RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: RAB1
Target: Staphylococcus aureus (S. aureus) surface molecules
Type of nucleic acid: ssDNA
Sequence: 5'TAGCTCACTCATTAGGCACGGGTGGGCTCCAATATGAATCGCTTGCCCTGACGCTATCTGCATAGTTAAGCCAGCC3'
Sequence length: 76
GC content: 0.5263157894736842
Affinity: Kd: 56 ± 87 nmol/mL
Pool type: 5`-TAGCTCACTCATTAGGCAC-N40-GCATAGTTAAGCCAGCC-3`
Pool random region: 40
Binding buffer/conditions: Binding buffer (BB) containing bovine serum albumin (BSA)
Buffer type: Other Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " In the present study, a high throughput whole cell SELEX method has been applied successfully in selecting specific aptamers against whole cells of Staphylococcus aureus, a potent food poisoning bacterium. The established assay could be a reliable detection tool for the routine investigation of Staphylococcus aureus in samples from food and clinical sources."
Reference (2017, Int J Food Microbiol ): Ramlal, S., Mondal, B., Lavu, P. S., N, B., & Kingston, J. (2018). Capture and detection of Staphylococcus aureus with dual labeled aptamers to cell surface components. International journal of food microbiology, 265, 74–83. https://doi.org/10.1016/j.ijfoodmicro.2017.11.002
Aptamer: RAB3
Target: Staphylococcus aureus (S. aureus) surface molecules
Type of nucleic acid: ssDNA
Sequence: 5'TAGCTCACTCATTAGGCACCGTAGTCTAGTGTCGATTAGTTTCCTTGAGACCTTGTGCTGCATAGTTAAGCCAGCC3'
Sequence length: 76
GC content: 0.4736842105263157
Affinity: Kd: 37 ± 112 nmol/mL
Pool type: 5`-TAGCTCACTCATTAGGCAC-N40-GCATAGTTAAGCCAGCC-3`
Pool random region: 40
Binding buffer/conditions: Binding buffer (BB) containing bovine serum albumin (BSA)
Buffer type: Other Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " In the present study, a high throughput whole cell SELEX method has been applied successfully in selecting specific aptamers against whole cells of Staphylococcus aureus, a potent food poisoning bacterium. The established assay could be a reliable detection tool for the routine investigation of Staphylococcus aureus in samples from food and clinical sources."
Reference (2017, Int J Food Microbiol ): Ramlal, S., Mondal, B., Lavu, P. S., N, B., & Kingston, J. (2018). Capture and detection of Staphylococcus aureus with dual labeled aptamers to cell surface components. International journal of food microbiology, 265, 74–83. https://doi.org/10.1016/j.ijfoodmicro.2017.11.002
Aptamer: RAB5
Target: Staphylococcus aureus (S. aureus) surface molecules
Type of nucleic acid: ssDNA
Sequence: 5'TAGCTCACTCATTAGGCACCGTAGTCTAGTGTCGATTAGTTTCCTTGCTATTGCAGACCTTGTGCTGCATAGTTAAGCCAGCC3'
Sequence length: 83
GC content: 0.4698795180722891
Affinity: Kd: 58 ± 14 nmol/mL
Pool type: 5`-TAGCTCACTCATTAGGCAC-N40-GCATAGTTAAGCCAGCC-3`
Pool random region: 40
Binding buffer/conditions: Binding buffer (BB) containing bovine serum albumin (BSA)
Buffer type: Other Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " In the present study, a high throughput whole cell SELEX method has been applied successfully in selecting specific aptamers against whole cells of Staphylococcus aureus, a potent food poisoning bacterium. The established assay could be a reliable detection tool for the routine investigation of Staphylococcus aureus in samples from food and clinical sources."
Reference (2017, Int J Food Microbiol ): Ramlal, S., Mondal, B., Lavu, P. S., N, B., & Kingston, J. (2018). Capture and detection of Staphylococcus aureus with dual labeled aptamers to cell surface components. International journal of food microbiology, 265, 74–83. https://doi.org/10.1016/j.ijfoodmicro.2017.11.002
Aptamer: RAB10
Target: Staphylococcus aureus (S. aureus) surface molecules
Type of nucleic acid: ssDNA
Sequence: 5'TAGCTCACTCATTAGGCACTCGAGAGGGATCTCGGGGCGTGCGATGATTTTGCCTTCATGCATAGTTAAGCCAGCC3'
Sequence length: 76
GC content: 0.5263157894736842
Affinity: Kd: 46 ± 24 nmol/mL
Pool type: 5`-TAGCTCACTCATTAGGCAC-N40-GCATAGTTAAGCCAGCC-3`
Pool random region: 40
Binding buffer/conditions: Binding buffer (BB) containing bovine serum albumin (BSA)
Buffer type: Other Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " In the present study, a high throughput whole cell SELEX method has been applied successfully in selecting specific aptamers against whole cells of Staphylococcus aureus, a potent food poisoning bacterium. The established assay could be a reliable detection tool for the routine investigation of Staphylococcus aureus in samples from food and clinical sources."
