bxpc3 cell lines  (ATCC)

Journal: PLOS One

Article Title: Statin-dye conjugates for selective targeting of KRAS mutant cancer cells

doi: 10.1371/journal.pone.0340189

Figure Lengend Snippet: Simvastatin-Cy5.5, pravastatin-Cy5.5, and free Cy5.5 uptake was measured by fluorescence (red) in (a) Panc1 ( KRAS MUT ) and BxPC3 ( KRAS WT ) and (b) HPDE KRAS MUT (HPDE i KRAS with doxycycline) and HPDE KRAS WT (HPDE i KRAS without doxycycline). The scale bars indicate 10 μm. The cell nuclei were stained with DAPI (blue). Quantitative measurements of the cellular uptake of the statin-dye conjugates are presented relative fluorescence intensity per cell count. Bars indicate Mean ± S.E. (n ≥ 3). Statistically significant differences are represented as * for p < 0.05, *** for p < 0.001, and **** for p < 0.0001.

Article Snippet: Panc1 (CRL-1469) and BxPC3 (CRL-1687) cell lines were purchased from the American Type Culture Collection.

Techniques: Fluorescence, Staining, Cell Counting

Journal: Glycobiology

Article Title: Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells

doi: 10.1093/glycob/cwaf066

Figure Lengend Snippet: Measuring drug binding interactions on whole single cells using SPRM. A) Schematic of SPRM setup. SPRM light source induces SPR on gold chip containing adhered BXPC3 pancreatic cancer cells. Plasmonic resonance condition, which is extremely sensitive to ligand binding, is recorded by SPRM detector. Anti-ErbB1–3 antibodies, peptides, or small molecules are delivered via an automated microfluidics system though a transparent flow cell that supports both precision sample delivery and bright field optical imaging. B) Bright field image of BXPC3 cells and its corresponding SPRM image. Red squares indicate binding activity. C) Simultaneous cell binding responses from kinetic titration injection series. D) Representative small sampling of anti-ErbB2 SPR sensorgrams with binding responses shown closely fitting the heterogeneous 1:2 kinetic binding model (in red). Arrows indicate the ROI location on the cell where each sensorgram is derived. E) Representative anti-ErbB2 antibody data displaying bivalent interactions. The calculated ka and kd rates from every binding interaction series are collected to form an iso-affinity scatter plot, displaying the heterogeneity of the binding interaction. Gaussian distributions are applied to the histograms along each axis and the diagonal to extract the mean and standard deviation for the ka, kd, and KD values.

Article Snippet: BxPC3 cell line (ATCC) was kindly provided by Dr. Shaopeng Wang’s lab of the Biodesign Institute at Arizona State University.

Techniques: Binding Assay, Ligand Binding Assay, Optical Imaging, Activity Assay, Titration, Injection, Sampling, Derivative Assay, Standard Deviation

Journal: Glycobiology

Article Title: Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells

doi: 10.1093/glycob/cwaf066

Figure Lengend Snippet: Quantification of ErbB antibody binding on the surface of BXPC3 cells. A) Anti-HER1 (cetuximab) binding on the surface of HER1 positive BXPC3 cells. B) Anti-HER2 (Herceptin) binding on the surface of HER2 positive BXPC3 cells. C) Anti-HER3 binding on the surface of HER3 positive BXPC3 cells. Red squares on SPR images indicate areas of detected binding activity, which overlap well with the cells, indicating high cell specificity. D) Quantification for relative ErbB receptor expression levels on BXPC3 cells based upon fluorescence analysis. Fluorescence was collected on the same sensor chip immediately after SPRM analysis. Average fluorescence intensity for each receptor interaction was normalized by the sum total of all three ErbB receptors in BXPC3 cells. **** indicates statically significant differences between HER1–3 receptors ( P < 0.0001). Statistical significance determined using one-way ANOVA with Turkey posthoc test. Error bars represent standard deviation.

Article Snippet: BxPC3 cell line (ATCC) was kindly provided by Dr. Shaopeng Wang’s lab of the Biodesign Institute at Arizona State University.

Techniques: Binding Assay, Activity Assay, Expressing, Fluorescence, Standard Deviation

Journal: Glycobiology

Article Title: Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells

doi: 10.1093/glycob/cwaf066

Figure Lengend Snippet: Cetuximab (anti-HER1) binding kinetics on native and deglycosylated BXPC3 pancreatic cancer cells. A) Iso-affinity scatter plot extracted from millions of responsive ROIs for Cetuximab binding on native control BXPC3 cells. Two predominate binding modes ( a & b ) for the bivalent interaction are observed, showing similar on-rates but dissimilar off-rates. Mode ( a ) designates the double-arm avidity interaction and mode ( b ) designates the single-arm affinity interaction. B) KD histogram extracted from iso-affinity scatter plot taken along the diagonal axis kd/ka with gaussian distribution fitted to statistically analyze the kinetic interaction of Cetuximab on native BXPC3 cells. C) Iso-affinity scatter plot extracted from millions of responsive ROIs for Cetuximab binding on deglycosylated (PNGaseF treated) BXPC3 cells. Two predominate binding modes ( a & b ) for the bivalent interaction are observed, however with much greater affinity due to faster on-rates. D) KD histogram extracted from iso-affinity scatter plot with gaussian distribution fitted to statistically analyze the kinetic interaction of Cetuximab on deglycosylated BXPC3 cells. Representative data from a total of four different experiments.

