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SAE0076

Sigma-Aldrich

Tau-441 human

recombinant, lyophilized powder, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

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Synonym(s):
Neurofibrillary tangle protein, PHF-tau, Paired helical filament-tau
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in HEK 293 cells

Assay

≥95% (SDS-PAGE)

form

lyophilized powder

mol wt

calculated mol wt 50.3 kDa (including c-terminal His and V5 tags)
observed mol wt 70-100 kDa by SDS-PAGE (The protein migrates as a 70-110 kDa protein on SDS-PAGE due to glycosylation)

technique(s)

cell based assay: suitable

UniProt accession no.

shipped in

ambient

storage temp.

−20°C

Gene Information

human ... MAPT(4137)

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This Item
MSST0032SAE0071SAE0075
Tau-441 human recombinant, lyophilized powder, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

Sigma-Aldrich

SAE0076

Tau-441 human

HIV-1 GP120 protein recombinant, expressed in HEK 293 cells

Sigma-Aldrich

SAE0071

HIV-1 GP120 protein

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

assay

≥95% (SDS-PAGE)

assay

≥98% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

calculated mol wt 50.3 kDa (including c-terminal His and V5 tags), observed mol wt 70-100 kDa by SDS-PAGE (The protein migrates as a 70-110 kDa protein on SDS-PAGE due to glycosylation)

mol wt

calculated mol wt 50 kDa

mol wt

calculated mol wt 55 kDa (The protein migrates as a 100-130 kDa protein on SDS-PAGE due to glycosylation)

mol wt

calculated mol wt 138 kDa (The protein migrates as a 180 kDa protein on SDS-PAGE due to glycosylation)

technique(s)

cell based assay: suitable

technique(s)

mass spectrometry (MS): suitable

technique(s)

-

technique(s)

-

General description

Research area: Neuroscience

Tau-441 is a member of the Tau family of proteins. Tau is a family of neuronal microtubule-associated proteins. Six isoforms have been found that differ from each other in having either 3 or 4 binding repeats (R) of 31-32 amino acids, and from zero to 3 amino terminal inserts (N) of 29 amino acids each.

Application

Tau-441 human has been used to study the tau uptake by human bronchial epithelial cells (HBEC).

Biochem/physiol Actions

Tau proteins are mainly expressed in the neurons of the central nervous system where they exert a role in stabilizing microtubules, key components of axonal transport, as well as in signal transduction. Tau proteins are subject to phosphorylation, which regulates their association with the microtubules. Deposits of Alzheimer′s disease AD-associated proteins, such as hyperphosphorylated Tau, as well as other shared misfolded proteins, such as beta-amyloid precursor protein (beta-APP), ubiquitin, and various chaperones and protein kinases, are thought to play a pathologic role in the cognitive decline and muscular failure. Malfunctioning of Tau proteins is associated with microtubule disintegration and collapsing of the neuronal transport system. Among other diseases, Tau forms in cerebrospinal fluid are considered a reliable biomarker for progressive supranuclear palsy, where the levels of Tau forms ratio were significantly reduced.

Sequence

MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGLDRIRGRKLGPFEGKPIPNPLLGLDSTRTGHHHHHHHHGGQ

This sequence includes a polyhistidine and V5 tags at the C-terminus.

Physical form

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4.

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Zhang Zhenxia et al.
International journal of biological macromolecules, 171, 74-81 (2020-12-11)
In this study, the in vitro assembly of tau and anti-amyloidogenic properties of one naturally occurring phytoestrogen, calycosin, was investigated by spectroscopic techniques including ThT and ANS fluorescence, CD, Congo red absorbance as well as TEM analysis. Afterwards the cytotoxicity
Soluble pathogenic tau enters brain vascular endothelial cells and drives cellular senescence and brain microvascular dysfunction in a mouse model of tauopathy.
Hussong, et al.
Nature Communications, 14, 2367-2367 (2023)

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