Difference between revisions of "Team:Dundee/Part Collection"
| Line 19: | Line 19: | ||
<h1>Part:BBa_K1590000 (<i>hHBA</i>) </h1> | <h1>Part:BBa_K1590000 (<i>hHBA</i>) </h1> | ||
<h2> FluID- Blood Detection</h2> | <h2> FluID- Blood Detection</h2> | ||
| − | <p>Coding | + | <p>Coding sequence for Human haemoglobin A. Haemoglobin is the tetrameric protein molecule in red blood cells that carries oxygen. It is composed of four polypeptide chains, which in adults consist of two alpha (a) globin chains and two beta (b) globin chains. In blood plasma, haptoglobin binds free haemoglobin released from red blood cells, inhibiting its oxidative activity. The haptoglobin-hemoglobin complex can then be removed by the reticuloendothelial system which is a part of the immune system. Despite this, haemoglobin is still found free in the blood plasma at a concentration of up to 0.1g/l and this is what we hope to detect. |
| + | .</p> | ||
<div class="button-center"><a role="button" class="btn btn-lg btn-primary" href="http://parts.igem.org/Part:BBa_K1590000">Registry page for this part</a></div> | <div class="button-center"><a role="button" class="btn btn-lg btn-primary" href="http://parts.igem.org/Part:BBa_K1590000">Registry page for this part</a></div> | ||
</div> | </div> | ||
| Line 42: | Line 43: | ||
<h2>FluID- Blood Detection</h2> | <h2>FluID- Blood Detection</h2> | ||
| − | <p>Coding | + | <p>Coding sequence for Human haemoglobin B. Haemoglobin is the tetrameric protein molecule in red blood cells that carries oxygen. It is composed of four polypeptide chains, which in adults consist of two alpha (a) globin chains and two beta (b) globin chains. In blood plasma, haptoglobin binds free haemoglobin released from red blood cells, inhibiting its oxidative activity. The haptoglobin-hemoglobin complex can then be removed by the reticuloendothelial system which is a part of the immune system. Despite this, haemoglobin is still found free in the blood plasma at a concentration of up to 0.1g/l and this is what we hope to detect. |
| + | </p> | ||
<div class="button-center"><a role="button" class="btn btn-lg btn-primary" href="http://parts.igem.org/Part:BBa_K1590001">Registry page for this part</a></div> | <div class="button-center"><a role="button" class="btn btn-lg btn-primary" href="http://parts.igem.org/Part:BBa_K1590001">Registry page for this part</a></div> | ||
</div> | </div> | ||
| Line 69: | Line 71: | ||
<h2> FluID - Blood Detection</h2> | <h2> FluID - Blood Detection</h2> | ||
| − | <p> | + | <p>Coding sequence for Human haptoglobin.Haemoglobin is the tetrameric protein molecule in red blood cells that carries oxygen. It is composed of four polypeptide chains, which in adults consist of two alpha (a) globin chains and two beta (b) globin chains. In blood plasma, haptoglobin binds free haemoglobin released from red blood cells, inhibiting its oxidative activity. The haptoglobin-hemoglobin complex can then be removed by the reticuloendothelial system which is a part of the immune system. Despite this, haemoglobin is still found free in the blood plasma at a concentration of up to 0.1g/l and this is what we hope to detect. </p> |
<div class="button-center"><a role="button" class="btn btn-lg btn-primary" href="http://parts.igem.org/Part:BBa_K1590002">Registry page for this part</a></div> | <div class="button-center"><a role="button" class="btn btn-lg btn-primary" href="http://parts.igem.org/Part:BBa_K1590002">Registry page for this part</a></div> | ||
</div> | </div> | ||
Revision as of 01:25, 18 September 2015
Part:BBa_K1590000 (hHBA)
FluID- Blood Detection
Coding sequence for Human haemoglobin A. Haemoglobin is the tetrameric protein molecule in red blood cells that carries oxygen. It is composed of four polypeptide chains, which in adults consist of two alpha (a) globin chains and two beta (b) globin chains. In blood plasma, haptoglobin binds free haemoglobin released from red blood cells, inhibiting its oxidative activity. The haptoglobin-hemoglobin complex can then be removed by the reticuloendothelial system which is a part of the immune system. Despite this, haemoglobin is still found free in the blood plasma at a concentration of up to 0.1g/l and this is what we hope to detect. .
