Protein_Domain

Part:BBa_K2946000

Designed by: eden asraf   Group: iGEM19_TelHai-Migal_Israel   (2019-10-02)
Revision as of 17:33, 20 October 2020 by Lavanya karinje (Talk | contribs)


scFv (Single-Chain Variable Fragment)

b31903af2fefc1bd07ef31c08f9846e7-full.png

scFv (single-chain variable fragment) is a fusion protein containing variable domains of the light (VL) and heavy (VH) chains connected by a short peptide linker. The peptide linker is rich in glycine and serine for its flexibility. Features of scFv:

1. Specificity: Though remove of the constant regions, scFv still maintain the binding affinity and specificity of the original immunoglobulin.

2. Efficient: ScFv is smaller than the entire antibody, so it places less stress on the host cell while expressing it. Therefore, the gene attached to it is well expressed.


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 236
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 99


MIT MAHE 2020

Summary

It is a fusion protein containing variable domains of the light (VL) and heavy (VH) chains connected by a short peptide linker. The peptide linker is rich in glycine and serine for its flexibility. Though remove of the constant regions, scFv still maintain the binding affinity and specificity of the original immunoglobulin. ScFv is smaller than the entire antibody, so it places less stress on the host cell while expressing it. Therefore, the gene attached to it is well expressed.

References

1. Berger, M., Shankar, V., & Vafai, A. (2002). Therapeutic applications of monoclonal antibodies. The American journal of the medical sciences, 324(1), 14–30. https://doi.org/10.1097/00000441-200207000-00004

2. Byrne, H., Conroy, P. J., Whisstock, J. C., & O'Kennedy, R. J. (2013). A tale of two specificities: bispecific antibodies for therapeutic and diagnostic applications. Trends in biotechnology, 31(11), 621–632. https://doi.org/10.1016/j.tibtech.2013.08.007

3. Zeng, X., Shen, Z., & Mernaugh, R. (2012). Recombinant antibodies and their use in biosensors. Analytical and bioanalytical chemistry, 402(10), 3027–3038. https://doi.org/10.1007/s00216-011-5569-z

4. Bird, R. E., Hardman, K. D., Jacobson, J. W., Johnson, S., Kaufman, B. M., Lee, S. M., Lee, T., Pope, S. H., Riordan, G. S., & Whitlow, M. (1988). Single-chain antigen-binding proteins. Science (New York, N.Y.), 242(4877), 423–426. https://doi.org/10.1126/science.3140379 "

[edit]
Categories
//collections/immune_regulation/antibodies
Parameters
None