SILu^™Prot APOA2 Apolipoprotein A-II human

Apolipoprotein A-II (ApoA-II) occurs in plasma as a dimer of two 77-amino acid chains linked by a disulfide bridge. After apoA-I, it is the second major protein component of HDL, accounting for approximately 20% of HDL total protein. ApoA-II is thought to play an important role in triglyceride metabolism both from animal and human studies. 3 Recent findings attribute apoA-II to inhibitory effects on lipoprotein lipase-mediated hydrolysis of triglyceride-rich particles. Additional associations of apoA-II have been reported for a variety of protein factors including hepatic lipase (HL), lipoprotein lipase (LPL), endothelial lipase, CETP, PLTP, and LCAT.

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SILu^™ Prot APOA2 is a recombinant, stable isotope-labeled human APOA2 which incorporates [¹³C₆, ¹⁵N₄]-Arginine and [¹³C₆, ¹⁵N₄]-Lysine. Expressed in human 293 cells, it is designed to be used as an internal standard for bioanalysis of APOA2 in mass-spectrometry. SILu Prot APOA2 is a homodimer of 97 amino acids (including C-terminal polyhistidine and FLAG^® tags), with a calculated molecular mass of 11 kDa.

Supplied as a lyophilized powder containing phosphate buffered saline.

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