Reference (2017, Int J Food Microbiol ): Ramlal, S., Mondal, B., Lavu, P. S., N, B., & Kingston, J. (2018). Capture and detection of Staphylococcus aureus with dual labeled aptamers to cell surface components. International journal of food microbiology, 265, 74–83. https://doi.org/10.1016/j.ijfoodmicro.2017.11.002
Aptamer: RAB20
Target: Staphylococcus aureus (S. aureus) surface molecules
Type of nucleic acid: ssDNA
Sequence: 5'TAGCTCACTCATTAGGCACGCGTTACGTTAGTGGCCGCCTATGAGGACAGGCGGTTGTAGCATAGTTAAGCCAGCC3'
Sequence length: 76
GC content: 0.5394736842105263
Affinity: Kd: 128 ± 45 nmol/mL
Pool type: 5`-TAGCTCACTCATTAGGCAC-N40-GCATAGTTAAGCCAGCC-3`
Pool random region: 40
Binding buffer/conditions: Binding buffer (BB) containing bovine serum albumin (BSA)
Buffer type: Other Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " In the present study, a high throughput whole cell SELEX method has been applied successfully in selecting specific aptamers against whole cells of Staphylococcus aureus, a potent food poisoning bacterium. The established assay could be a reliable detection tool for the routine investigation of Staphylococcus aureus in samples from food and clinical sources."
Reference (2017, Int J Food Microbiol ): Ramlal, S., Mondal, B., Lavu, P. S., N, B., & Kingston, J. (2018). Capture and detection of Staphylococcus aureus with dual labeled aptamers to cell surface components. International journal of food microbiology, 265, 74–83. https://doi.org/10.1016/j.ijfoodmicro.2017.11.002
Aptamer: RAB28
Target: Staphylococcus aureus (S. aureus) surface molecules
Type of nucleic acid: ssDNA
Sequence: 5'TAGCTCACTCATTAGGCACTGGACGTCGTGGCGGAGGTTTTATAAAACGGCGCCACTGTGCATAGTTAAGCCAGCC3'
Sequence length: 76
GC content: 0.5263157894736842
Affinity: Kd: 49 ± 39 nmol/mL
Pool type: 5`-TAGCTCACTCATTAGGCAC-N40-GCATAGTTAAGCCAGCC-3`
Pool random region: 40
Binding buffer/conditions: Binding buffer (BB) containing bovine serum albumin (BSA)
Buffer type: Other Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " In the present study, a high throughput whole cell SELEX method has been applied successfully in selecting specific aptamers against whole cells of Staphylococcus aureus, a potent food poisoning bacterium. The established assay could be a reliable detection tool for the routine investigation of Staphylococcus aureus in samples from food and clinical sources."
Reference (2017, Int J Food Microbiol ): Ramlal, S., Mondal, B., Lavu, P. S., N, B., & Kingston, J. (2018). Capture and detection of Staphylococcus aureus with dual labeled aptamers to cell surface components. International journal of food microbiology, 265, 74–83. https://doi.org/10.1016/j.ijfoodmicro.2017.11.002
Aptamer: RAB35
Target: Staphylococcus aureus (S. aureus) surface molecules
Type of nucleic acid: ssDNA
Sequence: 5'TAGCTCACTCATTAGGCACGGGGGGTTGTGCCATTTAAGATGACCGGTTGCCGCGATTTGCATAGTTAAGCCAGCC3'
Sequence length: 76
GC content: 0.5263157894736842
Affinity: Kd: 34 ± 5 nmol/mL
Pool type: 5`-TAGCTCACTCATTAGGCAC-N40-GCATAGTTAAGCCAGCC-3`
Pool random region: 40
Binding buffer/conditions: Binding buffer (BB) containing bovine serum albumin (BSA)
Buffer type: Other Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " In the present study, a high throughput whole cell SELEX method has been applied successfully in selecting specific aptamers against whole cells of Staphylococcus aureus, a potent food poisoning bacterium. The established assay could be a reliable detection tool for the routine investigation of Staphylococcus aureus in samples from food and clinical sources."
