Figure 1 | Scientific Reports

Figure 1

From: Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma

Figure 1

rGal3C is able to bind immobilized lactose and HepG2. (A) The 22.86 kDa band of rGal3C was detected. (B) Molecular weight of rGal3C detected by MALDI-TOF MS is 22862.71, which is consistent with its theoretical molecular weight. (C) Biotinylation of rGal3C was detected. (D) Binding of rGal3C to immobilize lactose was identified. Input fraction, washing fractions (band 1–4), eluting fractions (band 5–8) and NaOH eluting fraction (band 9) were detected. (E) Binding of rGal3C to cell surface of HepG2 was identified. Red fluorescence of Alexa 594 dye displayed total distribution of both Galectin-3 and rGal3C, while green fluorescence of FITC displayed only rGal3C binding to HepG2. (F) Galactose disrupted binding of rGal3C or Galectin-3 to HepG2. Cells washed with galactose displays a decreased Galectin-3 band, while mannose washing has no effect. HepG2 treated by rGal3C displays an rGal3C band which could be attenuated by galactose washing, but not mannose. Con, untreated HepG2 cells.

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