Abstract
The low-density lipoprotein receptor-related protein (LRP) is a large multifunctional cell surface membrane receptor capable of binding over 50 ligands. These include molecules important in Alzheimer's disease such as the amyloid beta-protein precursor (A beta PP), the beta-amyloid (A beta) peptide and apolipoprotein E (ApoE). Full length LRP consists of a 515 kDa extracellular ligand binding alpha-chain and an 85 kDa membrane spanning beta-chain. A soluble form of LRP (sLRP) present in human plasma retains the ability to bind ligands, including A beta. This soluble form is an ectodomain fragment generated from the membrane bound form of the receptor by proteolytic cleavage. Here we report data demonstrating that some commercial 'serum-free' supplements and 'serum-free' media contain unlisted sLRP immunoreactive species that may reflect the presence of undefined serum protein extracts in these 'serum-free' preparations. This has the potential to interfere with experimental results and interpretation in a range of cell culture studies involving LRP or any of its ligands and possibly also other serum proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 110-116 |
| Number of pages | 7 |
| Journal | Analytical Methods |
| Volume | 9 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2017 |
Keywords
- body fluids
- cell culture
- cell membranes
- glycoproteins
- ligands
- lipoproteins
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