Journal: Frontiers in Oncology

Article Title: Establishment, characterization, and drug screening of low-passage patient individual non-small cell lung cancer in vitro models including the rare pleomorphic subentity

doi: 10.3389/fonc.2023.1089681

Figure Lengend Snippet: Antibodies used for flow cytometry.

Article Snippet: LYPD3 , APC , Sino Biological Europe GmbH, Düsseldorf, Germany , 11836-H08H.

Techniques: Cytometry

Journal: Frontiers in Oncology

Article Title: Establishment, characterization, and drug screening of low-passage patient individual non-small cell lung cancer in vitro models including the rare pleomorphic subentity

doi: 10.3389/fonc.2023.1089681

Figure Lengend Snippet: Flow cytometry. Histogram overlays of unstained controls (dotted lines for all three cell lines) and measurements for HROLu55 (green), HROLu22 (blue), and HROBML01 (red) for the epitopes CD326, PD-L1, EGFR, CD26, LYPD3, DSG3, CCD59, CD27, and CD90 are shown.

Article Snippet: LYPD3 , APC , Sino Biological Europe GmbH, Düsseldorf, Germany , 11836-H08H.

Techniques: Flow Cytometry

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Differential expression of LYPD3 in tumor and normal tissues in a pan-cancer cohort. A TCGA database. B TCGA-GTEx database. C CPTAC database

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Quantitative Proteomics

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Single-cell expression analysis of LYPD3 in NSCLC based on scRNA-seq. A , B The identified clusters and cell types in NSCLC tissues based on the GSE148071 dataset. C , D The expression levels of LYPD3 in the identified cell types in NSCLC tissues based on the GSE148071 dataset

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Expressing

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Spatial transcriptomics analysis of LYPD3 in LUAD. A Localization of all cells after spatial transcriptome deconvolution. B Single-gene spatial transcriptome localization. C Spearman correlation of gene expression with microenvironmental components at spatial resolution

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Gene Expression

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Forest plot of Cox regression analysis presenting the association between LYPD3 gene expression and OS, DSS, DFS, and PFS. HR greater than 1 indicate that expression of the gene is associated with an increased risk of death, whereas HR less than 1 indicate an association with a decreased risk of death

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Gene Expression, Expressing

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: ROC analysis. A LYPD3 showed significant diagnostic efficacy in pan-cancer. B ROC analysis showed that LYPD3 was able to efficiently distinguish tumor tissues from normal tissues in LUSC, CESC, PCPG, KICH, KIRP, LUAD, KIRC, and CHOL

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Diagnostic Assay

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Multi-algorithm calculation of the correlation between LYPD3 expression and immune infiltrating cells in pan-cancer. The horizontal coordinates are the different immune infiltrating cells analyzed by different algorithms, the vertical coordinates are the different tumors, and the color of each square is red/blue to indicate positive/negative correlation, with the darker color representing the more significant correlation

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Expressing

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Correlation of LYPD3 expression with immune genes (chemokine, chemokine receptor, immunoinhibitor, immunostimulator, and MHC)

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Expressing

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: LYPD3 and genetic variants. A Mutation frequency map of LYPD3 in pan-cancer. B Mutation analysis of LYPD3 with multiple classical oncogenic signaling pathways in pan-cancer. C Waterfall plots showing the mutation distribution of LYPD3 in pan-cancer and the classification of SNV types

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Mutagenesis, Protein-Protein interactions

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Drug sensitivity analysis. A GDSC database. B CTRP database. C Correlation between LYPD3 expression and IC50 values of antitumor drugs (top 30). D Analyzing small molecule drugs that might reverse the biological effects caused by LYPD3 dysregulation in pan-cancer in the Connectivity Map (CMap) database

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Expressing

Journal: Mammalian Genome

Article Title: Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments

doi: 10.1007/s00335-026-10198-4

Figure Lengend Snippet: Knockdown of LYPD3 inhibits lung cancer cell invasion and metastasis and promotes apoptosis. A , B Transfection efficiency detection. C Flow cytometry detection of apoptosis. D , E Transwell detection of cell invasion and migration. F Western blot was used to detect molecular markers related to apoptosis, invasion and metastasis

Article Snippet: Primary antibodies were LYPD3 (Huabio, HA721332, 1:1000, China) and GAPDH (Absin, Abs132004, 1:5000, China).

