The apparent half-maximal binding to cell surface ROBO1 was estimated to be approximately 32.5 ng/mL from the fitted curve in ELISA (Figure 1c).
Biotinylation and immunofluorescence microscopy demonstrated rapid and prolonged relocation of TPβ from the ER to the cell surface, maximal within 1 hour and persisting for 8 hours.
We showed that, with the exception of breast and lung, primary tumors show cell surface maximal similarity with the cell lines of same tissue origin (t-test p-value<0.01).
Anti-ROBO1 exhibited high half-maximal binding (32.5 ng/mL) to cell surface ROBO1 on ROBO1-expressing CHO cells.
Observations suggest that the propeptide is a key functional domain of ADAMTS9, mediating an unusual regulatory mechanism that may have evolved to ensure maximal activity of this protease at the cell surface.
Treatment with resistin for 1, 2, 4 and 8 h induced rapid increases (within 1 h) in the ICAM-1 and VCAM-1 mRNA expressions and cell surface protein expressions, which reached a maximal level compared to the untreated control within 4 h, and then declined but remained elevated after 8 h of treatment.
As shown in Fig. 5C, for pro-B cells, CXCL12 treatment induced internalization of 35 40% of cell surface WT CXCR4 within 5 min, and maximal internalization of 50% was achieved at 60 min. On the contrary, CXCL12 binding to ΔT did not trigger endocytosis at all.
As recombinant expression results in robust constitutive expression, recovery could be maximal due to ongoing receptor synthesis and transport to the cell surface.
As shown (Fig. 2 F ), GnRH II caused a rapid reduction in cell surface expression of XGnRHRs (significant reduction at 10 min, maximal effect at 120 min).
In both F9 and F9-Dab2 ceLRP6 LRP6 is rapidly internalized following Wnt3A treatment, with maximal internalization observed at 1 2 h, followed by its reappearance on the cell surface at 4 h.
