Phospho-Annexin A2 (Tyr24) Antibody - #AF7096

igure 1. Anxa2 regulated the expression of VEGFs. HepG2 cells were treated with three different Anxa2-shRNAs. (A) Protein level and phosphorylation status of STAT3 and Anxa2 were determined by immuno-blotting. (B) The activation of STAT3 was determined via reporter gene assay. (C) The expression of STAT3 target genes was determined by qRT-PCR. (D) The protein level of four VEGFs was determined by immuno-blotting. (E) The concentration of four VEGFs in cell-free supernatant was determined by ELISA. All experiments were performed with triple replicant.

FIGURE 4 NASP promotes ANXA2-mediated DNA repair. (A) The top 15 proteins potentially associated with NASP were isolated by immunoprecipitation and identified by mass spectrometry in NASP-overexpressing U87 cells. Cell lysates were immunoprecipitated with an antibody against NASP, while an antibody against IgG was used as the negative control. (B) Mass spectrogram of ANXA2. (C, D) Western blot detection of NASP and ANXA2 proteins by reciprocal immunoprecipitation with an antibody against NASP (C) or ANXA2 (D) in U87 and U251 cells. IgG was used as the control. (E) Immunofluorescence detection of NASP, ANXA2, and p-ANXA2 localization in control and NASP-overexpressing U87 cells. Scale bars, 50 μM. (F) Abundance of NASP, ANXA2, and p-ANXA2 in cytoplasmic, nuclear, and total protein fractions from the control and NASP-overexpressing U87 cells estimated by western blotting. (G) Effects of NASP upregulation and ANXA2 downregulation on DNA double-strand breaks in U87 cells after radiotherapy as detected by immunofluorescence. Scale bars, 50 μM. (H) Comet assay showing the effect of NASP upregulation and ANXA2 downregulation on DNA double-strand breaks in U87 cells after RT. Scale bars, 100 μM. Data are presented as mean ± SD from at least three independent experiments. *p 

FIGURE 4 NASP promotes ANXA2-mediated DNA repair. (A) The top 15 proteins potentially associated with NASP were isolated by immunoprecipitation and identified by mass spectrometry in NASP-overexpressing U87 cells. Cell lysates were immunoprecipitated with an antibody against NASP, while an antibody against IgG was used as the negative control. (B) Mass spectrogram of ANXA2. (C, D) Western blot detection of NASP and ANXA2 proteins by reciprocal immunoprecipitation with an antibody against NASP (C) or ANXA2 (D) in U87 and U251 cells. IgG was used as the control. (E) Immunofluorescence detection of NASP, ANXA2, and p-ANXA2 localization in control and NASP-overexpressing U87 cells. Scale bars, 50 μM. (F) Abundance of NASP, ANXA2, and p-ANXA2 in cytoplasmic, nuclear, and total protein fractions from the control and NASP-overexpressing U87 cells estimated by western blotting. (G) Effects of NASP upregulation and ANXA2 downregulation on DNA double-strand breaks in U87 cells after radiotherapy as detected by immunofluorescence. Scale bars, 50 μM. (H) Comet assay showing the effect of NASP upregulation and ANXA2 downregulation on DNA double-strand breaks in U87 cells after RT. Scale bars, 100 μM. Data are presented as mean ± SD from at least three independent experiments. *p 

FIGURE 4 GNAQ T96S peptide inhibitor induces apoptosis by competing with annexin A2 (ANXA2) binding to GNAQ T96S in natural killer cells. (A) A schematic diagram showing the different domains of GNAQ. (B) Identification of the interaction between different domains of GNAQ and ANXA2 by co‐immunoprecipitation (IP). M or R refers to the host of antibody. (C) GNAQ T96S peptide blocks the binding of GNAQ to ANXA2 in a dose‐dependent manner. (D) GNAQ T96S peptide significantly induces apoptosis in NK cells. (E) GNAQ peptide affects several signaling pathways, including the AKT, ERK, and ANXA2 signaling pathways. The experiment was independently repeated three times

Figure 6 I194496 inhibits the Anxa2/STAT3 and VEGF/FAK/Paxillin signalling pathways in human TNBC cells. (A, B) The effect of I194496 on Anxa2/STAT3 pathway in MDA-MB-231 cells. *P