Reference (2017, Int J Food Microbiol ): Ramlal, S., Mondal, B., Lavu, P. S., N, B., & Kingston, J. (2018). Capture and detection of Staphylococcus aureus with dual labeled aptamers to cell surface components. International journal of food microbiology, 265, 74–83. https://doi.org/10.1016/j.ijfoodmicro.2017.11.002
Aptamer: MAMB1
Target: Mammaglobin B (MGB2)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACCCAACGTCGAACTGAATCCCGTGTCCTTTGAGAACTGACTCATAC3'
Sequence length: 65
GC content: 0.4615384615384615
Affinity: Kd: 13 ± 3 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMB4
Target: Mammaglobin B (MGB2)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACGCGGCATGTTGGCATCTTGGTCCTGCTTTGAGAACTGACTCATAC3'
Sequence length: 65
GC content: 0.4769230769230769
Affinity: Kd: 105 ± 20 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMB8
Target: Mammaglobin B (MGB2)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACCACGACACGCGCGATCGTCTCACTGCTTTGAGAACTGACTCATAC3'
Sequence length: 65
GC content: 0.4923076923076923
Affinity: Kd: 78 ± 15 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMB12
Target: Mammaglobin B (MGB2)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACCCACCACACAGCGGATACACCATGGCTTTGAGAACTGACTCATAC3'
Sequence length: 65
GC content: 0.4769230769230769
Affinity: Kd: 19 ± 5 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMB57
Target: Mammaglobin B (MGB2)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACCCGAAGAGGATGTGCGGTCCCATTGCTTTGAGAACTGACTCATAC3'
Sequence length: 65
GC content: 0.4769230769230769
Affinity: Kd: 72 ± 9 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMA2
Target: Mammaglobin A (MGB1)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACCCGGGACAGAACGTGCGCTTTGAGCTTTGAGAACTGACTCATAC3'
Sequence length: 64
GC content: 0.484375
Affinity: Kd: 3 ± 1 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMA5
Target: Mammaglobin A (MGB1)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACGGTTGGCATCTTGGTCCTGCTTTGCTTTGAGAACTGACTCATAC3'
Sequence length: 64
GC content: 0.453125
Affinity: Kd: 54 ± 13 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMA6
Target: Mammaglobin A (MGB1)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACTGTTGGCATCTTGGTCCTGCTTTGCTTTGAGAACTGACTCATAC3'
Sequence length: 64
GC content: 0.4375
Affinity: Kd: 49 ± 20 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: MAMA12
Target: Mammaglobin A (MGB1)
Type of nucleic acid: ssDNA
Sequence: 5'CATGCTTACCTATAGTGAACGTTGGCATCTTGGTCCTGCTTTGACTTTGAGAACTGACTCATAC3'
Sequence length: 64
GC content: 0.4375
Affinity: Kd: 8 ± 3 nM
Pool type: 5′-CATGCTTACCTATAGTGAAC-N24-CTTTGAGAACTGACTCTAC-3′
Pool random region: 24
Binding buffer/conditions: 150 mM Tris, 150 mM NaCl, 5 mM KCl, 5 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 10 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " Mammaglobin B (MGB2) and mammaglobin A (MGB1) are proteins expressed in metastatic breast cancers. The early detection of circulating tumor cells (CTCs) in breast cancer patients is crucial to decrease mortality rate. Herein, novel aptamers were successfully selected and characterized against MGB2 and MGB1 proteins using a hybrid SELEX approach. The results obtained in this study indicate the great potential for the use of aptamers to detect MGB1 and MGB2 protein biomarkers, expressed on the surface of breast CTCs."
Reference (2017, Sci Rep ): Hassan, E. M., Willmore, W. G., McKay, B. C., & DeRosa, M. C. (2017). In vitro selections of mammaglobin A and mammaglobin B aptamers for the recognition of circulating breast tumor cells. Scientific reports, 7(1), 14487. https://doi.org/10.1038/s41598-017-13751-z
Aptamer: Apt51
Target: Interleukin 2 receptor alpha (IL2Rα CD25)
Type of nucleic acid: ssDNA
Sequence: 5′GCTGTGTGACTCCTGCAAATATAGCGGGCAGGGGTGGGGGGGTGTTTGCGGCTCTGGGATCGCAGCTGTATCTTGTCTCC3′
Sequence length: 80
GC content: 0.6
Affinity: Kd: 13.4 nM
Pool type: 5′-GCTGTGTGACTCCTGCAA-N43-GCAGCTGTATCTTGTCTCC-3′
Pool random region: 43
Binding buffer/conditions: 50 mM K2HPO4 pH 7.5, 150 mM NaCl, 0.05% Tween-20, BSA 1 μg/ml, 0.1 mg/ml yeast tRNA
Buffer type: PBS/phosphate buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " High levels of CD25, as part of the IL-2 receptor, are expressed on the surface of the activated T lymphocytes and regulatory T cells, indicating that the soluble CD25 (sCD25) could be a clinically valuable tool for treating several diseases. In the current study, generation of an ssDNA aptamer (Apt51) against CD25 is reported. Apt51 bound to CD25 with high affinity (Kd=13.4nM) and specificity. Apt51 showed good affinity and selectivity for the recognition of CD25 on the cell surface. Importantly, the study showed that Apt51 interfered with the binding of CD25 to its ligand (IL 2) and consequently decreased the IL-2-induced Akt activation."
Reference (2017, Int Immunopharmacol ): Shahdordizadeh, M., Taghdisi, S. M., Sankian, M., Ramezani, M., & Abnous, K. (2017). Design, isolation and evaluation of the binding efficiency of a DNA aptamer against interleukin 2 receptor alpha, in vitro. International immunopharmacology, 53, 96–104. https://doi.org/10.1016/j.intimp.2017.10.011