (7:null)||2016|
Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils.
44-764G was used in immunohistochemistry - paraffin section to assess induction by Abeta 42 fibrils on the formation of neurofibrillary tangles in P301I tau transgenic mice
|Götz J,Chen F,van Dorpe J,Nitsch RM||Science (New York, N.Y.) (293:1491)||2001|
|Not Applicable||Not Cited||
Functional screening of Alzheimer risk loci identifies PTK2B as an in vivo modulator and early marker of Tau pathology.
44-764G was used in western blot to identify PTK2B as an in vivo modulator and early marker of Tau pathology due to functional screening of Alzheimer risk loci
|Dourlen P,Fernandez-Gomez FJ,Dupont C,Grenier-Boley B,Bellenguez C,Obriot H,Caillierez R,Sottejeau Y,Chapuis J,Bretteville A,Abdelfettah F,Delay C,Malmanche N,Soininen H,Hiltunen M,Galas MC,Amouyel P,Sergeant N,Buée L,Lambert JC,Dermaut B||Molecular psychiatry (null:null)||2016|
Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer's disease brain.
44-764G was used in western blot to research Alzheimer's disease brain and neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau
|Takeda S,Wegmann S,Cho H,DeVos SL,Commins C,Roe AD,Nicholls SB,Carlson GA,Pitstick R,Nobuhara CK,Costantino I,Frosch MP,Müller DJ,Irimia D,Hyman BT||Nature communications (6:null)||2015|
|Mouse||Not Cited||Targeting phospho-Ser422 by active Tau Immunotherapy in the THYTau22 mouse model: a suitable therapeutic approach.||Troquier L,Caillierez R,Burnouf S,Fernandez-Gomez FJ,Grosjean ME,Zommer N,Sergeant N,Schraen-Maschke S,Blum D,Buee L||Current Alzheimer research (9:397)||2012|
Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo.
44-764G was used in western blot to report that autophagy is a mechanism by which methylene blue reduces tau levels.
|Congdon EE,Wu JW,Myeku N,Figueroa YH,Herman M,Marinec PS,Gestwicki JE,Dickey CA,Yu WH,Duff KE||Autophagy (8:609)||2012|
|Human||Not Cited||Nature of "Tau" immunoreactivity in normal myonuclei and inclusion body myositis.||Salajegheh M,Pinkus JL,Nazareno R,Amato AA,Parker KC,Greenberg SA||Muscle and nerve (40:520)||2009|
|Mouse||Not Cited||Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: evidence for distinct molecular processes underlying tau abnormalities.||Lambourne SL,Sellers LA,Bush TG,Choudhury SK,Emson PC,Suh YH,Wilkinson LS||Molecular and cellular biology (25:278)||2005|
High Resolution Dissection of Reactive Glial Nets in Alzheimer's Disease.
44-764G was used in immunohistochemistry - free floating to analyze reactive glial nets in Alzheimer's disease by high resolution dissection
|Bouvier DS,Jones EV,Quesseveur G,Davoli MA,A Ferreira T,Quirion R,Mechawar N,Murai KK||Scientific reports (6:null)||2016|
|Not Applicable||Not Cited||
Increased tau phosphorylation and cleavage in mouse models of type 1 and type 2 diabetes.
44-764G was used in immunohistochemistry and western blot to assess tau modification in type 1 and type 2 mouse models of diabetes
|Kim B,Backus C,Oh S,Hayes JM,Feldman EL||Endocrinology (150:5294)||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|