Article Snippet: BxPC3 cell line (ATCC) was kindly provided by Dr. Shaopeng Wang’s lab of the Biodesign Institute at Arizona State University.

Techniques: Binding Assay, Control

Journal: Glycobiology

Article Title: Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells

doi: 10.1093/glycob/cwaf066

Figure Lengend Snippet: Herceptin (anti-HER2) binding kinetics on native and deglycosylated BXPC3 pancreatic cancer cells. A) Iso-affinity scatter plot extracted from millions of responsive ROIs showing Herceptin binding heterogeneity. Two predominant binding modes ( a & b ) for the bivalent interaction are observed, showing similar on-rates but dissimilar off-rates. Mode ( a ) designates the double-arm avidity interaction and mode ( b ) designates the single-arm affinity interaction. B) KD histogram extracted from iso-affinity scatter plot taken along the diagonal axis kd/ka with fitted gaussian distribution to statistically analyze the kinetic interaction of Herceptin on BXPC3 cells. C) Iso-affinity scatter plot extracted from millions of responsive ROIs for Herceptin binding on deglycosylated (PNGaseF treated) BXPC3 cells. Two predominate binding modes ( a & b ) for the bivalent interaction are observed, showing negligible differences from the native glycosylated state. D) KD histogram extracted from iso-affinity scatter plot taken along the diagonal axis kd/ka with gaussian distribution fitted to statistically analyze the kinetic interaction of Herceptin on deglycosylated BXPC3 cells. Representative data from a total of three different experiments.

Article Snippet: BxPC3 cell line (ATCC) was kindly provided by Dr. Shaopeng Wang’s lab of the Biodesign Institute at Arizona State University.

Techniques: Binding Assay

Journal: Glycobiology

Article Title: Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells

doi: 10.1093/glycob/cwaf066

Figure Lengend Snippet: Anti-HER3 binding kinetics on native and deglycosylated BXPC3 pancreatic cancer cells. A) Iso-affinity scatter plot extracted from millions of responsive ROIs for anti-HER3 binding on native control BXPC3 cells. Two predominant binding modes ( a & b ) for the bivalent interaction are observed, showing similar on-rates but dissimilar off-rates. Mode (a) designates the double-arm avidity interaction and mode (b) designates the single-arm affinity interaction. B) KD histogram extracted from iso-affinity scatter plot taken along the diagonal axis kd/ka with gaussian distribution fitted to statistically analyze the kinetic interaction of anti-HER3 on BXPC3 cells. C) Iso-affinity scatter plot extracted from millions of responsive ROIs for anti-HER3 binding on deglycosylated (PNGaseF treated) BXPC3 cells. Two predominant modes for the bivalent interaction are observed, however with much greater affinity due to faster on-rates. D) KD histogram extracted from iso-affinity scatter plot taken along the diagonal axis kd/ka with gaussian distribution fitted to statistically analyze the kinetic interaction of anti-HER3 on deglycosylated BXPC3 cells. Representative data from a total of three different experiments.

Article Snippet: BxPC3 cell line (ATCC) was kindly provided by Dr. Shaopeng Wang’s lab of the Biodesign Institute at Arizona State University.

Techniques: Binding Assay, Control

Journal: Glycobiology

Article Title: Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells

doi: 10.1093/glycob/cwaf066

Figure Lengend Snippet: Affinity-avidity analysis of anti-HER1–3 antibodies. A) Percent of total binding events observed for avidity and affinity among HER1, HER2, and HER3. The percentage of interactions attributed to avidity or affinity binding modes on BXPC3 cells are presented. The total number of binding events were determined, then the percent total was calculated by normalizing to the sum of the three receptor total binding events. Data were pooled from three different experiments. The inset schematic shows avidity and affinity interactions. The affinity interaction occurs by a single-arm attachment scenario. The avidity interaction occurs by additional attachment of the second arm, resulting in a longer more stable interaction. B) Increasing relationship between the occurrence of avidity and receptor density. Relative expression levels obtained by fluorescence were plotted on the x-axis, and percent of total binding events observed for avidity were plotted on the y-axis. *indicates statically significant differences between avidity and affinity ( P < 0.0001). Statistical significance determined using one-way ANOVA with Turkey posthoc test. Error bars represent standard deviation.

Article Snippet: BxPC3 cell line (ATCC) was kindly provided by Dr. Shaopeng Wang’s lab of the Biodesign Institute at Arizona State University.

Techniques: Binding Assay, Expressing, Fluorescence, Standard Deviation

Journal: bioRxiv

Article Title: Phenotypic AI-based design of cell-specific small molecule cytotoxics

doi: 10.1101/2025.10.15.682546

Figure Lengend Snippet: Both for the exercises BXPC3 vs CAPAN2 and BXPC3 vs HEK293 we found this substructure to be extremely prevalent in the proposed designs, thus the generative cycle was run again penalising the molecules containing this motif.

Article Snippet: We acquired the pancreatic cancer cell lines BXPC3, CAPAN2, HPAFII, PANC10.05, and SW1990 from the American Type Culture Collection (ATCC), and CFPAC1 and AsPC-1 lines were kindly provided by Dr Cristina Mayor-Ruiz (IRB Barcelona).

Techniques: