T5530

Sigma-Aldrich

Monoclonal Anti-τ (Tau) antibody produced in mouse

clone TAU-2, ascites fluid

MDL number:
NACRES:
NA.41
En este momento no podemos mostrarle ni los precios ni la disponibilidad

Quality Level

biological source

mouse

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

bovine, chicken, human, monkey

application(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

conjugate

unconjugated

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

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.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point F

Not applicable

Flash Point C

Not applicable

Proteasome inhibition drives HDAC6-dependent recruitment of tau to aggresomes.
Guthrie, et al.
Journal of Molecular Neuroscience, 45, 32-41 (2018)
Severity of gliosis in Pick?s disease and frontotemporal lobar degeneration: tau-positive glia differentiate these disorders
Schofield E, et al.
Brain, 126(4), 827-840 (2003)
Huishan Guo et al.
The American journal of pathology, 165(2), 523-531 (2004-07-28)
Previously, we have shown that caspase-6 but not caspase-3 is activated by serum deprivation and induces a protracted cell death in primary cultures of human neurons (LeBlanc AC, Liu H, Goodyer C, Bergeron C, Hammond J: Caspase-6 role in apoptosis...
Emma C Schofield et al.
Movement disorders : official journal of the Movement Disorder Society, 26(2), 256-263 (2011-03-18)
To determine whether brain atrophy differs between the two subtypes of progressive supranuclear palsy (PSP), Richardson's syndrome (PSP-RS), and PSP parkinsonism (PSP-P), and whether such atrophy directly relates to clinical deficits and the severity of tau deposition. We compared 24...
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...
Artículos
Alzheimer's disease (AD) is the most common cause of dementia in the elderly and is characterized by gradual loss of cognitive functions.
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