Serum albumin is a globular protein which comprises about 50 - 60 % of all
serum proteins. It serves as protein reserve and plays an important role in
osmoregulation. Furthermore, it functions as carrier and binding protein in
the blood circulation system for fatty acids, growth factors, hormones,
metabolites, vitamins etc.. Compared with other proteins, serum albumin is
characterized by the following features:
High solubility in salt-free water
High stability against heat
(especially in the presence of stabilizers such as Na-caprylate) and other
Compatibility with other proteins
These properties and the relatively simple way to isolate it in large
quantities are the reason why there are so many fields of application for
albumin. Using different isolation and purification methods, allows to
manufacture albumins with different properties, e.g. protease-free, fatty
acid-free, low in endotoxins or heavy metals.
ImmunoPrecipitation (IP) is widely used as a method to selectively isolate protein complexes from primary tissues. However, due to lack of specificity and selectivity of most antibodies and unspecific binding of the carrier beads, the method can produce false positives. The ICPL approach, employing stable isotope labelling and mass spectrometry, can discriminate true positive from false positive IP complexes.
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