T5530
ANTI-TAU (MAPT) Antibody
mouse monoclonal, TAU-2
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关于此项目
Conjugate:
unconjugated
Clone:
TAU-2, monoclonal
Application:
ARR, IHC (p), WB
Citations:
25
产品名称
Monoclonal Anti-τ (Tau) antibody produced in mouse, clone TAU-2, ascites fluid
biological source
mouse
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
Quality Level
Gene Information
human ... MAPT(4137)
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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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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
动植物来源生物产品
常规特殊物品
此项目有
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
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.
Brain : a journal of neurology, 128(Pt 10), 2272-2280 (2005-07-15)
Changes in motor cortical activation are associated with the major symptoms observed in both Parkinson's disease and progressive supranuclear palsy (PSP). While research has concentrated on basal ganglia abnormalities as central to these cortical changes, several studies in both disorders
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