Techniques: Knockdown, Transfection, Flow Cytometry, Migration, Western Blot

Journal: International Journal of Medical Sciences

Article Title: Multi-omics and single-cell analysis reveals machine learning-based pyrimidine metabolism-related signature in the prognosis of patients with lung adenocarcinoma

doi: 10.7150/ijms.107694

Figure Lengend Snippet: Experimental validation of LYPD3 in LUAD cell lines. (A-D) RT-qPCR and Western blot were applied to assess the expression of LYPD3 in PC-9 and NCI-H1975. (E-F) CCK8 assay was used to determine the proliferation of PC-9 and NCI-H1975 transfected with si-LYPD3 or pcDNA3.1-CMV-LYPD3. (G-H) Wound-healing assay was utilized to analyze the migratory activity of PC-9 and NCI-H1975 with the overexpression or knockdown of LYPD3. (I-J) Transwell migration assay was used to evaluate the migration of transfected A549 and PC9 cells. (K-L) Transwell invasion assay was used to detect invasion after transfection with si-LYPD3 or pcDNA3.1- CMV-LYPD3 . Data are presented as mean ± 95% confidence interval [CI]. **P < 0.01; ***P < 0.001.

Article Snippet: The plasmid pcDNA3.1-CMV-LYPD3 and an empty vector were purchased from GeneChem (Shanghai, China).

Techniques: Quantitative RT-PCR, Western Blot, Expressing, CCK-8 Assay, Transfection, Wound Healing Assay, Activity Assay, Over Expression, Knockdown, Transwell Migration Assay, Migration, Transwell Invasion Assay

Journal: Antibodies

Article Title: A High-Affinity Monoclonal Antibody Against the Pancreatic Ductal Adenocarcinoma Target, Anterior Gradient-2 (AGR2/PDIA17)

doi: 10.3390/antib13040101

Figure Lengend Snippet: High-affinity anti-AGR2 MAbs inhibit AGR2-mediated cell adhesion, migration, and binding to LYPD3. ( A ) ELISA plates were coated with BSA or AGR2, and PANC-1 cells were allowed to adhere for 1 h in the absence (“0”) or presence of the indicated anti-AGR2 MAbs. Non-adherent cells were washed away, and adherent cells were quantified using the Cell Titer-Glo assay system. Cell adhesion data are shown. ( B ) KPC cells were used in migration assays using a Boyden chamber design with 8 μm porous membrane. (Left) KPC cells were added to the top chamber in the presence or absence of rAGR2 (500 nM) and allowed to migrate toward a chemoattractant gradient composed of KPC-conditioned media (CM) for 6 h. Quantification of migrated cells is shown. (Right) KPC or KPC cells with AGR2 overexpression were added to the top chamber and allowed to migrate toward a chemoattractant gradient composed of KPC-conditioned media (CM) for 6 h. Quantification of migrated cells is shown. Statistical significance was determined using a Student’s t -test (n = 3). ( C ) LYPD3 binding to AGR2-coated or BSA-coated (control) plates was analyzed. ELISA data are shown. ( D ) LYPD3 binding to AGR2-coated plates was measured in the presence of the indicated concentrations of the affinity-mature anti-AGR2 MAb S31R/A53Y. ELISA data are shown.

Article Snippet: Subcloning: Genes for AGR2, LYPD3, scFvs, and monoclonal antibodies were codon optimized for either E. coli or human cells by GenScript Biotech (Piscataway, NJ, USA.

Techniques: Migration, Binding Assay, Enzyme-linked Immunosorbent Assay, Glo Assay, Membrane, Over Expression, Control

Journal: Frontiers in Drug Discovery

Article Title: Targeting a cancer-specific LYPD3 glycoform for tumor therapy

doi: 10.3389/fddsv.2023.1298916

Figure Lengend Snippet: FIGURE 1 Glycosylation-dependent recognition of LYPD3 by GT-002. (A) LYPD3 proteins carrying truncated O-glycans (w/O-glyc) or no O-glycans (w/o O-glyc) were coated onto ELISA plates and tested for binding of 250 ng/mL GT-002 and Lupartumab, both expressed with human IgG1 backbones. (B) Dose-response curves (exemplary experiment measured in duplicates) of GT-002 (black circles) and Lupartumab (white squares) were determined by ELISA on LYPD3 carrying truncated O-glycans. (C) Flow cytometric analysis of cells overexpressing LYPD3 carrying truncated O-glycans (LYPD3-F9), no O-glycans (LYPD3-HEK-OglycKO) or low endogenous LYPD3 levels (F9) using 10 μg/mL GT-002. Lupartumab (1 μg/mL) and aTF mAb (0.1 μg/mL) served as expression controls. Signal/noise ratios were calculated as quotient of MFI (mean fluorescence intensity) values of mAb and appropriate isotype control staining. Error bars indicate standard deviation (SD) of duplicates.

