Difference between revisions of "Part:BBa K3117040"
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| − | The constant region 1 (CH1) within an antibody. Together with the single chain variable fragment and the Igk light chain, the constant region 1 forms the antigen-binding fragment (Fab) of an antibody. Ig are heterodimeric proteins composed of two H and two L chains. Each L chain contains either a Ck or a Cl and a VL domain that helps define the Ag-binding site of the Ab. In addition to a variable domain, each H chain contains between three and four constant domains that specify the effector function of the Ab. | + | The constant region 1 (CH1) within an antibody. Together with the single chain variable fragment and the Igk light chain, the constant region 1 forms the antigen-binding fragment (Fab) of an antibody. Ig are heterodimeric proteins composed of two H and two L chains. Each L chain contains either a Ck or a Cl and a VL domain that helps define the Ag-binding site of the Ab. In addition to a variable domain, each H chain contains between three and four constant domains that specify the effector function of the Ab. |
==References== | ==References== | ||
Latest revision as of 18:16, 23 October 2020
constant region 1 (CH1) of an antibody
Usage and Biology
Part BBa_K3117039 is the constant region 1 (CH1) within an antibody. Together with the single chain variable fragment and the Igk light chain (BBa_K3117039) the constant region 1 forms the antigen-binding fragment (Fab) of an antibody.
MIT_MAHE 2020
Summary
The constant region 1 (CH1) within an antibody. Together with the single chain variable fragment and the Igk light chain, the constant region 1 forms the antigen-binding fragment (Fab) of an antibody. Ig are heterodimeric proteins composed of two H and two L chains. Each L chain contains either a Ck or a Cl and a VL domain that helps define the Ag-binding site of the Ab. In addition to a variable domain, each H chain contains between three and four constant domains that specify the effector function of the Ab.
References
1. Kaplon, H., & Reichert, J. M. (2019). Antibodies to watch in 2019. mAbs, 11(2), 219–238. https://doi.org/10.1080/19420862.2018.1556465
2. Kaplon, H., & Reichert, J. M. (2018). Antibodies to watch in 2018. mAbs, 10(2), 183–203. https://doi.org/10.1080/19420862.2018.1415671
3. Gilliland, G. L., Luo, J., Vafa, O., & Almagro, J. C. (2012). Leveraging SBDD in protein therapeutic development: antibody engineering. Methods in molecular biology (Clifton, N.J.), 841, 321–349. https://doi.org/10.1007/978-1-61779-520-6_14
4. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., & Bourne, P. E. (2000). The Protein Data Bank. Nucleic acids research, 28(1), 235–242. https://doi.org/10.1093/nar/28.1.235
5. Pritsch, O., Hudry-Clergeon, G., Buckle, M., Petillot, Y., Bouvet, J. P., Gagnon, J., & Dighiero, G. (1996). Can immunoglobulin C(H)1 constant region domain modulate antigen binding affinity of antibodies?. The Journal of clinical investigation, 98(10), 2235–2243. https://doi.org/10.1172/JCI119033 "