Part:BBa_K1590001(hHBB)
FluID- Blood Detection
Coding sequence for Human haemoglobin B. Haemoglobin is the tetrameric protein molecule in red blood cells that carries oxygen. It is composed of four polypeptide chains, which in adults consist of two alpha (a) globin chains and two beta (b) globin chains. In blood plasma, haptoglobin binds free haemoglobin released from red blood cells, inhibiting its oxidative activity. The haptoglobin-hemoglobin complex can then be removed by the reticuloendothelial system which is a part of the immune system. Despite this, haemoglobin is still found free in the blood plasma at a concentration of up to 0.1g/l and this is what we hope to detect.
Characterisation of haemoglobin beta following SEC (size exclusion chromatography). A) The sample of concentrated fractions containing haemoglobin beta from nickel affinity purification was loaded onto a SEC column and the protein was eluted. B) 10µl of each fraction corresponding to the two observed peaks was mixed with 10µl of laemmli buffer and loaded onto a SDS gel (12.5% acrylamide). The bands observable on the gel are in line with the expected size of haemoglobin beta - 16kDa. C) Western blotting was then carried out against an anti-his antibody to confirm the presence of hHHB- His.
Part:BBa_K1590002(hHBN)
FluID - Blood Detection
Coding sequence for Human haptoglobin.Haemoglobin is the tetrameric protein molecule in red blood cells that carries oxygen. It is composed of four polypeptide chains, which in adults consist of two alpha (a) globin chains and two beta (b) globin chains. In blood plasma, haptoglobin binds free haemoglobin released from red blood cells, inhibiting its oxidative activity. The haptoglobin-hemoglobin complex can then be removed by the reticuloendothelial system which is a part of the immune system. Despite this, haemoglobin is still found free in the blood plasma at a concentration of up to 0.1g/l and this is what we hope to detect.
Characterization of Human haptoglobin following nickel affinity FPLC. A) Chromatogram showing the purification profile of the His-tagged Human haptoglobin. The fractions corresponding to the two peaks observed on the chromatograph were further analysed western blotting. B) 10µl of the fractions A8-A10 were mixed with 10µl of laemmli buffer and samples separated by SDS-PAGE (12.5% acrylamide) and transferred to a nitrocellulose membrane and probed with an anti-His antibody. The western blot shows successful production of hHHB – His (expected size 45kDa).
Lanosterol Synthase
Fingerprint Aging
Pellentesque habitant morbi tristique senectus et netus et malesuada fames ac turpis egestas. Vestibulum tortor quam, feugiat vitae, ultricies eget, tempor sit amet, ante. Donec eu libero sit amet quam egestas semper. Aenean ultricies mi vitae est. Mauris placerat eleifend leo.
Lanosterol Synthase
Fingerprint Aging
Pellentesque habitant morbi tristique senectus et netus et malesuada fames ac turpis egestas. Vestibulum tortor quam, feugiat vitae, ultricies eget, tempor sit amet, ante. Donec eu libero sit amet quam egestas semper. Aenean ultricies mi vitae est. Mauris placerat eleifend leo.
Lanosterol Synthase
Fingerprint Aging
Pellentesque habitant morbi tristique senectus et netus et malesuada fames ac turpis egestas. Vestibulum tortor quam, feugiat vitae, ultricies eget, tempor sit amet, ante. Donec eu libero sit amet quam egestas semper. Aenean ultricies mi vitae est. Mauris placerat eleifend leo.
Lanosterol Synthase
Fingerprint Aging
Pellentesque habitant morbi tristique senectus et netus et malesuada fames ac turpis egestas. Vestibulum tortor quam, feugiat vitae, ultricies eget, tempor sit amet, ante. Donec eu libero sit amet quam egestas semper. Aenean ultricies mi vitae est. Mauris placerat eleifend leo.
Lanosterol Synthase
Fingerprint Aging
Pellentesque habitant morbi tristique senectus et netus et malesuada fames ac turpis egestas. Vestibulum tortor quam, feugiat vitae, ultricies eget, tempor sit amet, ante. Donec eu libero sit amet quam egestas semper. Aenean ultricies mi vitae est. Mauris placerat eleifend leo.