Article Snippet: Protein-specific anti-LYPD3 polyclonal antibodies HPA041529 (Atlas Antibodies) or AF5428 (R&D Systems) served as positive control.

Techniques: Glycoproteomics, Enzyme-linked Immunosorbent Assay, Binding Assay, Expressing, Control, Staining, Standard Deviation

Journal: Frontiers in Drug Discovery

Article Title: Targeting a cancer-specific LYPD3 glycoform for tumor therapy

doi: 10.3389/fddsv.2023.1298916

Figure Lengend Snippet: FIGURE 2 Fine-specificity of GT-002 in ELISA. (A) O-glycan profiling of LYPD3 glycoforms used for binding studies. Monosaccharide symbols follow the CFG recommended symbol nomenclature (Varki et al., 2015). Open circles: unspecified hexose; peaks marked with an asterisk are methodically-derived peeling products. (B) Recognition of indicated LYPD3 glycoforms by GT-002 (12.5 ng/mL) was analyzed by ELISA. LYPD3 purified from different cell lines was treated with neuraminidase (de-sialyl.) or with galactosidase (de-gal.), where indicated. Lupartumab (10 ng/mL), aTF mAb (1 μg/mL) and aTn mAb (5 μg/mL) served as controls. (C) Binding of GT-002 (250 ng/mL) to irrelevant TF-carrying glycoproteins produced in F9 cells was tested by ELISA. Lupartumab (250 ng/mL) and aTF mAb (1 μg/mL) served as controls. Error bars indicate standard deviation (SD) of duplicates.

Article Snippet: Protein-specific anti-LYPD3 polyclonal antibodies HPA041529 (Atlas Antibodies) or AF5428 (R&D Systems) served as positive control.

Techniques: Enzyme-linked Immunosorbent Assay, Glycoproteomics, Binding Assay, Derivative Assay, Produced, Standard Deviation

Journal: Frontiers in Drug Discovery

Article Title: Targeting a cancer-specific LYPD3 glycoform for tumor therapy

doi: 10.3389/fddsv.2023.1298916

Figure Lengend Snippet: FIGURE 3 Binding of GT-002 to tumor cells. (A) LYPD3-positive (CaOV-3 and ZR-75-1) and -negative (MDA-MB-231) human tumor cell lines were treated with neuraminidase (w/neu) or not treated (w/o neu) and stained with 10 μg/mL GT-002. Lupartumab (1 μg/mL) and aTF (10 μg/mL) served as expression controls. Signal to noise ratios were calculated as the quotient of MFI values of mAb and appropriate isotype control stainings. (B) Immunohistochemical staining of a human tumor CDX section derived from the CaOV-3 cell line with 10 μg/mL GT-002. Scale bars indicate 50 µm. Error bars indicate SD of duplicates.

Article Snippet: Protein-specific anti-LYPD3 polyclonal antibodies HPA041529 (Atlas Antibodies) or AF5428 (R&D Systems) served as positive control.

Techniques: Binding Assay, Staining, Expressing, Control, Immunohistochemical staining, Derivative Assay

Journal: Frontiers in Drug Discovery

Article Title: Targeting a cancer-specific LYPD3 glycoform for tumor therapy

doi: 10.3389/fddsv.2023.1298916

Figure Lengend Snippet: FIGURE 6 Internalization of GT-002 into tumor cell line. GT-002 (black circles), Lupartumab (white squares) or an isotype control (grey circle) where labeled with anti-human Fabfluor-pH antibody labeling dye and then added to LYPD3-F9 cells (A) or F9 cells (B). Internalization, measured as red fluorescence induced by low acidic pH after antibody uptake, was monitored for 24 h. Percentage of lysosomal routing was expressed as the Red Area (Red positive cells)/Phase Area (Total cell confluency). Error bars indicate SD of duplicates.

Article Snippet: Protein-specific anti-LYPD3 polyclonal antibodies HPA041529 (Atlas Antibodies) or AF5428 (R&D Systems) served as positive control.

Techniques: Control, Labeling, Antibody Labeling