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Proteintech igf2bp1
Igf2bp1, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 129 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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CircNF1 interacts with <t>IGF2BP1</t> to promote tumor metastasis. (A) Venn diagram depicting potential RBPs. (B) Identification of interacting proteins via pull-down assays. Arrows indicate the additional band presented in the circNF1-protein complex. (C) RIP assays demonstrate the interaction of IGF2BP1 with circNF1. (D) The relative levels of IGF2BP1 mRNA and protein were quantified in GC cells after transfection with si-circNF1 and circNF1 overexpression plasmids. (E) IF-FISH assay demonstrates that circNF1 was colocalized with IGF2BP1 protein in the cytoplasm. (F, G) The relative mRNA and protein expression levels of IGF2BP1 were determined after transfection with si-IGF2BP1 and IGF2BP1 overexpression plasmids. (H) Transwell migration assay for circNF1 overexpressing GC cells with or without IGF2BP1 knockdown. (I, J) QRT-PCR and Western blot assays of relative markers. si-NC/nc, small interfering RNA negative control; vector/ev, empty vector control. Data are shown as mean ± SD, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.
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PBs act as PANoptosis inhibitors by targeting RIPK1, ZBP1, and AIM2 to suppress multiple PANoptosomes, effectively blocking crosstalk among pyroptosis, apoptosis, and necroptosis in PANoptosis-driven diseases. In addition, PB regulates mitochondrial metabolism and immune-inflammatory homeostasis, further disrupting multimodal cell death crosstalk. Some elements in the image were sourced from BioRender (Created in BioRender. xu, L. (2026) https://BioRender.com/9kka4p3 ).

Journal: Nature Communications

Article Title: Prussian blue nanoparticles targeting multiple PANoptosome-mediated PANoptosis for myocardial ischemia-reperfusion injury therapy

doi: 10.1038/s41467-026-70012-2

Figure Lengend Snippet: PBs act as PANoptosis inhibitors by targeting RIPK1, ZBP1, and AIM2 to suppress multiple PANoptosomes, effectively blocking crosstalk among pyroptosis, apoptosis, and necroptosis in PANoptosis-driven diseases. In addition, PB regulates mitochondrial metabolism and immune-inflammatory homeostasis, further disrupting multimodal cell death crosstalk. Some elements in the image were sourced from BioRender (Created in BioRender. xu, L. (2026) https://BioRender.com/9kka4p3 ).

Article Snippet: Necrostatin-1 (HY-15760), Disulfiram (HY-B0240), Z-VAD-FMK (HY-16658B), ZBP1 (HY- P83326 ), phospho-RIPK1 (HY- P81539 ), phospho-MLKL (HY- P80468 ), cleaved caspase 1 (HY- P80622 ), cell counting kit-8 (CCK-8) assay kit (HY-K030), and cleaved caspase 8 (HY- P80624 ) were obtained from MedChemExpress, USA.

