Tau-441 (2N4R) and Alpha Synuclein Co-Polymer Fibrils

Tau-441 (2N4R) and Alpha Synuclein Co-Polymer Fibrils

• Background: Brain-specific tau isoforms vary in the number of N-terminal inserts and C- terminal repeat domains due to alternative splicing of exons; the 2N4R isoform of tau is expressed in adult brain yet is absent from the fetal brain (1). Tau and alpha-synuclein polymerize into amyloid fibrils to form filamentous inclusions in neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease. Tau has been shown to interact with alpha-synuclein in vitro (2), with synergistic cross-seeding between tau and alpha-synuclein resulting in polymerization of each other into fibrillary amyloid lesions in neuronal cultures and in vivo (3,4). Recombinant tau and alpha-synuclein co-polymer fibrils have demonstrated a more widespread transmission of induced pathology in a rodent model of tauopathies compared to pure Tau or alpha-synuclein fibrils alone (5). These co-polymer fibrils have also shown enhanced alpha-synuclein aggregation in vitro, and more severe alpha-synuclein pathology and Parkinson’s disease-like symptoms in mice (6).
• Description: Human Recombinant Tau-441 (2N4R) and Human Recombinant Alpha Synuclein Co-Polymer Fibrils
• Product Name Alternative: MAPT, 2N4R, Tau40 neurofibrillary tangle protein, paired-helical filament, PHFs, SNCA, NACP, PARK1, asyn, alpha-synuclein, pre-formed fibril, PFFs, mixed fibrils
• UNSPSC: 12352202
• Swiss Prot: P10636-8 and P37840-1
• Host: E. coli
• Origin Species: Human
• Target: Tau and Alpha Synuclein Co-Polymer
• Conjugation: No Tag
• Sequence: Tau: MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL Asyn: MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
• Applications: WB, SDS PAGE, In vitro assay
• Purification Method: Ion-exchange Purified
• Concentration: Total Protein Concentration: 2mg/mL (1mg/ml of tau and 1mg/ml of aSyn)
• Purity: >95%
• Weight: 0.05
• Length: Full Length (Tau 2N4R: 1-441 aa, ASYN: 1-140 )
• Buffer: 1X PBS pH 7.4
• Molecular Weight: 2N4R: 45.84 kDa, ASYN: 14.46 kDa
• Precautions: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
• Additionnal Information: For corresponding monomers, see catalog# SPR-321 and SPR-479
• References & Citations: 1. Goedert et al. Multiple Isoforms of Human Microtubule-associated Protein Tau: Sequences and Localization in Neurofibrilary Tangles of Alzheimer’s Disease. Neuron. 1989;3(4):519-526. 2. Jensen et al. α-synuclein Binds to Tau and Stimulates the Protein Kinase A-catalyzed Tau Phosphorylation of Serine Residues 262 and 356. 1999. JBC. 274(36): 25481-25489. DOI:https://doi.org/10.1074/jbc.274.36.25481 3. Giasson et al. Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein. Science. 2003; 300: 636-40. DOI: 10.1126/science.1082324 4. Guo et al. Distinct α-synuclein Strains Differentially Promote Tau Inclusions in Neurons. 2013. Cell. 154(1) doi:10.1016/j.cell.2013.05.057. 5. Williams et al. Differential Cross-seeding Properties of Tau and α-synuclein in Mouse Models of Tauopathy and Synucleinopathy. Brain Communications. 2020; 2(2):fcaa090. doi:10.1093/braincomms/fcaa090 6. Pan et al. Tau Accelerates α-synuclein Aggregation and Spreading in Parkinson’s Disease. 2022. Brain. Doi: 10.1093/braiwac171