Target: Tau-383 (0N4R)
Nature: Recombinant
Swiss-Prot: P10636-6
Expression System: E. coli
Protein Length: 383 aa
Amino Acid Sequence: MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
Purification: Ion-exchange Purified
Purity: >95% as per SDS-PAGE, >80% as per A260/A280
Storage Buffer: 10mM Hepes pH 7.4, 100mM NaCl
Protein Size: 40.007 kDa
Conjugate: No Tag
Scientific Background: Several tau isoforms, including 0N4R, are expressed in the human brain, and the existence of multiple human tauopathies with distinct fibril morphologies suggests different molecular conformers incorporating different isoforms may exist (1, 2). NMR data indicates that both 3R and 4R tau are incorporated into AD-tau seeded fibrils (3).
References: 1. Goedert et al. 1989. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer’s disease. Neuron. DOI: 10.1016/0896-6273(89)90210-92. Goedert, Eisenberg and Crowther. 2017. Propagation of Tau Aggregates and Neurodegeneration. Annual Review of Neuroscience. DOI: 10.1146/annurev-neuro-072116-0311533. Dregni et al. 2022. Fluent molecular mixing of Tau isoforms in Alzheimer’s disease neurofibrillary tangles. Nature communications. DOI: 10.1038/s41467-022-30585-0
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
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