Human Anti-CD18 Recombinant Antibody (clone H52) (CAT#: PABZ-019)

Figure 1 Flow cytometry analysis of COS‐7 transfected with LFA‐1 integrin subunits.

The expression profiles of the epitopes of YFC118, H52, KIM185 and MHM24 are shown in bold. The background profiles for the rat mAb YFC118 expression were obtained with the rat mAb YTS191, and those for mouse mAbs, i.e. H52, KIM185, and MHM24, were obtained with OX33. All first antibody staining was done in RPMI‐1640 supplemented with 5% fetal calf serum and 10 mM HEPES, pH 7.5. The positive gates, shown as horizontal lines, were set to include the brightest 5% of the cells in the background profiles. % positive cells, obtained with the specific mAbs in the gated region, and their mean fluorescence intensity (MFI), are indicated above the bar, and an expression index, defined as the product of (% positive cells)×(MFI of the positive population), is shown below the bar.

Douglass, W. A., Hyland, R. H., Buckley, C. D., Al-Shamkhani, A., Shaw, J. M., Scarth, S. L., ... & Law, S. A. (1998). The role of the cysteine‐rich region of the β2 integrin subunit in the leukocyte function‐associated antigen‐1 (LFA‐1, αLβ2, CD11a/CD18) heterodimer formation and ligand binding. FEBS letters, 440(3), 414-418.

Figure 2 Effect of different concentrations of antibodies recognizing CD15 (circles), CEA (boxes) or CD18 (triangles) on adhesion of neutrophils to plastic microtitre-plate wells

Stocks, S. C., & Kerr, M. A. (1992). Stimulation of neutrophil adhesion by antibodies recognizing CD15 (Lex) and CD15-expressing carcinoembryonic antigen-related glycoprotein NCA-160. Biochemical Journal, 288(1), 23-27.

Figure 3 In vitro platelet binding and phagocytosis and confocal microscopy.

(A) Plot of fluorescence representing percent human platelets bound and phagocytosed by domestic and α1,3-galactosyltransferase knockout/ human decay accelerating factor transgenic (GTKO/hDAF) porcine Kupffer cells (KC) at various time points shown with ±1 SD bars. Domestic and GTKO/hDAF KC phagocytosis of human platelets was statistically significant compared with phagocytosis of autologous domestic platelets (n=2–5, P<0.05) and GTKO/hDAF platelets (n=2–5, P<0.05). (B) Confocal micrographs of domestic and GTKO/hDAF KC binding and phagocytosing human platelets with staining for CD11b. (C) Confocal micrograph of domestic and GTKO/hDAF KC binding and phagocytosing human platelets with staining for CD18. Outer membrane of cells was defined with a dashed white line. Images are representative of three biological replicates.

Chihara, R. K., Paris, L. L., Reyes, L. M., Sidner, R. A., Estrada, J. L., Downey, S. M., ... & Burlak, C. (2011). Primary porcine Kupffer cell phagocytosis of human platelets involves the CD18 receptor. Transplantation, 92(7), 739-744.

Figure 4 Inhibition of human platelet phagocytosis by domestic and α1,3-galactosyltransferase knockout/human decay accelerating factor transgenic (GTKO/hDAF) porcine Kupffer cells (KC) by asialofetuin and anti-CD18 blocking antibody.

(A) Graphical representation of inhibition of human platelet phagocytosis by fetuin and asialofetuin treatments normalized to a nontreated control. Error bars represent ±1 SD plotted against 5, 10, and 20 mg/mL concentrations were statistically significant for both domestic (n=3, P<0.05) and GTKO/hDAF (n=3, P<0.05) compared with no treatment and fetuin-treated KC. (B) Anti-CD18 blocking of human platelet phagocytosis normalized to an isotype control with ±1 SD. *Indicates statistical significance compared with no treatment (n=3, P<0.05). **Statistical significance compared with all other values (n=3, P<0.05).

Chihara, R. K., Paris, L. L., Reyes, L. M., Sidner, R. A., Estrada, J. L., Downey, S. M., ... & Burlak, C. (2011). Primary porcine Kupffer cell phagocytosis of human platelets involves the CD18 receptor. Transplantation, 92(7), 739-744.