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anti gal 3bp antibody  (R&D Systems)


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    R&D Systems anti gal 3bp antibody
    Affinity matured, <t>anti-Gal-3BP</t> antibodies show superior in vitro efficacy for blocking PDAC cell migration and invasion. A . Schematic diagram of antibody affinity maturation of the humanized anti-Gal-3BP antibody. The #13 − 7 clone was used as a template. Two high-affinity clones, #34 and #132, were tested in further study. B . Affinity of the engineered #34 and #132 antibody clones measured by Octet (on left) and their value (Table on right). The affinity of parental clone #13 − 7 is shown at the bottom of the table. C – D . Validation of Gal-3BP binding of engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132), shown by immunoprecipitation in PDX_PC 110,621 ( C ) or PDAC PKCY ( D ). E – F . Migration and invasion of PDX_PC 115,026 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG (human IgG). Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 200 μm. G – H . Migration and invasion of Pan02 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG. Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 50 μm.* p < 0.05; ** p < 0.01; *** p < 0.001; ns (not significant)
    Anti Gal 3bp Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gal 3bp antibody/product/R&D Systems
    Average 93 stars, based on 21 article reviews
    anti gal 3bp antibody - by Bioz Stars, 2026-06
    93/100 stars

    Images

    1) Product Images from "The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3"

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    Journal: Cell Communication and Signaling : CCS

    doi: 10.1186/s12964-026-02801-7

    Affinity matured, anti-Gal-3BP antibodies show superior in vitro efficacy for blocking PDAC cell migration and invasion. A . Schematic diagram of antibody affinity maturation of the humanized anti-Gal-3BP antibody. The #13 − 7 clone was used as a template. Two high-affinity clones, #34 and #132, were tested in further study. B . Affinity of the engineered #34 and #132 antibody clones measured by Octet (on left) and their value (Table on right). The affinity of parental clone #13 − 7 is shown at the bottom of the table. C – D . Validation of Gal-3BP binding of engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132), shown by immunoprecipitation in PDX_PC 110,621 ( C ) or PDAC PKCY ( D ). E – F . Migration and invasion of PDX_PC 115,026 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG (human IgG). Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 200 μm. G – H . Migration and invasion of Pan02 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG. Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 50 μm.* p < 0.05; ** p < 0.01; *** p < 0.001; ns (not significant)
    Figure Legend Snippet: Affinity matured, anti-Gal-3BP antibodies show superior in vitro efficacy for blocking PDAC cell migration and invasion. A . Schematic diagram of antibody affinity maturation of the humanized anti-Gal-3BP antibody. The #13 − 7 clone was used as a template. Two high-affinity clones, #34 and #132, were tested in further study. B . Affinity of the engineered #34 and #132 antibody clones measured by Octet (on left) and their value (Table on right). The affinity of parental clone #13 − 7 is shown at the bottom of the table. C – D . Validation of Gal-3BP binding of engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132), shown by immunoprecipitation in PDX_PC 110,621 ( C ) or PDAC PKCY ( D ). E – F . Migration and invasion of PDX_PC 115,026 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG (human IgG). Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 200 μm. G – H . Migration and invasion of Pan02 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG. Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 50 μm.* p < 0.05; ** p < 0.01; *** p < 0.001; ns (not significant)

    Techniques Used: In Vitro, Blocking Assay, Migration, Clone Assay, Biomarker Discovery, Binding Assay, Immunoprecipitation

    Gal-3BP positively regulates VEGFA production in PDAC. A . Clustered heatmap of the protein expression profile for PDX_PC 110,621 treated with rhGal-3BP, rhEGF, or rhGal-3BP+rhEGF combination. Red indicates upregulated protein levels, whereas green shows downregulated cases. The bottom panel indicates the VEGFA-VEGFR2 pathway enriched in C1 cluster, as shown by WikiPathway 2021 analysis. B and C . mRNA ( B ) and protein expression ( C ) of VEGFA in PDX_PC 110,621 after Gal-3BP knockdown by shRNA. D . VEGFA secretion measured by ELISA in PDX_PC 110,621 after Gal-3BP knockdown. E . The secretion of VEGFA measured in Panc-1 cells after Gal-3BP overexpression. F . Transwell migration of HUVEC co-cultured with control PDX_PC 110,621 or with Gal-3BP knockdown. The graph on right shows relative migration rate. Scale bar: 50 μm. G – H . Expression correlation analysis between Gal-3BP and VEGFA for mRNA ( G ) or protein ( H ), using cBioportal database.* p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)
    Figure Legend Snippet: Gal-3BP positively regulates VEGFA production in PDAC. A . Clustered heatmap of the protein expression profile for PDX_PC 110,621 treated with rhGal-3BP, rhEGF, or rhGal-3BP+rhEGF combination. Red indicates upregulated protein levels, whereas green shows downregulated cases. The bottom panel indicates the VEGFA-VEGFR2 pathway enriched in C1 cluster, as shown by WikiPathway 2021 analysis. B and C . mRNA ( B ) and protein expression ( C ) of VEGFA in PDX_PC 110,621 after Gal-3BP knockdown by shRNA. D . VEGFA secretion measured by ELISA in PDX_PC 110,621 after Gal-3BP knockdown. E . The secretion of VEGFA measured in Panc-1 cells after Gal-3BP overexpression. F . Transwell migration of HUVEC co-cultured with control PDX_PC 110,621 or with Gal-3BP knockdown. The graph on right shows relative migration rate. Scale bar: 50 μm. G – H . Expression correlation analysis between Gal-3BP and VEGFA for mRNA ( G ) or protein ( H ), using cBioportal database.* p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Techniques Used: Expressing, Knockdown, shRNA, Enzyme-linked Immunosorbent Assay, Over Expression, Migration, Cell Culture, Control

