Difference between revisions of "Team:Dundee/Part Collection"
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| − | + | <figcaption class="caption-center"><p> 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).</p></figcaption> | |
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Revision as of 01:13, 18 September 2015
Part:BBa_K1590000 (hHBA)
FluID- Blood Detection
Coding sequences for human Haemoglobin A. Forms a tetramer consisting of 2 A-chains and 2B-chains (See BBa_K1590001 for Haemboglobin B). Binds to Haptoglobin (BBa_K1590002). It is still being tested if Haptoglobin interacts with either single chain, or if it only binds to the complex.
Part:BBa_K1590001(hHBB)
FluID- Blood Detection
Coding sequences for human Haemoglobin B. Forms a tetramer consisting of 2 A-chains and 2B-chains (See BBa_K1590000 for Haemboglobin A). Binds to Haptoglobin (BBa_K1590002). It is still being tested if Haptoglobin interacts with either single chain, or if it only binds to the complex.
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
Haptoglobin is a binding protein with high affinity for free Haemoglobin.
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.
