Difference between revisions of "Part:BBa K4375005"
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| − | EGFR receptor-specific Nanobody, namely 7D12, | + | EGFR receptor-specific Nanobody, namely 7D12. It was optimized to the E. coli’s codon set, because in this way it gives a bigger yield. This Nanobody has the ability to bind to the EGFR receptor and thus can be used to identify cells expressing the EGFR receptor. |
| − | < | + | <html> |
| − | + | </p> | |
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| + | __TOC__ | ||
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| − | + | ==Usage and Biology== | |
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| + | Nanobodies are monomeric, single-domain antibody fragments derived from camelids and are useful in therapies due to their small size and specific antigen binding. Nanobodies can be expressed in bacterial systems because unlike antibodies, it has no characteristic post-translational modification like glycosylation. They can bind specific targets and when cargo is fused to them, they can be used in targeted therapies. Anti-EGFR nanobody binds to EGFR (Epidermal growth factor Receptor) antigen, a transmembrane receptor often overexpressed on tumor cells, especially HER1 and HER2. EGF binds to them and stimulates migration, proliferation, and survival, which is why EGFR is often targeted in tumor therapies. anti-EGFR Nanobody can bind to EGFR as it is an antibody derivative and it is useful against cancer as it can penetrate solid tumors due to its small, 15 kDa size. | ||
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| + | ==Sequence and Features== | ||
<partinfo>BBa_K4375005 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4375005 SequenceAndFeatures</partinfo> | ||
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| + | ==References== | ||
| + | Karl R. Schmitz, Atrish Bagchi, Rob C. Roovers, Paul M.P. van Bergen en Henegouwen, Kathryn M. Ferguson, | ||
| + | Structural Evaluation of EGFR Inhibition Mechanisms for Nanobodies/VHH Domains, | ||
| + | Structure, Volume 21, Issue 7, 2013, Pages 1214-1224, ISSN 0969-2126, https://doi.org/10.1016/j.str.2013.05.008. | ||
Latest revision as of 19:27, 10 October 2022
anti-EGFR Nanobody (7D12)
EGFR receptor-specific Nanobody, namely 7D12. It was optimized to the E. coli’s codon set, because in this way it gives a bigger yield. This Nanobody has the ability to bind to the EGFR receptor and thus can be used to identify cells expressing the EGFR receptor.
Usage and Biology
Nanobodies are monomeric, single-domain antibody fragments derived from camelids and are useful in therapies due to their small size and specific antigen binding. Nanobodies can be expressed in bacterial systems because unlike antibodies, it has no characteristic post-translational modification like glycosylation. They can bind specific targets and when cargo is fused to them, they can be used in targeted therapies. Anti-EGFR nanobody binds to EGFR (Epidermal growth factor Receptor) antigen, a transmembrane receptor often overexpressed on tumor cells, especially HER1 and HER2. EGF binds to them and stimulates migration, proliferation, and survival, which is why EGFR is often targeted in tumor therapies. anti-EGFR Nanobody can bind to EGFR as it is an antibody derivative and it is useful against cancer as it can penetrate solid tumors due to its small, 15 kDa size.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 46
Illegal AgeI site found at 178 - 1000COMPATIBLE WITH RFC[1000]
References
Karl R. Schmitz, Atrish Bagchi, Rob C. Roovers, Paul M.P. van Bergen en Henegouwen, Kathryn M. Ferguson, Structural Evaluation of EGFR Inhibition Mechanisms for Nanobodies/VHH Domains, Structure, Volume 21, Issue 7, 2013, Pages 1214-1224, ISSN 0969-2126, https://doi.org/10.1016/j.str.2013.05.008.