Difference between revisions of "Part:BBa K1189025"
| Line 5: | Line 5: | ||
</p> | </p> | ||
| + | <html> | ||
<figure> | <figure> | ||
<img src="https://static.igem.org/mediawiki/2013/1/18/UCalgary2013TRFerritinrender2png.png" alt="Ferritin" width="300" height="300"> | <img src="https://static.igem.org/mediawiki/2013/1/18/UCalgary2013TRFerritinrender2png.png" alt="Ferritin" width="300" height="300"> | ||
| Line 11: | Line 12: | ||
</figcaption> | </figcaption> | ||
</figure> | </figure> | ||
| + | </html> | ||
<p> | <p> | ||
Revision as of 11:18, 28 September 2013
Heavy chain human ferritin
This heavy ferritin chain comes from humans. This part along with light ferritin (BBa_K1189024), form the ferritin nanoparticle, an iron-storage particle made up of 24 subunits. The formed nanoparticle is highly robust, remaining stable at extreme pHs and temperatures. The difference between light ferritin is that this chain contains a ferroxidase centre. Protein domains which orient toward the core of ferritin molecules cause the oxidation of intracellular iron from Fe^2+ to Fe^3+ to initiate formation of a ferrihydrite core.
Figure 1. Ribbon visualization of a fully assembled ferritin protein.
This nanoparticle can also be used as a reporter when the iron core is modified with potassium ferrocyanide to form Prussian Blue. The Prussian Blue ferritin can then act as a peroxidase mimic, similar to horseradish peroxidase, resulting in colour changes in the presence of hydrogen peroxide, and TMB or ABTS.
This part was primarily used to construct BBa_K1189019 in order to allow us to express and purify the protein.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]