Techniques: Blocking Assay

A Schematic of ischemic zone (IZ), remote zone (RZ), and border zone (BZ) in human acute myocardial infarction. The heart element in the image was sourced from BioRender (Created in BioRender. xu, L. (2026) https://BioRender.com/9kka4p3 ). B UMAP visualization of cell distribution (left) and annotated cell types (right) in the control ( n = 4) versus IZ ( n = 11) groups. C Cardiomyocyte subpopulation quantification (left) and UMAP-based clustering (right) in the control and IZ groups. D , E UMAP projection ( D ) and box plots ( E ) showing PANoptosis activation across cardiac cell types. (The exact n in E = [left to right] 20, 84 cells; 17326, 3506 cells; 6231, 6969 cells; 9468, 12187 cells; 3386, 7142 cells; 3039, 2286 cells; 583, 254 cells; 531, 1138 cells). The minima, maxima, mean, median, bounds, whiskers, and percentile information were provided in the Source Data file. Exact P- values from left to right: 2.39E-265, 1.55E-300, 1.05E-35, 4.09E-05, 2.21E-06, 0.0002, 1.9E-11. F Violin plots comparing PANoptosis-related gene expression ( AIM2, ZBP1, RIPK1, Pyrin, NLRP12, NLRP3, MLKL, GSDMD, RIPK3, caspase 3, caspase 1 , and caspase 8 ) in total cells. ( n = 40706 cells [control], 33688 cells [IZ]). The minima, maxima, mean, median, bounds, whiskers, and percentile information were provided in the Source Data file. Exact P- values from left to right ( AIM2 to caspase 8 ): 0.2752, 0.0002, 0, 0.0854, 6.67E-09, 7.19E-82, 3.59E-37, 0.0709, 0.0269, 2.29E-280, 2.45E-30, 4.07E-09. G, H Cardiomyocyte-specific UMAP ( G ) and quantitative PANoptosis levels ( H ) of the control and IZ groups. (The exact n in H = [left to right] 6904 cells, 0; 5281 cells, 0; 1191, 3346 cells; 3192, 80 cells; 758, 80 cells). The minima, maxima, mean, median, bounds, whiskers, and percentile information were provided in the Source Data file. Exact P- values from left to right: 4.01E-05, 0.0021. I Proportional representation of cardiomyocyte subpopulations. J , K Heatmap depicting activation patterns of apoptosis/PANoptosis/pyroptosis/necroptosis ( J ) and PANoptosis-related genes ( K ) across cardiomyocyte subtypes. Significance: wilcox.test, a two-sided test; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns : no significant difference ( P > 0.05). Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Prussian blue nanoparticles targeting multiple PANoptosome-mediated PANoptosis for myocardial ischemia-reperfusion injury therapy

doi: 10.1038/s41467-026-70012-2

Figure Lengend Snippet: A Schematic of ischemic zone (IZ), remote zone (RZ), and border zone (BZ) in human acute myocardial infarction. The heart element in the image was sourced from BioRender (Created in BioRender. xu, L. (2026) https://BioRender.com/9kka4p3 ). B UMAP visualization of cell distribution (left) and annotated cell types (right) in the control ( n = 4) versus IZ ( n = 11) groups. C Cardiomyocyte subpopulation quantification (left) and UMAP-based clustering (right) in the control and IZ groups. D , E UMAP projection ( D ) and box plots ( E ) showing PANoptosis activation across cardiac cell types. (The exact n in E = [left to right] 20, 84 cells; 17326, 3506 cells; 6231, 6969 cells; 9468, 12187 cells; 3386, 7142 cells; 3039, 2286 cells; 583, 254 cells; 531, 1138 cells). The minima, maxima, mean, median, bounds, whiskers, and percentile information were provided in the Source Data file. Exact P- values from left to right: 2.39E-265, 1.55E-300, 1.05E-35, 4.09E-05, 2.21E-06, 0.0002, 1.9E-11. F Violin plots comparing PANoptosis-related gene expression ( AIM2, ZBP1, RIPK1, Pyrin, NLRP12, NLRP3, MLKL, GSDMD, RIPK3, caspase 3, caspase 1 , and caspase 8 ) in total cells. ( n = 40706 cells [control], 33688 cells [IZ]). The minima, maxima, mean, median, bounds, whiskers, and percentile information were provided in the Source Data file. Exact P- values from left to right ( AIM2 to caspase 8 ): 0.2752, 0.0002, 0, 0.0854, 6.67E-09, 7.19E-82, 3.59E-37, 0.0709, 0.0269, 2.29E-280, 2.45E-30, 4.07E-09. G, H Cardiomyocyte-specific UMAP ( G ) and quantitative PANoptosis levels ( H ) of the control and IZ groups. (The exact n in H = [left to right] 6904 cells, 0; 5281 cells, 0; 1191, 3346 cells; 3192, 80 cells; 758, 80 cells). The minima, maxima, mean, median, bounds, whiskers, and percentile information were provided in the Source Data file. Exact P- values from left to right: 4.01E-05, 0.0021. I Proportional representation of cardiomyocyte subpopulations. J , K Heatmap depicting activation patterns of apoptosis/PANoptosis/pyroptosis/necroptosis ( J ) and PANoptosis-related genes ( K ) across cardiomyocyte subtypes. Significance: wilcox.test, a two-sided test; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns : no significant difference ( P > 0.05). Source data are provided as a Source Data file.