    STAT3/AKT activation mediates VEGFA production induced by Gal-3BP and is reversed by the engineered anti-Gal-3BP antibodies. A . Activation of EGFR, STAT3, and AKT in PDX_PC 110,621 with Gal-3BP knockdown, as analyzed by Western blot using phosphoantibodies. B . Activation profile of AKT and STAT3 determined by Western blot in Panc-1 stimulated with rhGal-3BP (1 µg/ml). b-actin was used as a loading control. C and D . mRNA ( C ) and secreted VEGFA levels (C and D ) in rhGal-3BP-stimulated PDX_PC 17,884 cells. E and F . Engineered Gal-3BP antibody reduces VEGFA mRNA expression ( E ) and secretion ( F ) in PDAC cell PDX_PC 17,884. G and H . The #34 or #132 Ab inactivate EGFR and STAT3 in PDX_PC 110,621. The cells were treated with 1–5 µg/ml ( G ) or 0.25–1 µg/ml ( H ) and analyzed by Western blot. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)
    Figure Legend Snippet: STAT3/AKT activation mediates VEGFA production induced by Gal-3BP and is reversed by the engineered anti-Gal-3BP antibodies. A . Activation of EGFR, STAT3, and AKT in PDX_PC 110,621 with Gal-3BP knockdown, as analyzed by Western blot using phosphoantibodies. B . Activation profile of AKT and STAT3 determined by Western blot in Panc-1 stimulated with rhGal-3BP (1 µg/ml). b-actin was used as a loading control. C and D . mRNA ( C ) and secreted VEGFA levels (C and D ) in rhGal-3BP-stimulated PDX_PC 17,884 cells. E and F . Engineered Gal-3BP antibody reduces VEGFA mRNA expression ( E ) and secretion ( F ) in PDAC cell PDX_PC 17,884. G and H . The #34 or #132 Ab inactivate EGFR and STAT3 in PDX_PC 110,621. The cells were treated with 1–5 µg/ml ( G ) or 0.25–1 µg/ml ( H ) and analyzed by Western blot. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Techniques Used: Activation Assay, Knockdown, Western Blot, Control, Expressing

    Gal-3BP activates STAT3/AKT and promotes migration and tube formation of HUVEC cells. A . Increased migration of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows the relative migratory activity. B . Increased tube formation of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows number of meshes counted from the images. C and D . #132, but not anti-VEGFR2 antibody (ramucirumab), can reverse the increased migration ( C ) or tube formation ( D ) of HUVEC cells, which was induced by Gal-3BP treatment. Upper panel shows representative images, and lower graphs present analysis data. Graphs at bottom show the relative migratory activity ( C ) or the number of meshes ( D ). Scale bar: 200 μm. E . Migration assay of Gal-3BP-stimulated HUVEC cells in combination with anti-Gal-3BP antibodies (#34 and #132) or hIgG. Upper panels show representative images, and lower graphs present analysis data. Bottom graphs show relative migratory activity. Scale bar: 200 μm. F . Tube formation assay of HUVEC cells in PDX_PC 115,026-conditioned media in the presence of anti-Gal-3BP antibodies (#13 − 7, #34 and #132) or hIgG. Scale bar: 200 μm. G . Western blot analysis of p-STAT3, STAT3, p-AKT, AKT, and β-actin in VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml)-stimulated HUVEC cells. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)
    Figure Legend Snippet: Gal-3BP activates STAT3/AKT and promotes migration and tube formation of HUVEC cells. A . Increased migration of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows the relative migratory activity. B . Increased tube formation of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows number of meshes counted from the images. C and D . #132, but not anti-VEGFR2 antibody (ramucirumab), can reverse the increased migration ( C ) or tube formation ( D ) of HUVEC cells, which was induced by Gal-3BP treatment. Upper panel shows representative images, and lower graphs present analysis data. Graphs at bottom show the relative migratory activity ( C ) or the number of meshes ( D ). Scale bar: 200 μm. E . Migration assay of Gal-3BP-stimulated HUVEC cells in combination with anti-Gal-3BP antibodies (#34 and #132) or hIgG. Upper panels show representative images, and lower graphs present analysis data. Bottom graphs show relative migratory activity. Scale bar: 200 μm. F . Tube formation assay of HUVEC cells in PDX_PC 115,026-conditioned media in the presence of anti-Gal-3BP antibodies (#13 − 7, #34 and #132) or hIgG. Scale bar: 200 μm. G . Western blot analysis of p-STAT3, STAT3, p-AKT, AKT, and β-actin in VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml)-stimulated HUVEC cells. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Techniques Used: Migration, Activity Assay, Tube Formation Assay, Western Blot

    VAMP5 is a mediator for the pro-angiogenic effect of Gal-3BP in HUVEC cells. A . Tube formation assay of HUVEC cells treated with Vehicle (DMSO), lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), and S3I-201 (30 µM, right graph) in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 200 μm. B . HUVEC migration assay with Vehicle, lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), S3I-201 (30 µM, right graph) treatment in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 50 μm. C . Schematic diagram for IP-LC-MS/MS analysis to identify receptor protein of secreted Gal-3BP on HUVEC cells. Engineered anti-Gal-3BP antibody #132 was used, and top 3 candidates were listed. D . MICAL2, VAMP5, and FADD mRNA levels in HUVEC cells with shRNA-mediated knockdown. E and F . Tube formation and migration assay of HUVEC cells depleted with MICAL2, VAMP5, and FADD after treatment with rhGal-3BP (1 µg/ml, marked as Gal-3BP[+]). Upper panel shows representative images, and lower graphs present data analysis. Scale bar: 200 μm (tube formation assay) and 50 μm (migration assay). G . Western blot for VAMP5, p-STAT3, STAT3, p-AKT, AKT, and β-actin in shRNA-targeted VAMP5 knockdown of HUVEC cells (left) and VAMP5 -overexpressing HUVEC cells (right). * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)
    Figure Legend Snippet: VAMP5 is a mediator for the pro-angiogenic effect of Gal-3BP in HUVEC cells. A . Tube formation assay of HUVEC cells treated with Vehicle (DMSO), lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), and S3I-201 (30 µM, right graph) in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 200 μm. B . HUVEC migration assay with Vehicle, lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), S3I-201 (30 µM, right graph) treatment in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 50 μm. C . Schematic diagram for IP-LC-MS/MS analysis to identify receptor protein of secreted Gal-3BP on HUVEC cells. Engineered anti-Gal-3BP antibody #132 was used, and top 3 candidates were listed. D . MICAL2, VAMP5, and FADD mRNA levels in HUVEC cells with shRNA-mediated knockdown. E and F . Tube formation and migration assay of HUVEC cells depleted with MICAL2, VAMP5, and FADD after treatment with rhGal-3BP (1 µg/ml, marked as Gal-3BP[+]). Upper panel shows representative images, and lower graphs present data analysis. Scale bar: 200 μm (tube formation assay) and 50 μm (migration assay). G . Western blot for VAMP5, p-STAT3, STAT3, p-AKT, AKT, and β-actin in shRNA-targeted VAMP5 knockdown of HUVEC cells (left) and VAMP5 -overexpressing HUVEC cells (right). * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Techniques Used: Tube Formation Assay, Migration, Liquid Chromatography with Mass Spectroscopy, shRNA, Knockdown, Western Blot

