5c2 (Novus Biologicals)
Structured Review
5c2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/5c2/alpha-Synuclein+Antibody+(5C2)+-+BSA+Free/pm40301692-411-52-53
Average 93 stars, based on 7 article reviews
Images
Related Articles
Incubation:Article Title: Flow cytometric isolation of drug-like conformational antibodies specific for amyloid fibrils. Article Snippet: .. 13 Tau dot blots, as reported in Fig. S6A, were next incubated with antibodies at 10 nM (1% nonfat dry milk in 14 TBST) overnight at 4 °C. α-synuclein dot blots, as reported in Fig. S14, were incubated with 50 nM antibody 15 (aS2.1 WT, H2.7, H2.4, H2.3) or a 1000x dilution of Article Title: Facile generation of drug-like conformational antibodies specific for amyloid fibrils. Article Snippet: Antibodies that recognize insoluble antigens, such as amyloid fibrils associated with neurodegenerative disorders, are important for research, diagnostic and therapeutic applications.. However, these types of antibodies are difficult to generate, typically require animal immunization and also commonly require humanization in the case of therapeutic applications.. Here we report a methodology for generating high-quality, fully human, conformation-specific antibodies against amyloid fibrils using a published human nonimmune library, yeast-surface display and quantitative fluorescence-activated cell sorting. Article Title: Flow cytometric isolation of drug-like conformational antibodies specific for amyloid fibrils Article Snippet: .. Tau dot blots, as reported in Fig. S6A , were next incubated with antibodies at 10 nM (1% nonfat dry milk in TBST) overnight at 4 °C. α-synuclein dot blots, as reported in Fig. S14 , were incubated with 50 nM antibody (aS2.1 WT, H2.7, H2.4, H2.3) or a 1000x dilution of Binding Assay:Article Title: Nature-inspired design and evolution of anti-amyloid antibodies Article Snippet: .. Antibody binding was performed by incubating the blocked membranes with 10 ml of 100 n m scFv, 10 n m scFv–Fc fusion, 1:1000 dilution of NAB228 (2 mg/ml stock concentration; A8354, Sigma), 1E1/A6 (stock concentration unknown; 05-804, EMD Millipore), or 1:10,000 of Article Title: Nature-inspired design and evolution of anti-amyloid antibodies Article Snippet: .. Antibody binding was performed by incubating the blocked membranes with 10 mL of 100 nM scFv, 10 nM scFv-Fc fusion, 1:1000 dilution of NAB228 (2 mg/mL stock concentration; A8354, Sigma-Aldrich), 1E1/A6 (stock concentration unknown; 05-804, EMD Millipore) or 1:10000 of Concentration Assay:Article Title: Nature-inspired design and evolution of anti-amyloid antibodies Article Snippet: .. Antibody binding was performed by incubating the blocked membranes with 10 ml of 100 n m scFv, 10 n m scFv–Fc fusion, 1:1000 dilution of NAB228 (2 mg/ml stock concentration; A8354, Sigma), 1E1/A6 (stock concentration unknown; 05-804, EMD Millipore), or 1:10,000 of Article Title: Nature-inspired design and evolution of anti-amyloid antibodies Article Snippet: .. Antibody binding was performed by incubating the blocked membranes with 10 mL of 100 nM scFv, 10 nM scFv-Fc fusion, 1:1000 dilution of NAB228 (2 mg/mL stock concentration; A8354, Sigma-Aldrich), 1E1/A6 (stock concentration unknown; 05-804, EMD Millipore) or 1:10000 of Western Blot:Article Title: Anti-amyloid Compounds Inhibit α-Synuclein Aggregation Induced by Protein Misfolding Cyclic Amplification (PMCA) Article Snippet: .. The anti-α-synuclein antibodies Syn1 (BD Biosciences), Generated:Article Title: Discrimination of MSA-P and MSA-C by RT-QuIC analysis of olfactory mucosa: the first assessment of assay reproducibility between two specialized laboratories Article Snippet: .. Eight μL of αSyn_RT-QuIC products generated by MSA-P and MSA-C samples were treated with PK [2.5 mg/mL] for 1 h at 37 °C under shaking (500 rpm) and immunoblotted with antibodies directed against three different epitopes of α-synuclein: (i) clone |
