Tau (260–267) Light IGSTENLK-acid


Phosphoprotein involved in microtubule assembly and stability as well as brain development

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Catalogue number crb1001246
Sequence (one letter code) IGSTENLK-acid
Sequence (three letter code) Ile-Gly-Ser-Thr-Glu-Asn-Leu-Lys-OH
Aliases TAT-repeated 1 domain (TAT-R1D)
Purity >95%
Storage -20°C
Molecular Weight 860.5

Šimić, G., Babić Leko, M., Wray, S., Harrington, C., Delalle, I., Jovanov-Milošević, N., Bažadona, D., Buée, L., de Silva, R., Di Giovanni, G., Wischik, C. and Hof, P. (2016). Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies. Biomolecules, 6(1), 6. PMID: 26751493

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

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

Tau (260–267) Light

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