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T6402

Sigma-Aldrich

Anti-τ (Tau) antibody produced in rabbit

whole antiserum

Synonyme(s) :

Anti-DDPAC, Anti-FTDP-17, Anti-MAPTL, Anti-MSTD, Anti-MTBT1, Anti-MTBT2, Anti-PPND, Anti-PPP1R103, Anti-TAU, Anti-tau-40

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About This Item

Numéro MDL:
MFCD00164745
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

whole antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Contient

15 mM sodium azide

Espèces réactives

chicken, rat, mouse

Technique(s)

western blot: 1:100 using rat or mouse brain tissue extract

Numéro d'accès UniProt

P19332

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MAPT(4137)

Description générale

Tau (τ), also known as MAPT (microtubule associated protein tau) is encoded by the gene mapped on human chromosome 17q21.3. It is highly expressed in neurons but is most prominent in axons.
Tau (τ), also known as microtubule associated protein tau (MAPT) is encoded by the gene mapped on human chromosome 17q21.3. It is highly expressed in neurons but is most prominent in axons. Tau is a heat stable microtubule associated protein (MAP) with a molecular weight of 55- 65 kDa.

Spécificité

The antibody shows wide species reactivity. Anti-τ does not react with MAP1, MAP2 or tubulin. the antibody reacts with τ, one of the two major classes of heat stable microtubule-associated proteins (MAPs).

Immunogène

τ proteins from chicken embryo brain microtubules.

Application

Anti-τ (Tau) antibody produced in rabbit has been used as a primary antibody in western blotting.

Actions biochimiques/physiologiques

Removal of Tau (τ) results in developmental delay and learning disability. It participates in the pathology of Alzheimer′s disease (AD). Tau helps in the assembly and maintenance of microtubule structure.
Variation in the MAPT gene encoding tau protein results in frontotemporal dementia. Tau protein acts as a substrate for many kinases.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Tau pathology in Alzheimer disease and other tauopathies
Iqbal K, et al.
Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1739(2-3), 198-210 (2005)
Michael Briese et al.
Nucleic acids research, 44(4), e33-e33 (2015-10-16)
Most RNAs within polarized cells such as neurons are sorted subcellularly in a coordinated manner. Despite advances in the development of methods for profiling polyadenylated RNAs from small amounts of input RNA, techniques for profiling coding and non-coding RNAs simultaneously
Distinct neuroanatomical correlates of neuropsychiatric symptoms in the three main forms of genetic frontotemporal dementia in the GENFI cohort
Sellami L, et al.
Journal of Alzheimer'S Disease, 1-16 (2018)
Lieven Declercq et al.
Molecular imaging, 15 (2016-04-01)
Early clinical results of two tau tracers, [(18)F]T808 and [(18)F]T807, have recently been reported. In the present study, the biodistribution, radiometabolite quantification, and competition-binding studies were performed in order to acquire comparative preclinical data as well as to establish the
J H Su et al.
Acta neuropathologica, 96(5), 463-471 (1998-11-26)
Plaque-associated dystrophic neurites are a common pathological feature in the brains of patients with Alzheimer's disease (AD). In the present study, we investigated the relative abundance and progressive transformation of the amyloid precursor protein (APP), neurofilament (NF) and paired helical
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