Article Snippet: Necrostatin-1 (HY-15760), Disulfiram (HY-B0240), Z-VAD-FMK (HY-16658B), ZBP1 (HY- P83326 ), phospho-RIPK1 (HY- P81539 ), phospho-MLKL (HY- P80468 ), cleaved caspase 1 (HY- P80622 ), cell counting kit-8 (CCK-8) assay kit (HY-K030), and cleaved caspase 8 (HY- P80624 ) were obtained from MedChemExpress, USA.

Techniques: Control, Activation Assay, Gene Expression

A Initial and final snapshots (200 ns) of the PB-AIM2 HIN simulation system. Interaction interfaces are highlighted (blue/yellow boxes). B , C The residue contact detail of two chains of AIM2 HIN with PB is highlighted on the left snapshots. D , E The interaction energy analysis of these contact residues of AIM2 HIN with PB ( n = 10, taken from the final 10 ns interaction energy of the simulated system). F The interaction energy between PB and proteins in PB-AIM2 HIN changes with time. G–L The conformation images of the PB-ZBP1 ( G ) and PB-RIPK1 ( J ) systems at the end of the simulation ( t = 200 ns) and the residue contact details. The interaction energy analysis of the contact residues of ZBP1 ( H ) and RIPK1 ( K ) with PB ( n = 10, taken from the final 10 ns interaction energy of the simulated system). The interaction energy between PB and proteins in PB-ZBP1 ( I ) and PB-RIPK1 ( L ) changes with time. Data: mean ± SD. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Prussian blue nanoparticles targeting multiple PANoptosome-mediated PANoptosis for myocardial ischemia-reperfusion injury therapy

doi: 10.1038/s41467-026-70012-2

Figure Lengend Snippet: A Initial and final snapshots (200 ns) of the PB-AIM2 HIN simulation system. Interaction interfaces are highlighted (blue/yellow boxes). B , C The residue contact detail of two chains of AIM2 HIN with PB is highlighted on the left snapshots. D , E The interaction energy analysis of these contact residues of AIM2 HIN with PB ( n = 10, taken from the final 10 ns interaction energy of the simulated system). F The interaction energy between PB and proteins in PB-AIM2 HIN changes with time. G–L The conformation images of the PB-ZBP1 ( G ) and PB-RIPK1 ( J ) systems at the end of the simulation ( t = 200 ns) and the residue contact details. The interaction energy analysis of the contact residues of ZBP1 ( H ) and RIPK1 ( K ) with PB ( n = 10, taken from the final 10 ns interaction energy of the simulated system). The interaction energy between PB and proteins in PB-ZBP1 ( I ) and PB-RIPK1 ( L ) changes with time. Data: mean ± SD. Source data are provided as a Source Data file.

Article Snippet: Necrostatin-1 (HY-15760), Disulfiram (HY-B0240), Z-VAD-FMK (HY-16658B), ZBP1 (HY- P83326 ), phospho-RIPK1 (HY- P81539 ), phospho-MLKL (HY- P80468 ), cleaved caspase 1 (HY- P80622 ), cell counting kit-8 (CCK-8) assay kit (HY-K030), and cleaved caspase 8 (HY- P80624 ) were obtained from MedChemExpress, USA.

