Difference between revisions of "Part:BBa K4375005"
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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.
 
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.
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==Usage and Biology==
 
==Usage and Biology==
  
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Epidermal growth factor (EGF) is a 53-amino acid cytokine (6.2 kDa) that is secreted by ectodermic cells, monocytes, kidneys, and duodenal glands. EGF stimulates growth of epidermal and epithelial cells. EGF and at least seven other growth factors and their transmembrane receptor kinases play important roles in cell proliferation, survival, adhesion, migration, and differentiation. The EGF receptor (EGFR) family consists of four transmembrane receptors, including EGFR (HER1/erbB-1), HER2 (erbB-2/neu), HER3 (erbB-3), and HER4 (erbB-4). HER1 as well as HER2 are overexpressed on many solid tumor cells such as breast, non–small-cell lung, head and neck, and colon cancers. Nanobodies are the smallest intact antigen-binding fragments (15 kDa) isolated from heavy-chain camelid antibodies, and they exhibit efficient and specific tumor targeting. One of them is Nanobody 7D12.
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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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<span class='h3bb'>Sequence and Features</span>
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==Sequence and Features==
 
<partinfo>BBa_K4375005 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4375005 SequenceAndFeatures</partinfo>
  
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==References==
 
  
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==References==
 
https://www.ncbi.nlm.nih.gov/books/NBK97357/
 
https://www.ncbi.nlm.nih.gov/books/NBK97357/
  

Revision as of 12:30, 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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 46
    Illegal AgeI site found at 178
  • 1000
    COMPATIBLE WITH RFC[1000]


References

https://www.ncbi.nlm.nih.gov/books/NBK97357/