RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: GS24
Target: Mouse transferrin receptor (TfR-ECD)
Type of nucleic acid: ssDNA
Sequence: 5'GAATTCCGCGTGTGCACACGCTCACAGTTACTATCGCTACGTTCTTTGGTAGTCCGTTCGGGAT3'
Sequence length: 64
GC content: 0.515625
Affinity: Not reported
Pool type: 5'-TAATACGACTCACTATAGGGCGAATTCCGCGTGTGC-49N-GTCCGTTCGGGATCCTC-3'
Pool random region: 49
Binding buffer/conditions: RNA binding buffer 20 mM Na PO4, pH 7.4/120 mM NaCl/2.5 mM KCl/0.12 mM MgSO4/40mM Hepes, pH 7.4)
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research:". In this study, we chose an RNA and a DNA aptamer binding to the extracellular domain of mouse TfR (TfR-ECD) and demonstrated their ability to deliver streptavi_x0002_din to Ltk_x0002_ cells. We then showed the ability of the DNA aptamer to deliver a lysosomal enzyme into deficient mouse fibroblasts and correct the defective glycosaminoglycan (GAG) degradation in these cells
Additional information: DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
After characterization in the model system, the DNA aptamer was conjugated to a lysosomal enzyme, α-l-iduronidase, from which mannose 6-phosphate had been removed. The aptamer had been modified by attachment of terminal glycerol for oxidation by periodate and reaction of the resulting aldehyde with amino groups on the protein.
Reference (2008,Proc Natl Acad Sci U S A): Chen, C. H., Dellamaggiore, K. R., Ouellette, C. P., Sedano, C. D., Lizadjohry, M., Chernis, G. A., Gonzales, M., Baltasar, F. E., Fan, A. L., Myerowitz, R., & Neufeld, E. F. (2008). Aptamer-based endocytosis of a lysosomal enzyme. Proceedings of the National Academy of Sciences of the United States of America, 105(41), 15908–15913. https://doi.org/10.1073/pnas.0808360105
Aptamer: GS24 (truncated version)
Target: Mouse transferrin receptor (TfR-ECD)
Type of nucleic acid: ssDNA
Sequence: 5'GCGTGTGCACACGGTCACTTAGTATCGCTACGTTCTTTGGTTCCGTTCGG3'
Sequence length: 50
GC content: 0.54
Affinity: Not reported
Pool type: 5'-TAATACGACTCACTATAGGGCGAATTCCGCGTGTGC-49N-GTCCGTTCGGGATCCTC-3'
Pool random region: 49
Binding buffer/conditions: RNA binding buffer 20 mM Na PO4, pH 7.4/120 mM NaCl/2.5 mM KCl/0.12 mM MgSO4/40mM Hepes, pH 7.4)
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation: " Of 40 aptamers analyzed, 10 showed significant binding. One aptamer, “GS24,” was truncated to 50 nucleotides based on its folding structure "
Application as quoted in the referenced paper: Research:". In this study, we chose an RNA and a DNA aptamer binding to the extracellular domain of mouse TfR (TfR-ECD) and demonstrated their ability to deliver streptavi_x0002_din to Ltk_x0002_ cells. We then showed the ability of the DNA aptamer to deliver a lysosomal enzyme into deficient mouse fibroblasts and correct the defective glycosaminoglycan (GAG) degradation in these cells
Additional information: DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
After characterization in the model system, the DNA aptamer was conjugated to a lysosomal enzyme, α-l-iduronidase, from which mannose 6-phosphate had been removed. The aptamer had been modified by attachment of terminal glycerol for oxidation by periodate and reaction of the resulting aldehyde with amino groups on the protein.
Reference (2008,Proc Natl Acad Sci U S A): Chen, C. H., Dellamaggiore, K. R., Ouellette, C. P., Sedano, C. D., Lizadjohry, M., Chernis, G. A., Gonzales, M., Baltasar, F. E., Fan, A. L., Myerowitz, R., & Neufeld, E. F. (2008). Aptamer-based endocytosis of a lysosomal enzyme. Proceedings of the National Academy of Sciences of the United States of America, 105(41), 15908–15913. https://doi.org/10.1073/pnas.0808360105