Techniques: Residue

A PCA of RNA-seq data (Sham: orange; MIRI: green; PB@PM: blue; n = 5 biologically independent replicates). B Volcano plot of differentially expressed genes (DEGs; PB@PM vs. MIRI: red/blue = up/downregulated). The Wald test of DESeq2 (DESeq(dds) default test = “Wald”) was used, which is a two-sided test. Multiple comparisons correction: the FDR (False Discovery Rate) correction of the BH (Benjamini-Hochberg) method was computed to obtain P adjustment ( P .adj.). C Venn diagram of shared DEGs between Sham-MIRI and PB@PM-MIRI comparisons. D GSVA of pathway enrichment across groups. E KEGG pathway enrichment of downregulated genes in PB@PM vs. MIRI. A one-sided hypergeometric test was used. Multiple comparisons correction: the FDR correction for the BH method was calculated to obtain P .adj. F , G GSEA networks ( F ) and protein interaction networks ( G ) for pyroptosis, apoptosis, and necroptosis. H GSEA plots showing marked downward trends of pyroptosis, apoptosis, and necroptosis in the PB@PM group compared to the MIRI group. A permutation test was used, based on weighted Kolmogorov-Smirnov-like statistics. It is a two-sided test (tests whether the enrichment scores are significantly deviated from zero, which can be positive or negative, corresponding to up- or down-regulated enrichment, respectively). Multiple comparisons correction: The FDR correction for the BH method was calculated to obtain P .adj. I Pearson correlation between pyroptosis, apoptosis, and necroptosis in the Sham (C), MIRI (I), and PB@PM (T) groups. Using psych R package, method = “spearman” function, t-test, two-sided test, and no correction for multiple comparisons. J Western blot of PANoptosis-related proteins (AIM2, ZBP1, Pyrin, ASC, FADD, Bax, Bcl-2, phosphorylated/total RIPK1/RIPK3/MLKL, cleaved/total caspase-1/3/8 and GSDMD) in ischemic myocardium (day 3; n = 5 biologically independent replicates). Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Prussian blue nanoparticles targeting multiple PANoptosome-mediated PANoptosis for myocardial ischemia-reperfusion injury therapy

doi: 10.1038/s41467-026-70012-2

Figure Lengend Snippet: A PCA of RNA-seq data (Sham: orange; MIRI: green; PB@PM: blue; n = 5 biologically independent replicates). B Volcano plot of differentially expressed genes (DEGs; PB@PM vs. MIRI: red/blue = up/downregulated). The Wald test of DESeq2 (DESeq(dds) default test = “Wald”) was used, which is a two-sided test. Multiple comparisons correction: the FDR (False Discovery Rate) correction of the BH (Benjamini-Hochberg) method was computed to obtain P adjustment ( P .adj.). C Venn diagram of shared DEGs between Sham-MIRI and PB@PM-MIRI comparisons. D GSVA of pathway enrichment across groups. E KEGG pathway enrichment of downregulated genes in PB@PM vs. MIRI. A one-sided hypergeometric test was used. Multiple comparisons correction: the FDR correction for the BH method was calculated to obtain P .adj. F , G GSEA networks ( F ) and protein interaction networks ( G ) for pyroptosis, apoptosis, and necroptosis. H GSEA plots showing marked downward trends of pyroptosis, apoptosis, and necroptosis in the PB@PM group compared to the MIRI group. A permutation test was used, based on weighted Kolmogorov-Smirnov-like statistics. It is a two-sided test (tests whether the enrichment scores are significantly deviated from zero, which can be positive or negative, corresponding to up- or down-regulated enrichment, respectively). Multiple comparisons correction: The FDR correction for the BH method was calculated to obtain P .adj. I Pearson correlation between pyroptosis, apoptosis, and necroptosis in the Sham (C), MIRI (I), and PB@PM (T) groups. Using psych R package, method = “spearman” function, t-test, two-sided test, and no correction for multiple comparisons. J Western blot of PANoptosis-related proteins (AIM2, ZBP1, Pyrin, ASC, FADD, Bax, Bcl-2, phosphorylated/total RIPK1/RIPK3/MLKL, cleaved/total caspase-1/3/8 and GSDMD) in ischemic myocardium (day 3; n = 5 biologically independent replicates). Source data are provided as a Source Data file.

Article Snippet: Necrostatin-1 (HY-15760), Disulfiram (HY-B0240), Z-VAD-FMK (HY-16658B), ZBP1 (HY- P83326 ), phospho-RIPK1 (HY- P81539 ), phospho-MLKL (HY- P80468 ), cleaved caspase 1 (HY- P80622 ), cell counting kit-8 (CCK-8) assay kit (HY-K030), and cleaved caspase 8 (HY- P80624 ) were obtained from MedChemExpress, USA.

