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Key Documents

T7951

Sigma-Aldrich

Tau Protein Ladder, 6 isoforms

recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous glycerol solution

Synonyme(s) :

Tau Protein Ladder

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in E. coli

Pureté

≥90% (SDS-PAGE)

Forme

buffered aqueous glycerol solution

Poids mol.

36800
39700
40000
42600
42900
45900

Composition

dodecyl sulphate sodium salt, 1-5%
glycerine, 20-30%
mercaptoethanol, 10-20%

Technique(s)

immunoelectrophoresis: 10-20 μL using recombinant Tau protein marker
western blot: 2-5 μL using recombinant Tau protein marker

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Informations sur le gène

human ... MAPT(4137)

Description générale

Research area: Neuroscience

Tau gene, spanning 100 kb with 16 exons, is mapped to human chromosome 17q21. The six alternative splice variants of protein ranging in size from 352-441 amino acids have been identified in human adult brain. Tau is a member of the microtubule-associated protein (MAP) family. It is predominantly expressed in neurons.

Application

Tau Protein Ladder, 6 isoforms human has been used as a sample in immunomagnetic reduction (IMR) assay. It has also been used as positive control in western blotting.

Actions biochimiques/physiologiques

In neurons, tau protein plays an important role in maintaining microtubule assembly and stability. It acts as a connector between microtubules and other cytoskeletal elements or proteins. Overexpression of the protein has been observed in Alzheimer′s disease and various neurodegenerative disorders denoted as ‘tauopathies′. Thus, pathological tau proteins act as a potential biomarker in the neurodegenerative process.

Conditionnement

A 50 μL vial of Tau Protein Ladder contains 0.25 μg of each of the six isoforms.

Caractéristiques

Contains 6 recombinant Tau proteins expressed in E. coli, which comprise six Tau isoforms with molecular weights of 45,900, 42,600, 42,900, 39,700, 40,000, and 36,800 respectively. No histidine-tags are present in the proteins.

Forme physique

Solution in 125 mM Tris-HCl, pH 6.8, containing 4% SDS, 10% 2-mercaptoethanol, 20% glycerol, and 0.004% bromphenol blue.

Stockage et stabilité

Tightly closed. Keep in a well-ventilated place. Keep locked up or in an area accessible only
to qualified or authorized persons

Pictogrammes

Skull and crossbonesHealth hazardCorrosion

Mention d'avertissement

Danger

Classification des risques

Acute Tox. 3 Dermal - Acute Tox. 4 Oral - Aquatic Chronic 3 - Eye Dam. 1 - Repr. 2 - Skin Irrit. 2 - Skin Sens. 1 - STOT RE 2 Oral

Organes cibles

Liver,Heart

Code de la classe de stockage

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Classe de danger pour l'eau (WGK)

WGK 3


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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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Reeteka Sud et al.
Molecular therapy. Nucleic acids, 3, e180-e180 (2014-07-30)
In Alzheimer's disease, progressive supranuclear palsy, and a number of other neurodegenerative diseases, the microtubule associated protein tau aggregates to form intracellular neurofibrillary tangles and glial tangles, abnormal structures that are part of disease pathogenesis. Disorders with aggregated tau are
Analytical performance of reagent for assaying tau protein in human plasma and feasibility study screening neurodegenerative diseases
Yang S, et al.
Scientific reports, 7(1), 9304-9304 (2017)
Tau protein in cerebrospinal fluid: a biochemical marker for axonal degeneration in Alzheimer disease?
Blennow K, et al.
Molecular and Chemical Neuropathology, 26(3), 231-245 (1995)
Rebecca L Mueller et al.
Frontiers in molecular neuroscience, 14, 647054-647054 (2021-04-06)
Over four decades ago, in vitro experiments showed that tau protein interacts with and stabilizes microtubules in a phosphorylation-dependent manner. This observation fueled the widespread hypotheses that these properties extend to living neurons and that reduced stability of microtubules represents
Nora Lemke et al.
The Journal of biological chemistry, 295(52), 18508-18523 (2020-11-01)
Synapse loss is associated with motor and cognitive decline in multiple neurodegenerative disorders, and the cellular redistribution of tau is related to synaptic impairment in tauopathies, such as Alzheimer's disease and frontotemporal dementia. Here, we examined the cellular distribution of

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