    Engineered anti-Gal-3BP antibodies attenuate the in vivo angiogenesis of PDAC. A . Schematic representation of the PDAC orthotopic model and treatment procedure of the Gal-3BP antibodies (#34 and #132) along with live imaging schedule using IVIS. B . Luciferase assay of the PDX_PC 110,621 cells with luciferase stable expression (110621_luc). C . Body weight measurements for each group during the antibody treatment ( n = 20). D and E . A graph of a ROI value ( D ) indicating tumor progression between week 3 (start of antibody treatment) and week 5 (end of antibody treatment) along with representative IVIS images for each treatment group ( E ) from week 3 to week 5 ( n = 20). F . Images of dissected PDAC orthotopic tumors from each antibody treatment group. G . Graph showing the average tumor weight for each antibody treatment group. H . Immunohistochemistry analysis of Ki-67 and CD31 in orthotopic tumors. Representative images are shown on the left panels, and their relative signal was presented in the graphs on right. Scale bar: 200 μm (H&E and Ki-67 staining) and 50 μm (CD31 staining) ( n = 20). I . Western blot analysis of CD31, Gal 3BP, and VEGFA expression levels in harvested tumors from each group. Graphs on right presents densitometry results for VEGFA or CD31 normalized by b-actin. * p < 0.05; *** p < 0.001; ns (not significant)
    Figure Legend Snippet: Engineered anti-Gal-3BP antibodies attenuate the in vivo angiogenesis of PDAC. A . Schematic representation of the PDAC orthotopic model and treatment procedure of the Gal-3BP antibodies (#34 and #132) along with live imaging schedule using IVIS. B . Luciferase assay of the PDX_PC 110,621 cells with luciferase stable expression (110621_luc). C . Body weight measurements for each group during the antibody treatment ( n = 20). D and E . A graph of a ROI value ( D ) indicating tumor progression between week 3 (start of antibody treatment) and week 5 (end of antibody treatment) along with representative IVIS images for each treatment group ( E ) from week 3 to week 5 ( n = 20). F . Images of dissected PDAC orthotopic tumors from each antibody treatment group. G . Graph showing the average tumor weight for each antibody treatment group. H . Immunohistochemistry analysis of Ki-67 and CD31 in orthotopic tumors. Representative images are shown on the left panels, and their relative signal was presented in the graphs on right. Scale bar: 200 μm (H&E and Ki-67 staining) and 50 μm (CD31 staining) ( n = 20). I . Western blot analysis of CD31, Gal 3BP, and VEGFA expression levels in harvested tumors from each group. Graphs on right presents densitometry results for VEGFA or CD31 normalized by b-actin. * p < 0.05; *** p < 0.001; ns (not significant)

    Techniques Used: In Vivo, Imaging, Luciferase, Expressing, Immunohistochemistry, Staining, Western Blot

    Engineered anti-Gal-3BP antibodies abrogate PDAC metastasis in vivo. A . Schematic diagram of the PDAC lung metastasis experiment using a tail-vein injection of BxPC3 PDAC cells along with the treatment schedule of #13 − 7 ( n = 6), #132 ( n = 6), and control IgG ( n = 8). B . Body weight of each treatment group during the experiment period ( n = 20). C and D . Images of lungs ( C ) and their weight ( D ) at the endpoint from each treatment group. E and F . Metastasis index ( E ) or PanCK-positive area ( F ) measured by immunohistochemistry of the lungs from each treatment group. Representative images are shown on left panels, and the graphs on right show data analysis. Scale bar: 200 μm. G . Graphical summary of the study, indicating the role of extracellular Gal-3BP in promoting angiogenesis by upregulating VEGFA secretion from cancer cells (autocrine effect) or directly interacting with VAMP5 on HUVEC (paracrine effect). * p < 0.05; *** p < 0.001; **** p < 0.0001; ns (not significant)
    Figure Legend Snippet: Engineered anti-Gal-3BP antibodies abrogate PDAC metastasis in vivo. A . Schematic diagram of the PDAC lung metastasis experiment using a tail-vein injection of BxPC3 PDAC cells along with the treatment schedule of #13 − 7 ( n = 6), #132 ( n = 6), and control IgG ( n = 8). B . Body weight of each treatment group during the experiment period ( n = 20). C and D . Images of lungs ( C ) and their weight ( D ) at the endpoint from each treatment group. E and F . Metastasis index ( E ) or PanCK-positive area ( F ) measured by immunohistochemistry of the lungs from each treatment group. Representative images are shown on left panels, and the graphs on right show data analysis. Scale bar: 200 μm. G . Graphical summary of the study, indicating the role of extracellular Gal-3BP in promoting angiogenesis by upregulating VEGFA secretion from cancer cells (autocrine effect) or directly interacting with VAMP5 on HUVEC (paracrine effect). * p < 0.05; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Techniques Used: In Vivo, Injection, Control, Immunohistochemistry



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    antibody against st6gal1  (R&D Systems)
    93
    R&D Systems antibody against st6gal1
    Affinity matured, <t>anti-Gal-3BP</t> antibodies show superior in vitro efficacy for blocking PDAC cell migration and invasion. A . Schematic diagram of antibody affinity maturation of the humanized anti-Gal-3BP antibody. The #13 − 7 clone was used as a template. Two high-affinity clones, #34 and #132, were tested in further study. B . Affinity of the engineered #34 and #132 antibody clones measured by Octet (on left) and their value (Table on right). The affinity of parental clone #13 − 7 is shown at the bottom of the table. C – D . Validation of Gal-3BP binding of engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132), shown by immunoprecipitation in PDX_PC 110,621 ( C ) or PDAC PKCY ( D ). E – F . Migration and invasion of PDX_PC 115,026 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG (human IgG). Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 200 μm. G – H . Migration and invasion of Pan02 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG. Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 50 μm.* p < 0.05; ** p < 0.01; *** p < 0.001; ns (not significant)
    Antibody Against St6gal1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Magellan platform-driven virtual screening for non-competitive, allosteric pharmacological regulators of β-Gal. ( a ) Ribbon diagram of β-Gal monomer used for VS (PDB ID: 3THC), with domains individually colored: β-domain 1 (red), TIM barrel (blue), TIM-β1 loop (yellow), and β-domain 2 (green). ( b ) High-throughput, docking-based virtual screening workflow for identifying small molecules. β-Gal, β-galactosidase; DSF, differential scanning fluorimetry; PDB, Protein Data Bank; TIM, triosephosphate isomerase; VS, virtual screening.