Techniques: RNA Sequencing, Western Blot

CircNF1 interacts with IGF2BP1 to promote tumor metastasis. (A) Venn diagram depicting potential RBPs. (B) Identification of interacting proteins via pull-down assays. Arrows indicate the additional band presented in the circNF1-protein complex. (C) RIP assays demonstrate the interaction of IGF2BP1 with circNF1. (D) The relative levels of IGF2BP1 mRNA and protein were quantified in GC cells after transfection with si-circNF1 and circNF1 overexpression plasmids. (E) IF-FISH assay demonstrates that circNF1 was colocalized with IGF2BP1 protein in the cytoplasm. (F, G) The relative mRNA and protein expression levels of IGF2BP1 were determined after transfection with si-IGF2BP1 and IGF2BP1 overexpression plasmids. (H) Transwell migration assay for circNF1 overexpressing GC cells with or without IGF2BP1 knockdown. (I, J) QRT-PCR and Western blot assays of relative markers. si-NC/nc, small interfering RNA negative control; vector/ev, empty vector control. Data are shown as mean ± SD, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: CircNF1 promotes gastric cancer metastasis by stabilizing HMGA2 mRNA through IGF2BP1 interaction

doi: 10.3389/fimmu.2026.1767319

Figure Lengend Snippet: CircNF1 interacts with IGF2BP1 to promote tumor metastasis. (A) Venn diagram depicting potential RBPs. (B) Identification of interacting proteins via pull-down assays. Arrows indicate the additional band presented in the circNF1-protein complex. (C) RIP assays demonstrate the interaction of IGF2BP1 with circNF1. (D) The relative levels of IGF2BP1 mRNA and protein were quantified in GC cells after transfection with si-circNF1 and circNF1 overexpression plasmids. (E) IF-FISH assay demonstrates that circNF1 was colocalized with IGF2BP1 protein in the cytoplasm. (F, G) The relative mRNA and protein expression levels of IGF2BP1 were determined after transfection with si-IGF2BP1 and IGF2BP1 overexpression plasmids. (H) Transwell migration assay for circNF1 overexpressing GC cells with or without IGF2BP1 knockdown. (I, J) QRT-PCR and Western blot assays of relative markers. si-NC/nc, small interfering RNA negative control; vector/ev, empty vector control. Data are shown as mean ± SD, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Article Snippet: SiRNAs targeting IGF2BP1 (si-IGF2BP1#1 and si-IGF2BP1#2) and HMGA2 (si-HMGA2) were synthesized by Sangon Biotech (Shanghai, China).

Techniques: Transfection, Over Expression, Expressing, Transwell Migration Assay, Knockdown, Quantitative RT-PCR, Western Blot, Small Interfering RNA, Negative Control, Plasmid Preparation, Control

The crucial role of circNF1 and IGF2BP1 in maintaining HMGA2 mRNA stability. (A) RIP assay showing the connection between IGF2BP1 and HMGA2. (B) Measurement of the half-life of HMGA2 mRNA in GC cells treated with ActD for the indicated times. (C, D) Relative expression of HMGA2 was measured by qRT-PCR and Western blot assays in GC cells transfected with si-circNF1 and circNF1 overexpression plasmid. (E, F) Relative expression of HMGA2 was measured by qRT-PCR and Western blot assays in GC cells transfected with si-IGF2BP1 and IGF2BP1 overexpression plasmid. si-NC/nc, small interfering RNA negative control; vector/ev, empty vector control. Data are shown as mean ± SD, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: CircNF1 promotes gastric cancer metastasis by stabilizing HMGA2 mRNA through IGF2BP1 interaction

