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T5530

Sigma-Aldrich

Monoclonal Anti-τ (Tau) antibody produced in mouse

clone TAU-2, ascites fluid

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

TAU-2, monoclonal

mol wt

antigen 55-62 kDa

contains

15 mM sodium azide

species reactivity

monkey, bovine, chicken, human

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
microarray: suitable
western blot: 1:1,000 using a fresh total bovine brain extract or an enriched microtubule protein preparation

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MAPT(4137)

General description

Monoclonal Anti- τ (TAU) (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. τ (TAU) proteins are a part of microtubule associated proteins (MAPs). They are densely found in neurons and in trace amounts in non-neuronal cells. In brain six isoforms of τ (TAU) proteins are present.
The antibody reacts exclusively with the chemically heterogeneous τ in both the phosphorylated and non-phosphorylated form. The antibody does not react with other MAPs or with tubulin. In immunohistochemical staining, it localizes τ along microtubules in axons, somata, dendrites and astrocytes, and on ribosomes. The antibody may be used for staining of τ in Alzheimer neurofibrillary tangles in sections of human brain tissue.
The best known microtubule associated proteins (MAPs) which copurify with microtubules are MAP2 and Tau. These two proteins are heat stable and stimulate formation of the microtubule polymer from purified tubulin subunits. Tau is chemically heterogenous, however, limited protolysis has demonstrated that the different eletrophoretic species are closely related. Tau is immunologically distinct from the other MAPs, namely MAP1, MAP2 and MAP5. Localization studies have demonstrated that Tau is intimately associated with the filamentous structures which compose the neurofibrillary tangles as found in an Alzheimer′s disease brain.

Immunogen

bovine microtubule-associated proteins (MAPs)

Application

Monoclonal Anti-τ (Tau) antibody has been used:
  • in immunohistology
  • in immunoblotting
  • in dot blot
  • in immunohistochemistry

Mouse monoclonal clone TAU-2 anti-Tau antibody maybe used to study microtubule associated proteins (MAP) expression and cytological localization in various tissue and cell lines, under different developmental and environmental circumstances.

Biochem/physiol Actions

Monoclonal Anti- τ (TAU) is phosphatase independent; it will bind Tau proteins in either their phosphorylated or non-phosphorylated forms. It localizes Tau proteins along microtubules in axons, somata, dendrites, astrocytes and on ribosomes (polysomes). The best-known microtubule associated proteins (MAPs) which copurify with microtubules are MAP2 and Tau. These two proteins are heat stable and stimulate formation of the microtubule polymer from purified tubulin subunits. Tau is immunologically distinct from the other MAPs. Tau is intimately associated with the filamentous structures which compose the neurofibrillary tangles as found in an Alzheimer′s disease brain.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Anna E Bugrova et al.
International journal of molecular sciences, 23(1) (2022-01-12)
Alzheimer's disease (AD) is the leading cause of dementia among the elderly. Neuropathologically, AD is characterized by the deposition of a 39- to 42-amino acid long β-amyloid (Aβ) peptide in the form of senile plaques. Several post-translational modifications (PTMs) in
Melissa Broe et al.
Brain : a journal of neurology, 127(Pt 10), 2214-2220 (2004-07-30)
The main unifying feature of cases with frontotemporal dementia (FTD) is the pattern of brain atrophy. Surprisingly, there are a variety of underlying histopathologies in cases with the clinical features and typical pattern of atrophy characterizing FTD. This suggests that
John R Hodges et al.
Annals of neurology, 56(3), 399-406 (2004-09-07)
The term frontotemporal dementia (FTD) encompasses a range of clinical syndromes that are believed not to map reliably onto the spectrum of recognized pathologies. This study reexamines the relationships between clinical and pathological subtypes of FTD in a large series
Glenda M Halliday et al.
Annals of neurology, 57(1), 139-143 (2004-12-29)
Presenilin-1 (PS-1) mutations can cause Pick's disease without evidence of Alzheimer's disease (AD). We describe a family with a PS-1 M146L mutation and both Pick bodies and AD. Sarkosyl-insoluble hyperphosphorylated tau showed three bands consistent with AD, although dephosphorylation showed
Chris R Guthrie et al.
Journal of molecular neuroscience : MN, 45(1), 32-41 (2011-02-23)
Lesions containing aggregated and hyperphosphorylated tau protein are characteristic of neurodegenerative tauopathies. We have developed a cellular model of pathological tau deposition and clearance by overexpressing wild type human tau in HEK293 cells. When proteasome activity is inhibited, HEK293/tau cells

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