    Journal: International Journal of Molecular Sciences

    Article Title: Development of Small-Molecule Allosteric Modulators of Beta-Galactosidase (β-Gal) for the Treatment of GM1 Gangliosidosis and Morquio B

    doi: 10.3390/ijms27083631

    Figure Lengend Snippet: Magellan platform-driven virtual screening for non-competitive, allosteric pharmacological regulators of β-Gal. ( a ) Ribbon diagram of β-Gal monomer used for VS (PDB ID: 3THC), with domains individually colored: β-domain 1 (red), TIM barrel (blue), TIM-β1 loop (yellow), and β-domain 2 (green). ( b ) High-throughput, docking-based virtual screening workflow for identifying small molecules. β-Gal, β-galactosidase; DSF, differential scanning fluorimetry; PDB, Protein Data Bank; TIM, triosephosphate isomerase; VS, virtual screening.

    Article Snippet: Each 25 μL reaction contained 12.5 μL of 1.5 μM recombinant human β-Gal protein (rhGLB1; Novoprotein, Shanghai, China) in PBS (pH 7.4), resulting in a final protein concentration of 1 μM, and 12.5 μL of compound solution dissolved in 100% DMSO and diluted in protein buffer to achieve a final DMSO concentration of 2%.

    Techniques: High Throughput Screening Assay

    Binding of small-molecule hit compounds to β-Gal protein as measured by DSF. ( a ) Change in melting temperature (ΔTm) of recombinant human β-Gal in the presence of hit compounds #1–3 at 100 μM and #1–9 at 30 μM, measured at pH 7.4. Mean ΔTm ± SD values are shown. The dotted line indicates the DSF screening threshold (ΔTm ≥ 0.5 °C). ( b ) Dose-dependent effect of Hit 3 on β-Gal thermal stability, with mean ΔTm ± SD. ( c ) Chemical structure of Hit 3 and Hit 5. DSF, differential scanning fluorimetry; SD, standard deviation; Tm, melting temperature.

    Journal: International Journal of Molecular Sciences

    Article Title: Development of Small-Molecule Allosteric Modulators of Beta-Galactosidase (β-Gal) for the Treatment of GM1 Gangliosidosis and Morquio B

    doi: 10.3390/ijms27083631

    Figure Lengend Snippet: Binding of small-molecule hit compounds to β-Gal protein as measured by DSF. ( a ) Change in melting temperature (ΔTm) of recombinant human β-Gal in the presence of hit compounds #1–3 at 100 μM and #1–9 at 30 μM, measured at pH 7.4. Mean ΔTm ± SD values are shown. The dotted line indicates the DSF screening threshold (ΔTm ≥ 0.5 °C). ( b ) Dose-dependent effect of Hit 3 on β-Gal thermal stability, with mean ΔTm ± SD. ( c ) Chemical structure of Hit 3 and Hit 5. DSF, differential scanning fluorimetry; SD, standard deviation; Tm, melting temperature.

    Article Snippet: Each 25 μL reaction contained 12.5 μL of 1.5 μM recombinant human β-Gal protein (rhGLB1; Novoprotein, Shanghai, China) in PBS (pH 7.4), resulting in a final protein concentration of 1 μM, and 12.5 μL of compound solution dissolved in 100% DMSO and diluted in protein buffer to achieve a final DMSO concentration of 2%.

    Techniques: Binding Assay, Recombinant, Standard Deviation

    ( a ) Hit 3 (left panel) and Hit 5 (right panel) reduction in GM1 ganglioside accumulation in canine fibroblasts. Representative immunofluorescence images of WT and R60H β-Gal canine fibroblasts (untreated or treated with indicated compounds). Images show GM1 ganglioside antibody staining (first column), merge of GM1 ganglioside staining and DAPI (second column), inset of a region (third column), and CellMask staining (fourth column). Scale bar: 100 μM; inset scale 10 μM. ( b , c ) Dose–response of Hit 3 and Hit 5, respectively. Results are presented as mean ± SD. Data represent the percentage of GM1 ganglioside area per cell area relative to untreated R60H canine fibroblasts. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s Multiple Comparison Test. Asterisks indicate statistically significant differences compared to untreated R60H canine fibroblasts: *** p < 0.001, **** p < 0.0001; WT, wild type.

    Journal: International Journal of Molecular Sciences

    Article Title: Development of Small-Molecule Allosteric Modulators of Beta-Galactosidase (β-Gal) for the Treatment of GM1 Gangliosidosis and Morquio B

    doi: 10.3390/ijms27083631

    Figure Lengend Snippet: ( a ) Hit 3 (left panel) and Hit 5 (right panel) reduction in GM1 ganglioside accumulation in canine fibroblasts. Representative immunofluorescence images of WT and R60H β-Gal canine fibroblasts (untreated or treated with indicated compounds). Images show GM1 ganglioside antibody staining (first column), merge of GM1 ganglioside staining and DAPI (second column), inset of a region (third column), and CellMask staining (fourth column). Scale bar: 100 μM; inset scale 10 μM. ( b , c ) Dose–response of Hit 3 and Hit 5, respectively. Results are presented as mean ± SD. Data represent the percentage of GM1 ganglioside area per cell area relative to untreated R60H canine fibroblasts. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s Multiple Comparison Test. Asterisks indicate statistically significant differences compared to untreated R60H canine fibroblasts: *** p < 0.001, **** p < 0.0001; WT, wild type.

    Article Snippet: Each 25 μL reaction contained 12.5 μL of 1.5 μM recombinant human β-Gal protein (rhGLB1; Novoprotein, Shanghai, China) in PBS (pH 7.4), resulting in a final protein concentration of 1 μM, and 12.5 μL of compound solution dissolved in 100% DMSO and diluted in protein buffer to achieve a final DMSO concentration of 2%.

    Techniques: Immunofluorescence, Staining, Comparison

    ( a ) Representative immunofluorescence images of WT or R60H β-Gal canine fibroblasts (untreated or treated with indicated compounds). Images show GM1 ganglioside antibody staining (first column), merge of GM1 ganglioside staining and DAPI (second column), inset of a region (third column), and CellMask staining (fourth column). Scale bar: 100 μm; inset scale 10 μm. ( b ) Quantification of GM1 ganglioside area per cell area at 3.13 μM and 12.5 μM concentrations. Results are expressed as a percentage relative to untreated cells and are presented as mean ± SD. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s Multiple Comparison Test. Asterisks indicate statistically significant differences compared to untreated R60H canine fibroblasts: ns, not significant; * p < 0.05; ** p < 0.01; **** p < 0.0001.