doi: 10.3389/fimmu.2026.1767319

Figure Lengend Snippet: The crucial role of circNF1 and IGF2BP1 in maintaining HMGA2 mRNA stability. (A) RIP assay showing the connection between IGF2BP1 and HMGA2. (B) Measurement of the half-life of HMGA2 mRNA in GC cells treated with ActD for the indicated times. (C, D) Relative expression of HMGA2 was measured by qRT-PCR and Western blot assays in GC cells transfected with si-circNF1 and circNF1 overexpression plasmid. (E, F) Relative expression of HMGA2 was measured by qRT-PCR and Western blot assays in GC cells transfected with si-IGF2BP1 and IGF2BP1 overexpression plasmid. si-NC/nc, small interfering RNA negative control; vector/ev, empty vector control. Data are shown as mean ± SD, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Article Snippet: SiRNAs targeting IGF2BP1 (si-IGF2BP1#1 and si-IGF2BP1#2) and HMGA2 (si-HMGA2) were synthesized by Sangon Biotech (Shanghai, China).

Techniques: Expressing, Quantitative RT-PCR, Western Blot, Transfection, Over Expression, Plasmid Preparation, Small Interfering RNA, Negative Control, Control

CircNF1 stabilizes HMGA2 mRNA via IGF2BP1 interaction. (A) Schematic structure showing RNA-binding domains within the IGF2BP1 protein and the list of different IGF2BP1 truncation mutants. (B) RT-PCR assays for the enrichment of circNF1 or HMGA2 mRNA in AGS cells expressing flag-tagged full-length or truncated mutants of IGF2BP1. (C) Relative enrichment representing the enrichment of circNF1 and HMGA2 associated with truncated IGF2BP1 compared to an input control. (D, E) QRT-PCR and Western blot assays of HMGA2 for circNF1 overexpression in GC cells with or without IGF2BP1 knockdown. (F) Molecular docking analysis predicting the binding sites of IGF2BP1 with circNF1 and HMGA2 mRNA. Data are shown as mean ± SD, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: Frontiers in Immunology

Article Title: CircNF1 promotes gastric cancer metastasis by stabilizing HMGA2 mRNA through IGF2BP1 interaction

doi: 10.3389/fimmu.2026.1767319

Figure Lengend Snippet: CircNF1 stabilizes HMGA2 mRNA via IGF2BP1 interaction. (A) Schematic structure showing RNA-binding domains within the IGF2BP1 protein and the list of different IGF2BP1 truncation mutants. (B) RT-PCR assays for the enrichment of circNF1 or HMGA2 mRNA in AGS cells expressing flag-tagged full-length or truncated mutants of IGF2BP1. (C) Relative enrichment representing the enrichment of circNF1 and HMGA2 associated with truncated IGF2BP1 compared to an input control. (D, E) QRT-PCR and Western blot assays of HMGA2 for circNF1 overexpression in GC cells with or without IGF2BP1 knockdown. (F) Molecular docking analysis predicting the binding sites of IGF2BP1 with circNF1 and HMGA2 mRNA. Data are shown as mean ± SD, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Article Snippet: SiRNAs targeting IGF2BP1 (si-IGF2BP1#1 and si-IGF2BP1#2) and HMGA2 (si-HMGA2) were synthesized by Sangon Biotech (Shanghai, China).

Techniques: RNA Binding Assay, Reverse Transcription Polymerase Chain Reaction, Expressing, Control, Quantitative RT-PCR, Western Blot, Over Expression, Knockdown, Binding Assay

Schematic illustration of circNF1 molecular mechanism. CircNF1, regulated by ZNF460, promotes GC metastasis by binding to IGF2BP1 and stabilizing HMGA2 mRNA.

Journal: Frontiers in Immunology

Article Title: CircNF1 promotes gastric cancer metastasis by stabilizing HMGA2 mRNA through IGF2BP1 interaction

doi: 10.3389/fimmu.2026.1767319

Figure Lengend Snippet: Schematic illustration of circNF1 molecular mechanism. CircNF1, regulated by ZNF460, promotes GC metastasis by binding to IGF2BP1 and stabilizing HMGA2 mRNA.

Article Snippet: SiRNAs targeting IGF2BP1 (si-IGF2BP1#1 and si-IGF2BP1#2) and HMGA2 (si-HMGA2) were synthesized by Sangon Biotech (Shanghai, China).

Techniques: Binding Assay