Mapping of the epitope on lipoprotein lipase recognized by a monoclonal antibody (5D2) which inhibits lipase activity.
A monoclonal antibody, 5D2, which inhibits human lipoprotein lipase (hLPL) activity has been widely used for assessment of LPL immunoreactive mass in the clinical evaluation of patients [1] and for analysis of structure-function relationships of LPL [2,3]. We have mapped the epitope on LPL, recognized by the 5D2 antibody, within residues 396-405. Ala400 is the critical amino acid residue conferring epitope specificity. This knowledge confirms that the C-terminal domain of LPL plays a critical role in LPL activity and also provides important information for studies exploring the structure-function relationship of LPL using this antibody.
Liu
M S
MS
Department of Medical Genetics, University of British Columbia, Vancouver, Canada.
Ma
Y
Y
Hayden
M R
MR
Brunzell
J D
JD
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D002415:Cats; D002417:Cattle; D002645:Chickens; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis*; D006801:Humans; D008071:Lipoprotein Lipase / Q000037:antagonists & inhibitors / Q000097:blood* / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D000911:Antibodies, Monoclonal; D000939:Epitopes; D008071:Lipoprotein Lipase