    Journal: International Journal of Molecular Sciences

    Article Title: Development of Small-Molecule Allosteric Modulators of Beta-Galactosidase (β-Gal) for the Treatment of GM1 Gangliosidosis and Morquio B

    doi: 10.3390/ijms27083631

    Figure Lengend Snippet: ( a ) Representative immunofluorescence images of WT or R60H β-Gal canine fibroblasts (untreated or treated with indicated compounds). Images show GM1 ganglioside antibody staining (first column), merge of GM1 ganglioside staining and DAPI (second column), inset of a region (third column), and CellMask staining (fourth column). Scale bar: 100 μm; inset scale 10 μm. ( b ) Quantification of GM1 ganglioside area per cell area at 3.13 μM and 12.5 μM concentrations. Results are expressed as a percentage relative to untreated cells and are presented as mean ± SD. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s Multiple Comparison Test. Asterisks indicate statistically significant differences compared to untreated R60H canine fibroblasts: ns, not significant; * p < 0.05; ** p < 0.01; **** p < 0.0001.

    Article Snippet: Each 25 μL reaction contained 12.5 μL of 1.5 μM recombinant human β-Gal protein (rhGLB1; Novoprotein, Shanghai, China) in PBS (pH 7.4), resulting in a final protein concentration of 1 μM, and 12.5 μL of compound solution dissolved in 100% DMSO and diluted in protein buffer to achieve a final DMSO concentration of 2%.

    Techniques: Immunofluorescence, Staining, Comparison

    Surface plasmon resonance (SPR) dose–response for compounds ( a ) Cpd 6, ( b ) Cpd 13, and ( c ) Cpd 18, showing their binding to immobilized β-Gal at neutral pH (7.4).

    Journal: International Journal of Molecular Sciences

    Article Title: Development of Small-Molecule Allosteric Modulators of Beta-Galactosidase (β-Gal) for the Treatment of GM1 Gangliosidosis and Morquio B

    doi: 10.3390/ijms27083631

    Figure Lengend Snippet: Surface plasmon resonance (SPR) dose–response for compounds ( a ) Cpd 6, ( b ) Cpd 13, and ( c ) Cpd 18, showing their binding to immobilized β-Gal at neutral pH (7.4).

    Article Snippet: Each 25 μL reaction contained 12.5 μL of 1.5 μM recombinant human β-Gal protein (rhGLB1; Novoprotein, Shanghai, China) in PBS (pH 7.4), resulting in a final protein concentration of 1 μM, and 12.5 μL of compound solution dissolved in 100% DMSO and diluted in protein buffer to achieve a final DMSO concentration of 2%.

    Techniques: SPR Assay, Binding Assay

    Affinity matured, anti-Gal-3BP antibodies show superior in vitro efficacy for blocking PDAC cell migration and invasion. A . Schematic diagram of antibody affinity maturation of the humanized anti-Gal-3BP antibody. The #13 − 7 clone was used as a template. Two high-affinity clones, #34 and #132, were tested in further study. B . Affinity of the engineered #34 and #132 antibody clones measured by Octet (on left) and their value (Table on right). The affinity of parental clone #13 − 7 is shown at the bottom of the table. C – D . Validation of Gal-3BP binding of engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132), shown by immunoprecipitation in PDX_PC 110,621 ( C ) or PDAC PKCY ( D ). E – F . Migration and invasion of PDX_PC 115,026 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG (human IgG). Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 200 μm. G – H . Migration and invasion of Pan02 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG. Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 50 μm.* p < 0.05; ** p < 0.01; *** p < 0.001; ns (not significant)

    Journal: Cell Communication and Signaling : CCS

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    doi: 10.1186/s12964-026-02801-7

    Figure Lengend Snippet: Affinity matured, anti-Gal-3BP antibodies show superior in vitro efficacy for blocking PDAC cell migration and invasion. A . Schematic diagram of antibody affinity maturation of the humanized anti-Gal-3BP antibody. The #13 − 7 clone was used as a template. Two high-affinity clones, #34 and #132, were tested in further study. B . Affinity of the engineered #34 and #132 antibody clones measured by Octet (on left) and their value (Table on right). The affinity of parental clone #13 − 7 is shown at the bottom of the table. C – D . Validation of Gal-3BP binding of engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132), shown by immunoprecipitation in PDX_PC 110,621 ( C ) or PDAC PKCY ( D ). E – F . Migration and invasion of PDX_PC 115,026 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG (human IgG). Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 200 μm. G – H . Migration and invasion of Pan02 treated with engineered anti-Gal-3BP antibodies (#13 − 7, #34, and #132) or hIgG. Upper panel shows representative images, and lower graphs present analysis data. Scale bar: 50 μm.* p < 0.05; ** p < 0.01; *** p < 0.001; ns (not significant)

    Article Snippet: The immunoblotting was performed with anti-Gal-3BP antibody (AF2226, R&D systems), anti-VEGFA antibody (ab46154, Abcam), anti-p-EGFR antibody (3777, Cell Signaling Technology), anti-EGFR antibody (4267, Cell Signaling Technology), anti-p-AKT antibody (9271, Cell Signaling Technology), anti-AKT antibody (9272, Cell Signaling Technology), anti-p-STAT3 antibody (9145, Cell Signaling Technology), anti-STAT3 antibody (4904, Cell Signaling Technology), anti-β-actin antibody (Santa Cruz Biotechnology), anti-VAMP5 antibody (ab216044, Abcam), and anti-CD31 antibody (77699, Cell Signaling Technology).

