Tau Peptide (45-73) ESPLQTPTEDGSEEPGSETSDAKSTPTAE-acid
Phosphoprotein involved in microtubule assembly and stability as well as brain development
Catalogue number crb1000520 Molecular Weight 2976.3 Sequence (one letter code) ESPLQTPTEDGSEEPGSETSDAKSTPTAE-acid Sequence (three letter code) H-Glu-Ser-Pro-Leu-Gln-Thr-Pro-Thr-Glu-Asp-Gly-Ser-Glu-Glu-Pro-Gly-Ser-Glu-Thr-Ser-Asp-Ala-Lys-Ser-Thr-Pro-Thr-Ala-Glu-OH Purity >95% Storage -20°C References
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
Gendreau and Hall (2013) Tangles, Toxicity, and Tau Secretion in AD – New Approaches to a Vexing Problem. Front. Neurol. 4 PMID: 24151487
Manufactured in: United Kingdom
Amino acids 45-73, derived from the exon 2/insert 1 domain, of tubulin-associated unit (tau). Tau is a phosphoprotein protein 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. Tau is also glycosylated, and O-glycosylation may have a role in its subcellular localisation and degradation.
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 is expressed from a single gene and is alternatively spliced to yield six different isoforms in the adult central nervous system (CNS)