heparin oligosaccharides dp8  (AMS Biotechnology)

Journal: Frontiers in Immunology

Article Title: CXCL17 binds efficaciously to glycosaminoglycans with the potential to modulate chemokine signaling

doi: 10.3389/fimmu.2023.1254697

Figure Lengend Snippet: CXCL4 and CXCL17 bind heparin and heparan sulfate with high capacities. Real-time assessment of CXCL4 and CXCL17 (24–119) binding to immobilized heparin (dp8) and HS as assessed by bio-layer interferometry (BLI). Sensorgrams illustrate the binding associations between streptavidin immobilized biotinylated heparin (A) , or HS (B) , and various equimolar concentrations of CXCL4 and CXCL17. Prepared solutions of chemokine were sampled with BLI (Octet) streptavidin-coated sensors containing bound GAG, for a 1,080-s association phase, and a 1,500-s dissociation phase. The experiment was performed in triplicate with data displayed as wavelength shift (nm) from a single representative sensorgram plot. (C–E) The extent of molecular association of CXCL4 or CXCL17 with heparin or HS at increasing concentrations of chemokine. Measurements were taken of induced wavelength shift (nm), with maximal recorded wavelength shifts for 15.6 nM (C) , 62.5 nM (D) , and 250 nM (E) of chemokine. Data are displayed as mean wavelength shift (nm) + SEM from three independent experiments, and two-way ANOVA with Sidak’s multiple comparison test was performed, and statistical significance is displayed as * p < 0.05.

Article Snippet: Heparin dp8 and heparan sulfate (HS) used in the bio-layer interferometry (BLI) assays were from Iduron (Alderley Edge, UK).

Techniques: Binding Assay, Comparison

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding

doi: 10.1073/pnas.2026650118

Figure Lengend Snippet: Context-dependent stability of LPL

Article Snippet: Measurements with the heparin derivative dp8 (from Iduron) were performed with 50 µM dp8.

Techniques:

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding

doi: 10.1073/pnas.2026650118

Figure Lengend Snippet: Context-dependent stability of LPL

Article Snippet: A defined heparin fragment, dp8 (with eight sulfated Ido2S-GlcNS6S units), was purchased from Iduron.

Techniques: