Human CXCL11/I-TAC Antibody

Chemotaxis Induced by CXCL11/I‑TAC and Neutralization by Human CXCL11/I‑TAC Antibody. Recombinant Human CXCL11/I-TAC (Catalog # 672-IT) chemoattracts the BaF3 mouse pro-B cell line transfected with human CXCR3 in a dose-dependent manner (orange line). The amount of cells that migrated through to the lower chemotaxis chamber was measured by Resazurin (Catalog # AR002). Chemotaxis elicited by Recombinant Human CXCL11/I-TAC (0.05 µg/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human CXCL11/I-TAC Antigen Affinity-purified Polyclonal Antibody (Catalog # AF260). The ND₅₀ is typically 0.5-1.5 µg/mL.

Detection of Human CXCL11/I-TAC by Block/Neutralize CXCR7-mediated Rb degradation requires ligand.pLEC cultures were infected with Trans only or Trans+CXCR7. At 6 hours post-infection, media was replaced with media only or media containing (A) SDF-1/CXCL12 neutralizing antibody at 1.5, or 3.0 µg/ml or (B) ITAC/CXCL11 neutralizing antibody at 0.5 or 1.0 µg/ml. At 20 hours post infection, cells were lysed and analyzed by western blot for total Rb levels. Densitometry analysis was performed and fold change values were calculated from GAPDH-normalized optical density ratios as described for Figure 3. Bar graphs (bottom) represent the average fold change at each condition for two independent experiments. Image collected and cropped by CiteAb from the following open publication (https://dx.plos.org/10.1371/journal.pone.0069828), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of Human CXCL11/I-TAC by Block/Neutralize CXCR7-mediated Rb degradation requires ligand.pLEC cultures were infected with Trans only or Trans+CXCR7. At 6 hours post-infection, media was replaced with media only or media containing (A) SDF-1/CXCL12 neutralizing antibody at 1.5, or 3.0 µg/ml or (B) ITAC/CXCL11 neutralizing antibody at 0.5 or 1.0 µg/ml. At 20 hours post infection, cells were lysed and analyzed by western blot for total Rb levels. Densitometry analysis was performed and fold change values were calculated from GAPDH-normalized optical density ratios as described for Figure 3. Bar graphs (bottom) represent the average fold change at each condition for two independent experiments. Image collected and cropped by CiteAb from the following open publication (https://dx.plos.org/10.1371/journal.pone.0069828), licensed under a CC-BY license. Not internally tested by R&D Systems.