    Techniques: In Vitro, Blocking Assay, Migration, Clone Assay, Biomarker Discovery, Binding Assay, Immunoprecipitation

    Gal-3BP positively regulates VEGFA production in PDAC. A . Clustered heatmap of the protein expression profile for PDX_PC 110,621 treated with rhGal-3BP, rhEGF, or rhGal-3BP+rhEGF combination. Red indicates upregulated protein levels, whereas green shows downregulated cases. The bottom panel indicates the VEGFA-VEGFR2 pathway enriched in C1 cluster, as shown by WikiPathway 2021 analysis. B and C . mRNA ( B ) and protein expression ( C ) of VEGFA in PDX_PC 110,621 after Gal-3BP knockdown by shRNA. D . VEGFA secretion measured by ELISA in PDX_PC 110,621 after Gal-3BP knockdown. E . The secretion of VEGFA measured in Panc-1 cells after Gal-3BP overexpression. F . Transwell migration of HUVEC co-cultured with control PDX_PC 110,621 or with Gal-3BP knockdown. The graph on right shows relative migration rate. Scale bar: 50 μm. G – H . Expression correlation analysis between Gal-3BP and VEGFA for mRNA ( G ) or protein ( H ), using cBioportal database.* p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Journal: Cell Communication and Signaling : CCS

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    doi: 10.1186/s12964-026-02801-7

    Figure Lengend Snippet: Gal-3BP positively regulates VEGFA production in PDAC. A . Clustered heatmap of the protein expression profile for PDX_PC 110,621 treated with rhGal-3BP, rhEGF, or rhGal-3BP+rhEGF combination. Red indicates upregulated protein levels, whereas green shows downregulated cases. The bottom panel indicates the VEGFA-VEGFR2 pathway enriched in C1 cluster, as shown by WikiPathway 2021 analysis. B and C . mRNA ( B ) and protein expression ( C ) of VEGFA in PDX_PC 110,621 after Gal-3BP knockdown by shRNA. D . VEGFA secretion measured by ELISA in PDX_PC 110,621 after Gal-3BP knockdown. E . The secretion of VEGFA measured in Panc-1 cells after Gal-3BP overexpression. F . Transwell migration of HUVEC co-cultured with control PDX_PC 110,621 or with Gal-3BP knockdown. The graph on right shows relative migration rate. Scale bar: 50 μm. G – H . Expression correlation analysis between Gal-3BP and VEGFA for mRNA ( G ) or protein ( H ), using cBioportal database.* p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Article Snippet: The immunoblotting was performed with anti-Gal-3BP antibody (AF2226, R&D systems), anti-VEGFA antibody (ab46154, Abcam), anti-p-EGFR antibody (3777, Cell Signaling Technology), anti-EGFR antibody (4267, Cell Signaling Technology), anti-p-AKT antibody (9271, Cell Signaling Technology), anti-AKT antibody (9272, Cell Signaling Technology), anti-p-STAT3 antibody (9145, Cell Signaling Technology), anti-STAT3 antibody (4904, Cell Signaling Technology), anti-β-actin antibody (Santa Cruz Biotechnology), anti-VAMP5 antibody (ab216044, Abcam), and anti-CD31 antibody (77699, Cell Signaling Technology).

    Techniques: Expressing, Knockdown, shRNA, Enzyme-linked Immunosorbent Assay, Over Expression, Migration, Cell Culture, Control

    STAT3/AKT activation mediates VEGFA production induced by Gal-3BP and is reversed by the engineered anti-Gal-3BP antibodies. A . Activation of EGFR, STAT3, and AKT in PDX_PC 110,621 with Gal-3BP knockdown, as analyzed by Western blot using phosphoantibodies. B . Activation profile of AKT and STAT3 determined by Western blot in Panc-1 stimulated with rhGal-3BP (1 µg/ml). b-actin was used as a loading control. C and D . mRNA ( C ) and secreted VEGFA levels (C and D ) in rhGal-3BP-stimulated PDX_PC 17,884 cells. E and F . Engineered Gal-3BP antibody reduces VEGFA mRNA expression ( E ) and secretion ( F ) in PDAC cell PDX_PC 17,884. G and H . The #34 or #132 Ab inactivate EGFR and STAT3 in PDX_PC 110,621. The cells were treated with 1–5 µg/ml ( G ) or 0.25–1 µg/ml ( H ) and analyzed by Western blot. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Journal: Cell Communication and Signaling : CCS

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    doi: 10.1186/s12964-026-02801-7

    Figure Lengend Snippet: STAT3/AKT activation mediates VEGFA production induced by Gal-3BP and is reversed by the engineered anti-Gal-3BP antibodies. A . Activation of EGFR, STAT3, and AKT in PDX_PC 110,621 with Gal-3BP knockdown, as analyzed by Western blot using phosphoantibodies. B . Activation profile of AKT and STAT3 determined by Western blot in Panc-1 stimulated with rhGal-3BP (1 µg/ml). b-actin was used as a loading control. C and D . mRNA ( C ) and secreted VEGFA levels (C and D ) in rhGal-3BP-stimulated PDX_PC 17,884 cells. E and F . Engineered Gal-3BP antibody reduces VEGFA mRNA expression ( E ) and secretion ( F ) in PDAC cell PDX_PC 17,884. G and H . The #34 or #132 Ab inactivate EGFR and STAT3 in PDX_PC 110,621. The cells were treated with 1–5 µg/ml ( G ) or 0.25–1 µg/ml ( H ) and analyzed by Western blot. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Article Snippet: The immunoblotting was performed with anti-Gal-3BP antibody (AF2226, R&D systems), anti-VEGFA antibody (ab46154, Abcam), anti-p-EGFR antibody (3777, Cell Signaling Technology), anti-EGFR antibody (4267, Cell Signaling Technology), anti-p-AKT antibody (9271, Cell Signaling Technology), anti-AKT antibody (9272, Cell Signaling Technology), anti-p-STAT3 antibody (9145, Cell Signaling Technology), anti-STAT3 antibody (4904, Cell Signaling Technology), anti-β-actin antibody (Santa Cruz Biotechnology), anti-VAMP5 antibody (ab216044, Abcam), and anti-CD31 antibody (77699, Cell Signaling Technology).

    Techniques: Activation Assay, Knockdown, Western Blot, Control, Expressing

    Gal-3BP activates STAT3/AKT and promotes migration and tube formation of HUVEC cells. A . Increased migration of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows the relative migratory activity. B . Increased tube formation of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows number of meshes counted from the images. C and D . #132, but not anti-VEGFR2 antibody (ramucirumab), can reverse the increased migration ( C ) or tube formation ( D ) of HUVEC cells, which was induced by Gal-3BP treatment. Upper panel shows representative images, and lower graphs present analysis data. Graphs at bottom show the relative migratory activity ( C ) or the number of meshes ( D ). Scale bar: 200 μm. E . Migration assay of Gal-3BP-stimulated HUVEC cells in combination with anti-Gal-3BP antibodies (#34 and #132) or hIgG. Upper panels show representative images, and lower graphs present analysis data. Bottom graphs show relative migratory activity. Scale bar: 200 μm. F . Tube formation assay of HUVEC cells in PDX_PC 115,026-conditioned media in the presence of anti-Gal-3BP antibodies (#13 − 7, #34 and #132) or hIgG. Scale bar: 200 μm. G . Western blot analysis of p-STAT3, STAT3, p-AKT, AKT, and β-actin in VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml)-stimulated HUVEC cells. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Journal: Cell Communication and Signaling : CCS

