Difference between revisions of "Part:BBa K4897020"
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===What is it?===
 
===What is it?===
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For our project, we applied polyhistidine tags to capsular antigen fragments 1 (Caf1). This protein attaches to other Caf1-His proteins as well as Capsular antigen fragment 1-Antimicrobial peptides (BBa_K4897007) through the property of Caf1 in its ability to form polymers under cool conditions, contrasting from the monomer form of the protein when heated. Through his-tag antibodies, individual his-tags are connected together from separate polymers, forming an even more stable net shape. Moreover, protein A/G can be attached to his-tag antibodies. Subsequently, protein A/G magnetic beads can attach to the protein A/G’s, allowing the removal of Caf1 as a whole using a magnet.  
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For our project, we applied polyhistidine tags to capsular antigen fragments 1 (Caf1). This protein attaches to other Caf1-His proteins as well as other caf1 network proteins like Capsular antigen fragment 1-Antimicrobial peptides (BBa_K4897007) through the property of Caf1 in its ability to form polymers under cool conditions, contrasting from the monomer form of the protein when heated. Through his-tag antibodies, individual his-tags are connected together from separate polymers, forming a net shape. Moreover, protein A/G can be attached to his-tag antibodies. Subsequently, protein A/G magnetic beads can attach to the protein A/G’s, allowing the removal of Caf1 as a whole using a magnet.  
  
 
===Usage and Biology===
 
===Usage and Biology===

Revision as of 00:29, 10 October 2023


Caf1-His protein

What is it?

For our project, we applied polyhistidine tags to capsular antigen fragments 1 (Caf1). This protein attaches to other Caf1-His proteins as well as other caf1 network proteins like Capsular antigen fragment 1-Antimicrobial peptides (BBa_K4897007) through the property of Caf1 in its ability to form polymers under cool conditions, contrasting from the monomer form of the protein when heated. Through his-tag antibodies, individual his-tags are connected together from separate polymers, forming a net shape. Moreover, protein A/G can be attached to his-tag antibodies. Subsequently, protein A/G magnetic beads can attach to the protein A/G’s, allowing the removal of Caf1 as a whole using a magnet.

Usage and Biology

By forming a net structure with his-tag antibodies, we have been able to use these proteins to trap P. acne ahead of time before initiating inhibition of the bacteria. Moreover, the interaction with protein A/G assists with the removal of the P. acne as well as the protein post-inhibition.

Fig. 1. Caf1-His Protein Interactions

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
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


References

[1] Dura, Gema, et al. “A thermally reformable protein polymer.” Chem, vol. 6, no. 11, 5 Nov. 2020, pp. 3132–3151, https://doi.org/10.1016/j.chempr.2020.09.020. [2] “His-Tagged Proteins–Production and Purification: Thermo Fisher Scientific.” ThermoFisher, www.thermofisher.cn/cn/zh/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/his-tagged-proteins-production-purification.html. Accessed 9 Oct. 2023.