Tau (260–267) Heavy IGSTENL-[U-13C6,15N2-Lys]-acid

  • Description

  • Application Data


Phosphoprotein involved in microtubule assembly and stability as well as brain development.Contains a lysine residue labelled with stable 13C and 15N isotopes

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Application Data

Catalogue number crb1301247
Molecular Weight 868.5
Sequence (one letter code) IGSTENL-[U-13C6,15N2-Lys]-acid
Sequence (three letter code) H-Ile-Gly-Ser-Thr-Glu-Asn-Leu-[U-13C6,15N2-Lys]-OH
Aliase TAT-repeated 1 domain (TAT-R1D)
Purity >95%
Storage -20°C

Gendreau and Hall G (2013) Tangles, Toxicity, and Tau Secretion in AD – New Approaches to a Vexing Problem. Front. Neurol. 4 PMID: 24151487

Pei et al (2015) A Novel Mechanism of Spine Damages in Stroke via DAPK1 and Tau. Cereb Cortex 25(11) 4559 PMID: 25995053

Šimić et al (2016) Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies. Biomolecules 6(1) 6 PMID: 26751493

Manufactured in: United Kingdom
Data Sheet Material Safety Data Sheet (MSDS)

Residues 260-267 of tubulin-associated unit (tau). This region represents the death-associated protein kinase 1 (DAPK1) binding domain within the tau microtubule repeat domains (R). DAPK1 phosphorylates tau on ser262 in ischemic brain injury. This peptide can block the interaction between DAPK1 and tau and reduce the level of ser262 phosphorylation and therefore may have therapeutic benefits.

Tau is a phosphoprotein involved in microtubule (MT) assembly and stability as well as brain development. Tau is phosphorylated at multiple sites by several protein kinases, including cyclic-AMP-dependent protein kinases and casein kinase type-1. Tau phosphorylation causes tau to change shape, negatively regulating its ability to stimulate MT assembly.

Malfunctioning tau protein contributes to the structural core of the paired helical filaments (PHFs), which make up neurofibrillary tangles (NFTs). NFTs are often observed in neurodegenerative disorders, such as Alzheimer’s disease and other tauopathies.

The lysine residue at position 8 of this peptide is isotopically labelled with carbon-13 (6) and nitrogen-15 (2), giving this peptide a mass increase of 8 compared to the unlabelled peptide

Tau (260–267) Heavy

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