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    doi: 10.1186/s12964-026-02801-7

    Figure Lengend Snippet: Gal-3BP activates STAT3/AKT and promotes migration and tube formation of HUVEC cells. A . Increased migration of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows the relative migratory activity. B . Increased tube formation of HUVEC cells treated with VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml). Scale bar: 200 μm. Graph on right shows number of meshes counted from the images. C and D . #132, but not anti-VEGFR2 antibody (ramucirumab), can reverse the increased migration ( C ) or tube formation ( D ) of HUVEC cells, which was induced by Gal-3BP treatment. Upper panel shows representative images, and lower graphs present analysis data. Graphs at bottom show the relative migratory activity ( C ) or the number of meshes ( D ). Scale bar: 200 μm. E . Migration assay of Gal-3BP-stimulated HUVEC cells in combination with anti-Gal-3BP antibodies (#34 and #132) or hIgG. Upper panels show representative images, and lower graphs present analysis data. Bottom graphs show relative migratory activity. Scale bar: 200 μm. F . Tube formation assay of HUVEC cells in PDX_PC 115,026-conditioned media in the presence of anti-Gal-3BP antibodies (#13 − 7, #34 and #132) or hIgG. Scale bar: 200 μm. G . Western blot analysis of p-STAT3, STAT3, p-AKT, AKT, and β-actin in VEGFA (20 ng/ml) or Gal-3BP (1 µg/ml)-stimulated HUVEC cells. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Article Snippet: The immunoblotting was performed with anti-Gal-3BP antibody (AF2226, R&D systems), anti-VEGFA antibody (ab46154, Abcam), anti-p-EGFR antibody (3777, Cell Signaling Technology), anti-EGFR antibody (4267, Cell Signaling Technology), anti-p-AKT antibody (9271, Cell Signaling Technology), anti-AKT antibody (9272, Cell Signaling Technology), anti-p-STAT3 antibody (9145, Cell Signaling Technology), anti-STAT3 antibody (4904, Cell Signaling Technology), anti-β-actin antibody (Santa Cruz Biotechnology), anti-VAMP5 antibody (ab216044, Abcam), and anti-CD31 antibody (77699, Cell Signaling Technology).

    Techniques: Migration, Activity Assay, Tube Formation Assay, Western Blot

    VAMP5 is a mediator for the pro-angiogenic effect of Gal-3BP in HUVEC cells. A . Tube formation assay of HUVEC cells treated with Vehicle (DMSO), lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), and S3I-201 (30 µM, right graph) in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 200 μm. B . HUVEC migration assay with Vehicle, lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), S3I-201 (30 µM, right graph) treatment in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 50 μm. C . Schematic diagram for IP-LC-MS/MS analysis to identify receptor protein of secreted Gal-3BP on HUVEC cells. Engineered anti-Gal-3BP antibody #132 was used, and top 3 candidates were listed. D . MICAL2, VAMP5, and FADD mRNA levels in HUVEC cells with shRNA-mediated knockdown. E and F . Tube formation and migration assay of HUVEC cells depleted with MICAL2, VAMP5, and FADD after treatment with rhGal-3BP (1 µg/ml, marked as Gal-3BP[+]). Upper panel shows representative images, and lower graphs present data analysis. Scale bar: 200 μm (tube formation assay) and 50 μm (migration assay). G . Western blot for VAMP5, p-STAT3, STAT3, p-AKT, AKT, and β-actin in shRNA-targeted VAMP5 knockdown of HUVEC cells (left) and VAMP5 -overexpressing HUVEC cells (right). * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Journal: Cell Communication and Signaling : CCS

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    doi: 10.1186/s12964-026-02801-7

    Figure Lengend Snippet: VAMP5 is a mediator for the pro-angiogenic effect of Gal-3BP in HUVEC cells. A . Tube formation assay of HUVEC cells treated with Vehicle (DMSO), lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), and S3I-201 (30 µM, right graph) in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 200 μm. B . HUVEC migration assay with Vehicle, lapatinib (1 µM, left graph), MK-2206 (100 nM, middle graph), S3I-201 (30 µM, right graph) treatment in the presence of rhGal-3BP (1 µg/ml). Left panels show representative images, and graphs on right present data analysis. Scale bar: 50 μm. C . Schematic diagram for IP-LC-MS/MS analysis to identify receptor protein of secreted Gal-3BP on HUVEC cells. Engineered anti-Gal-3BP antibody #132 was used, and top 3 candidates were listed. D . MICAL2, VAMP5, and FADD mRNA levels in HUVEC cells with shRNA-mediated knockdown. E and F . Tube formation and migration assay of HUVEC cells depleted with MICAL2, VAMP5, and FADD after treatment with rhGal-3BP (1 µg/ml, marked as Gal-3BP[+]). Upper panel shows representative images, and lower graphs present data analysis. Scale bar: 200 μm (tube formation assay) and 50 μm (migration assay). G . Western blot for VAMP5, p-STAT3, STAT3, p-AKT, AKT, and β-actin in shRNA-targeted VAMP5 knockdown of HUVEC cells (left) and VAMP5 -overexpressing HUVEC cells (right). * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Article Snippet: The immunoblotting was performed with anti-Gal-3BP antibody (AF2226, R&D systems), anti-VEGFA antibody (ab46154, Abcam), anti-p-EGFR antibody (3777, Cell Signaling Technology), anti-EGFR antibody (4267, Cell Signaling Technology), anti-p-AKT antibody (9271, Cell Signaling Technology), anti-AKT antibody (9272, Cell Signaling Technology), anti-p-STAT3 antibody (9145, Cell Signaling Technology), anti-STAT3 antibody (4904, Cell Signaling Technology), anti-β-actin antibody (Santa Cruz Biotechnology), anti-VAMP5 antibody (ab216044, Abcam), and anti-CD31 antibody (77699, Cell Signaling Technology).

