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MAB2239

Sigma-Aldrich

Anti-Tau Antibody, clone Tau 7

clone Tau 7, from mouse

Synonyme(s) :

G protein beta1/gamma2 subunit-interacting factor, Neurofibrillary tangle protein, Paired helical filament-tau, microtubule-associated protein tau, microtubule-associated protein tau, isoform 4

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

100

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

Tau 7, monoclonal

Espèces réactives

human, rat

Technique(s)

western blot: suitable

Isotype

IgG1κ

Numéro d'accès NCBI

NP_001116538.1

Numéro d'accès UniProt

P10636

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MAPT(4137)
rat ... Mapt(29477)

Description générale

Microtubule Associated Proteins, or MAPS, bind to the tubulin subunits of microtubule structures and regulate their functional stability. In the cell MAPs bind to monomer and multimerized tubulin. MAP binding to multimerized tubulin further stabilizes the formation of higher order microtubulin structures. MAP binding to microtubule structures is mediated through phosphorylation through Microtubule Affinity Regulated Kinase (MARK). Phosphorylation releases MAPs bound to microtubules, destabilizing the structure, driving it toward disassembly. There are predominately two MAP types, I, II. Type II MAP includes MAP2, MAP4, and tau and are found in nervous tissue. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains.

Spécificité

Cat. # MAB2239 recognizes the C-terminus region of Tau.
Reactivity with other species has not been determined.

Application

This Anti-Tau Antibody, clone Tau 7 is validated for use in WB for the detection of Tau.

Qualité

Western Blot:

Description de la cible

50-68 kDa

Forme physique

Format: Purified

Autres remarques

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

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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Chiara Galimberti et al.
American journal of cancer research, 11(7), 3558-3574 (2021-08-07)
Glioblastoma multiforme (GBM) is the most malignant primary brain cancer. Despite aggressive treatments currently there is no cure for GBM. Many challenges should be considered for the development of new therapeutical agents for glioblastoma, including appropriate target selectivity and pharmacokinetics.
Takayuki Ohnishi et al.
Proceedings of the National Academy of Sciences of the United States of America, 112(32), E4465-E4474 (2015-08-01)
Neurodegeneration correlates with Alzheimer's disease (AD) symptoms, but the molecular identities of pathogenic amyloid β-protein (Aβ) oligomers and their targets, leading to neurodegeneration, remain unclear. Amylospheroids (ASPD) are AD patient-derived 10- to 15-nm spherical Aβ oligomers that cause selective degeneration
Rik van der Kant et al.
Cell stem cell, 24(3), 363-375 (2019-01-29)
Genetic, epidemiologic, and biochemical evidence suggests that predisposition to Alzheimer's disease (AD) may arise from altered cholesterol metabolism, although the molecular pathways that may link cholesterol to AD phenotypes are only partially understood. Here, we perform a phenotypic screen for

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