Human Anti-LCAT Recombinant Antibody (clone Fab1) (CAT#: PABL-631)

Figure 1 Fab1 inhibits LCAT activity on lipid-associated but not soluble substrates.

A: Increasing concentrations of mAb1 (the parent antibody of Fab1) inhibit the full LCAT reaction and prevent the formation of CEs on ApoA-I-containing proteoliposome particles. Activity shown is per 0.05 μg of LCAT enzyme. Similar inhibition was seen with Fab1 (data not shown). B: LCAT and LCAT/Fab1 complex have similar phospholipase activity on soluble substrates.

Piper, D. E., Romanow, W. G., Gunawardane, R. N., Fordstrom, P., Masterman, S., Pan, O., ... & Wang, Z. (2015). The high-resolution crystal structure of human LCAT. Journal of lipid research, 56(9), 1711-1719.

Figure 2 Crystal structure of LCAT.

A: The overall structure of the LCAT/Fab1 complex. LCAT is shown in a rainbow multicolor depiction from the N to C terminus (blue to red). Fab1 (gray) binds to subdomain 1 at the N-terminal region of LCAT. B: Diagram of LCAT showing the secondary structure and chain trace of the protein. Secondary structure elements within the α/β hydrolase domain are numbered in canonical form. Secondary structure elements outside of the α/β hydrolase domain are labeled sequentially. The α/β hydrolase domain is colored blue, subdomain 1 is colored violet, and subdomain 2 is colored green. C: Structure of LCAT only with Fab1 removed for clarity. Regions of LCAT are colored as in B. The catalytic triad residues, N-linked carbohydrate sites, and disulfide bonds of LCAT are highlighted in stick representation. D: 2Fo-Fc electron density contoured at 1 σ focusing on the catalytic triad and β sheet of the α/β hydrolase core. Amino acids of the catalytic triad are labeled. Strong electron density for the Zn ion is present next to His377.

Piper, D. E., Romanow, W. G., Gunawardane, R. N., Fordstrom, P., Masterman, S., Pan, O., ... & Wang, Z. (2015). The high-resolution crystal structure of human LCAT. Journal of lipid research, 56(9), 1711-1719.