    Techniques: Tube Formation Assay, Migration, Liquid Chromatography with Mass Spectroscopy, shRNA, Knockdown, Western Blot

    Engineered anti-Gal-3BP antibodies attenuate the in vivo angiogenesis of PDAC. A . Schematic representation of the PDAC orthotopic model and treatment procedure of the Gal-3BP antibodies (#34 and #132) along with live imaging schedule using IVIS. B . Luciferase assay of the PDX_PC 110,621 cells with luciferase stable expression (110621_luc). C . Body weight measurements for each group during the antibody treatment ( n = 20). D and E . A graph of a ROI value ( D ) indicating tumor progression between week 3 (start of antibody treatment) and week 5 (end of antibody treatment) along with representative IVIS images for each treatment group ( E ) from week 3 to week 5 ( n = 20). F . Images of dissected PDAC orthotopic tumors from each antibody treatment group. G . Graph showing the average tumor weight for each antibody treatment group. H . Immunohistochemistry analysis of Ki-67 and CD31 in orthotopic tumors. Representative images are shown on the left panels, and their relative signal was presented in the graphs on right. Scale bar: 200 μm (H&E and Ki-67 staining) and 50 μm (CD31 staining) ( n = 20). I . Western blot analysis of CD31, Gal 3BP, and VEGFA expression levels in harvested tumors from each group. Graphs on right presents densitometry results for VEGFA or CD31 normalized by b-actin. * p < 0.05; *** p < 0.001; ns (not significant)

    Journal: Cell Communication and Signaling : CCS

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    doi: 10.1186/s12964-026-02801-7

    Figure Lengend Snippet: Engineered anti-Gal-3BP antibodies attenuate the in vivo angiogenesis of PDAC. A . Schematic representation of the PDAC orthotopic model and treatment procedure of the Gal-3BP antibodies (#34 and #132) along with live imaging schedule using IVIS. B . Luciferase assay of the PDX_PC 110,621 cells with luciferase stable expression (110621_luc). C . Body weight measurements for each group during the antibody treatment ( n = 20). D and E . A graph of a ROI value ( D ) indicating tumor progression between week 3 (start of antibody treatment) and week 5 (end of antibody treatment) along with representative IVIS images for each treatment group ( E ) from week 3 to week 5 ( n = 20). F . Images of dissected PDAC orthotopic tumors from each antibody treatment group. G . Graph showing the average tumor weight for each antibody treatment group. H . Immunohistochemistry analysis of Ki-67 and CD31 in orthotopic tumors. Representative images are shown on the left panels, and their relative signal was presented in the graphs on right. Scale bar: 200 μm (H&E and Ki-67 staining) and 50 μm (CD31 staining) ( n = 20). I . Western blot analysis of CD31, Gal 3BP, and VEGFA expression levels in harvested tumors from each group. Graphs on right presents densitometry results for VEGFA or CD31 normalized by b-actin. * p < 0.05; *** p < 0.001; ns (not significant)

    Article Snippet: The immunoblotting was performed with anti-Gal-3BP antibody (AF2226, R&D systems), anti-VEGFA antibody (ab46154, Abcam), anti-p-EGFR antibody (3777, Cell Signaling Technology), anti-EGFR antibody (4267, Cell Signaling Technology), anti-p-AKT antibody (9271, Cell Signaling Technology), anti-AKT antibody (9272, Cell Signaling Technology), anti-p-STAT3 antibody (9145, Cell Signaling Technology), anti-STAT3 antibody (4904, Cell Signaling Technology), anti-β-actin antibody (Santa Cruz Biotechnology), anti-VAMP5 antibody (ab216044, Abcam), and anti-CD31 antibody (77699, Cell Signaling Technology).

    Techniques: In Vivo, Imaging, Luciferase, Expressing, Immunohistochemistry, Staining, Western Blot

    Engineered anti-Gal-3BP antibodies abrogate PDAC metastasis in vivo. A . Schematic diagram of the PDAC lung metastasis experiment using a tail-vein injection of BxPC3 PDAC cells along with the treatment schedule of #13 − 7 ( n = 6), #132 ( n = 6), and control IgG ( n = 8). B . Body weight of each treatment group during the experiment period ( n = 20). C and D . Images of lungs ( C ) and their weight ( D ) at the endpoint from each treatment group. E and F . Metastasis index ( E ) or PanCK-positive area ( F ) measured by immunohistochemistry of the lungs from each treatment group. Representative images are shown on left panels, and the graphs on right show data analysis. Scale bar: 200 μm. G . Graphical summary of the study, indicating the role of extracellular Gal-3BP in promoting angiogenesis by upregulating VEGFA secretion from cancer cells (autocrine effect) or directly interacting with VAMP5 on HUVEC (paracrine effect). * p < 0.05; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Journal: Cell Communication and Signaling : CCS

    Article Title: The Galectin-3-binding protein promotes angiogenesis in pancreatic cancer via simultaneous upregulation of VEGFA and direct HUVEC activation mediated by and VAMP5-STAT3

    doi: 10.1186/s12964-026-02801-7

    Figure Lengend Snippet: Engineered anti-Gal-3BP antibodies abrogate PDAC metastasis in vivo. A . Schematic diagram of the PDAC lung metastasis experiment using a tail-vein injection of BxPC3 PDAC cells along with the treatment schedule of #13 − 7 ( n = 6), #132 ( n = 6), and control IgG ( n = 8). B . Body weight of each treatment group during the experiment period ( n = 20). C and D . Images of lungs ( C ) and their weight ( D ) at the endpoint from each treatment group. E and F . Metastasis index ( E ) or PanCK-positive area ( F ) measured by immunohistochemistry of the lungs from each treatment group. Representative images are shown on left panels, and the graphs on right show data analysis. Scale bar: 200 μm. G . Graphical summary of the study, indicating the role of extracellular Gal-3BP in promoting angiogenesis by upregulating VEGFA secretion from cancer cells (autocrine effect) or directly interacting with VAMP5 on HUVEC (paracrine effect). * p < 0.05; *** p < 0.001; **** p < 0.0001; ns (not significant)

    Article Snippet: The immunoblotting was performed with anti-Gal-3BP antibody (AF2226, R&D systems), anti-VEGFA antibody (ab46154, Abcam), anti-p-EGFR antibody (3777, Cell Signaling Technology), anti-EGFR antibody (4267, Cell Signaling Technology), anti-p-AKT antibody (9271, Cell Signaling Technology), anti-AKT antibody (9272, Cell Signaling Technology), anti-p-STAT3 antibody (9145, Cell Signaling Technology), anti-STAT3 antibody (4904, Cell Signaling Technology), anti-β-actin antibody (Santa Cruz Biotechnology), anti-VAMP5 antibody (ab216044, Abcam), and anti-CD31 antibody (77699, Cell Signaling Technology).

    Techniques: In Vivo, Injection, Control, Immunohistochemistry