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T7951

Sigma-Aldrich

Tau Protein Ladder, 6 isoforms human

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

Synonym(s):

Tau Protein Ladder

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in E. coli

Assay

≥90% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... MAPT(4137)

General description

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.

Biochem/physiol Actions

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.

Packaging

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

Specifications

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.

Physical form

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

Storage and Stability

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

Signal Word

Danger

Hazard Classifications

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

Target Organs

Liver,Heart

Storage Class Code

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

WGK

WGK 3


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Antibody-mediated clearance of tau in primary mouse microglial cultures requires Fc gamma-receptor binding and functional lysosomes
Andersson C, et al.
Scientific reports, 9(1), 4658-4658 (2019)
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)
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
Michael G Friedrich et al.
International journal of molecular sciences, 22(7) (2021-04-04)
The truncation of Tau is thought to be important in promoting aggregation, with this feature characterising the pathology of dementias such as Alzheimer disease. Antibodies to the C-terminal and N-terminal regions of Tau were employed to examine Tau cleavage in

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