Difference between revisions of "Part:BBa K1202100"

 
Line 3: Line 3:
  
 
This is the primary section of NanoFactory design. This part is one of the active domains of anti-EpCAM (Epithelial Cell Adhesion Molecule) antibody. We use this part in our NanoFactory system as a binding zone to EpCAM antigen. We added additional histidine tag for purification purposes. Also we added a linker sequence; thus, we want to prevent misfolding in our proteins.  
 
This is the primary section of NanoFactory design. This part is one of the active domains of anti-EpCAM (Epithelial Cell Adhesion Molecule) antibody. We use this part in our NanoFactory system as a binding zone to EpCAM antigen. We added additional histidine tag for purification purposes. Also we added a linker sequence; thus, we want to prevent misfolding in our proteins.  
 +
 
Epithelial Cell Adhesion Molecule (EpCAM) is a outer-cell antigen whose expression is elevated in some cancer types such as colon and breast. This difference makes this antigen a prospective cancer marker and it is planned to be used as an detection technique in immunochemistry for the grading and determining the aggressiveness of tumor.
 
Epithelial Cell Adhesion Molecule (EpCAM) is a outer-cell antigen whose expression is elevated in some cancer types such as colon and breast. This difference makes this antigen a prospective cancer marker and it is planned to be used as an detection technique in immunochemistry for the grading and determining the aggressiveness of tumor.
 +
 
Anti-EpCAM antibody has three binding domains for EpCAM antigen, each of them have different binding affinity.(REF) During our researches, we determined that the best choice would be C215 binding domain with the greatest binding affinity. This would allow us bind EpCAM antigen specifically and more efficiently.
 
Anti-EpCAM antibody has three binding domains for EpCAM antigen, each of them have different binding affinity.(REF) During our researches, we determined that the best choice would be C215 binding domain with the greatest binding affinity. This would allow us bind EpCAM antigen specifically and more efficiently.
 +
 
With the help of effective binding of C215, we hope to conduct accumulation of our NanoFactories on cancer cells, which hopefully ends up with amassing AI-2 units in the media and bacteria. AI-2 accumulation will start the production of cancer killing peptides.
 
With the help of effective binding of C215, we hope to conduct accumulation of our NanoFactories on cancer cells, which hopefully ends up with amassing AI-2 units in the media and bacteria. AI-2 accumulation will start the production of cancer killing peptides.
  

Latest revision as of 23:45, 4 October 2013

Nanofactory Binding Zone (C215)

This is the primary section of NanoFactory design. This part is one of the active domains of anti-EpCAM (Epithelial Cell Adhesion Molecule) antibody. We use this part in our NanoFactory system as a binding zone to EpCAM antigen. We added additional histidine tag for purification purposes. Also we added a linker sequence; thus, we want to prevent misfolding in our proteins.

Epithelial Cell Adhesion Molecule (EpCAM) is a outer-cell antigen whose expression is elevated in some cancer types such as colon and breast. This difference makes this antigen a prospective cancer marker and it is planned to be used as an detection technique in immunochemistry for the grading and determining the aggressiveness of tumor.

Anti-EpCAM antibody has three binding domains for EpCAM antigen, each of them have different binding affinity.(REF) During our researches, we determined that the best choice would be C215 binding domain with the greatest binding affinity. This would allow us bind EpCAM antigen specifically and more efficiently.

With the help of effective binding of C215, we hope to conduct accumulation of our NanoFactories on cancer cells, which hopefully ends up with amassing AI-2 units in the media and bacteria. AI-2 accumulation will start the production of cancer killing peptides.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 7
    Illegal NheI site found at 30
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]