Fig 1: (A) Quantitative analysis results and representative images of the Western blot results for MMP2 and MMP9 in ALT1 knockdown HepG2 cells. (B) Quantitative analysis results and representative images of the Western blot results for MMP2 and MMP9 in EP-CAM knockdown HepG2 cells. (C) RT-qPCR analyses showed the knockdown of ALT1 in HepG2 cells significantly decreased expression of N-cadherin, Snail, and Twist while increasing E-cadherin expression. (D) RT-qPCR analyses showed the knockdown of EP-CAM in HepG2 cells significantly decreased expression of N-cadherin, Snail, and Twist while increasing E-cadherin expression.
Fig 2: Knockdown of HHLA2 inhibited NSCLC cell migration, invasion via modulating the EMT‐related proteins. (A, B) HHLA2 knockdown decreased wound healing rates of A549 and H1299 cells. Scale bar: 200 μm. (C) Modified Boyden chamber assay revealed that HHLA2 deficiency inhibited the migration and invasion of A549 and H1299 cells. Scale bar: 200 μm. (D) Immunofluorescent analysis indicated that the expression of ZO‐1 was upregulated in HHLA2‐deficient A549 and H1299 cells. Scale bar: 100 μm. (E) Immunoblotting was performed to evaluate the protein levels of E‐Cadherin, N‐Cadherin, Vimentin, MMP2, and MMP9 expression after HHLA2 knockdown. (F) Knockdown of HHLA2 inhibited the activity of EGFR/MAPK/ERK signaling pathway in A549 and H1299 cells. *p < 0.05, **p < 0.01, ***p < 0.001
Fig 3: Effects of different Myr concentrations on expression of proliferation-, migration-, and invasion-related proteins in SKOV3 cells. (A) Western blot analysis image. Relative levels of (B) p-p38, (C) SAPLA, (D) EGFR, (E) MMP2, (F) MMP3, (G) MMP9, (H) Bax/Bcl-2, (I) cleaved caspase-3, and (J) caspase-9, were determined using western blot analysis. n=3; *p<0.05, **p<0.01 vs. control.
Fig 4: The MBOP/MEK1/pERK/MMP2/MMP9 axis in CRC. (A) MBOP substantially promoted the pERK1/2 in HCT116 and HCT15, but the total ERK expression did not show significant differences. (B) Overexpressing MBOP in HCT116 and HCT15 paved the axis of MBOP/MEK1/pERK/MMP2/MMP9. (C) The signaling pathway axis in animal assay met the expression tendency of in vitro assays (n = 4). (D) HCT116 and HCT15 were treated with the MEK1/2 inhibitor U0126-EtOH for 48 h, and the protein expression of MEK1/2, pERK1/2, and downstream MMP2 and MMP9 all decreased violently. (E) HCT116 cells were transfected with plasmids pcDNA3.1+, pORF-FLAG, and pORFmut-FLAG, followed by treatments of DMSO and U0126-EtOH. The overexpression of MEK1 and MBOP brought by transfecting cells with pORF-FLAG could be partially inhibited by U0126-EtOH, whereas the MAP2K1 showed no significant alterations. Data are presented as mean ± SD, **** p < 0.0001. ns: not significant. (F) The pro-migration effect driven by the transfection of pORF-FLAG could be partially reversed by U0126-EtOH.
Fig 5: Conformation of ligand and receptor binding. The binding conformation and interaction force between FTA and MMP-2 (a), TLR4 (b), MYD88 (c), and NFKB1 (d).
Supplier Page from ABclonal Technology for MMP2 Rabbit mAb