human her2 protein  (MedChemExpress)

Journal: Cell Reports Medicine

Article Title: Synergically enhanced anti-tumor immunity of in vivo panCAR by circRNA vaccine boosting

doi: 10.1016/j.xcrm.2025.102250

Figure Lengend Snippet: CircRNA CAR efficiently expressed CAR proteins and mediated remarkable tumor killing (A) Schematic representation of circRNA Anti-HER2-CAR circularization via group I intron autocatalysis. (B and C) Detecting the expression of CAR proteins in HEK293T cells after circRNA Anti-HER2-CAR transfection via western blot (B) and flow cytometry (C). (D) Comparative analysis of CAR expression levels from circRNA Anti-HER2-CAR , 1mΨ-mRNA Anti-HER2-CAR , and unmodified mRNA Anti-HER2-CAR in HEK293T cells. (E–G) Optimization of circRNA Anti-HER2-CAR encoding CAR in Jurkat (E), THP-1 (F), and J774A.1 (G). (H) Detection of CAR expression in primary T cells using flow cytometry. (I–K) Cytotoxic effects of primary T cells transfected with circRNA Anti-HER2-CAR on SK-OV-3 (I), B16F10-HER2 (J), and 4T1-HER2 (K) tumor cells. (L–N) Cytotoxic effects of Jurkat cells transfected with circRNA Anti-HER2-CAR on SK-OV-3 (L), B16F10-HER2 (M), and 4T1-HER2 (N) tumor cells. (O–Q) Cytotoxic effects of THP-1 cells transfected with circRNA Anti-HER2-CAR on SK-OV-3 (O), B16F10-HER2 (P), and 4T1-HER2 (Q) tumor cells. In (C)–(Q), data were presented as mean ± SEM ( n = 3). An unpaired two-sided Student’s t test was performed for comparison; ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001; ns, not significant. See also ; .

Article Snippet: The 96-well plates (Corning, #9018) were coated with recombinant human HER2 protein (MCE, #HY- P70254 ) diluted in coating solution (Bioss, #C04-01001) at 4°C overnight.

Techniques: Expressing, Transfection, Western Blot, Flow Cytometry, Comparison

Journal: Cell Reports Medicine

Article Title: Synergically enhanced anti-tumor immunity of in vivo panCAR by circRNA vaccine boosting

doi: 10.1016/j.xcrm.2025.102250

Figure Lengend Snippet: Macrophages exhibited efficient tumor phagocytosis and pro-inflammatory polarization induced by circRNA CAR (A and B) Phagocytosis of THP-1 cells transfected with circRNA Anti-HER2-CAR against SK-OV-3 (A) and MC38-HER2 (B) cells. (C) Phagocytosis of J774A.1 cells transfected with circRNA Anti-HER2-CAR against CT26-HER2 cells. (D and E) Effects of circRNA Anti-HER2-CAR on iNOS (D) and CD206 (E) expression in J774A.1. (F and G) Effects of circRNA Anti-HER2-CAR on iNOS (F) and CD206 (G) expression in THP-1 cells. (H) Volcano plot illustrating differentially expressed genes in THP-1 cells. (I) Heatmap depicting gene expression patterns in THP-1 cells ( n = 2). (J) Bubble chart of relevant biological processes via Gene Ontology (GO) analysis ( n = 2). Bubble size represents the number of genes. In (A)–(G), data were presented as mean ± SEM ( n = 3). An unpaired two-sided Student’s t test was conducted for comparison; ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001; ns, not significant. See also .

Article Snippet: The 96-well plates (Corning, #9018) were coated with recombinant human HER2 protein (MCE, #HY- P70254 ) diluted in coating solution (Bioss, #C04-01001) at 4°C overnight.

Techniques: Transfection, Expressing, Gene Expression, Comparison

Journal: Cell Reports Medicine

Article Title: Synergically enhanced anti-tumor immunity of in vivo panCAR by circRNA vaccine boosting

doi: 10.1016/j.xcrm.2025.102250

Figure Lengend Snippet: Screening for immunocyte-tropic LNPs that efficiently delivered circRNAs into immune cells in mice (A) Schematic representation of the LNP-circRNA complex. (B and C) The size distribution (B) and zeta potential (C) of the LNP-circRNA Luciferase complex. (D and E) Bioluminescence imaging in vivo (D) or ex vivo (E) of BALB/c mice intravenously injected with PBS or LNP-circRNA Luciferase . (F and G) Bioluminescence imaging in vivo (F) or ex vivo (G) of BALB/c mice intravenously injected with PBS or SORT-circRNA Luciferase . (H) Evaluation of targeting efficiency of SORT-circRNA Cre in the spleen of reporter mice. (I) Detection of anti-HER2-CAR expression at different time points in various immune cells of mouse spleen. In (H) and (I), data were presented as mean ± SEM, an unpaired two-sided Student’s t test was performed for comparison; ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001; ns, not significant. See also .

Article Snippet: The 96-well plates (Corning, #9018) were coated with recombinant human HER2 protein (MCE, #HY- P70254 ) diluted in coating solution (Bioss, #C04-01001) at 4°C overnight.

Techniques: Zeta Potential Analyzer, Luciferase, Imaging, In Vivo, Ex Vivo, Injection, Expressing, Comparison

Journal: Cell Reports Medicine

Article Title: Synergically enhanced anti-tumor immunity of in vivo panCAR by circRNA vaccine boosting

doi: 10.1016/j.xcrm.2025.102250

Figure Lengend Snippet: CircRNA CAR efficiently inhibited tumor growth and improved survival time in mice (A) Schematic illustration of intravenous PBS, LNP-circRNA Ctrl , or SORT-circRNA Anti-HER2-CAR treatment in the CT26-HER2 tumor model. (B) Tumor growth curves for CT26-HER2 tumor-bearing mice treated as indicated in (A). (C) Schematic illustration of intratumoral PBS, LNP-circRNA Ctrl , or LNP-circRNA Anti-HER2-CAR treatment in the CT26-HER2 tumor model. (D and E) Tumor growth curves (D) and survival curves (E) of CT26-HER2 tumor-bearing mice treated as indicated in (C). (F) In vivo bioluminescence imaging of CT26-HER2 tumor-bearing mice treated as indicated in (C). (G) The quantified signal intensity of bioluminescence imaging in (F). (H) Schematic illustration of intratumoral PBS, LNP-circRNA Ctrl , or LNP-circRNA Anti-HER2-CAR treatment in the 4T1-HER2 tumor model. (I) Tumor growth curves of 4T1-HER2 tumor-bearing mice treated as indicated in (H). (J) Tumor growth curves of individual 4T1-HER2 tumor-bearing mice treated as indicated in (H). (K) Schematic illustration of intratumoral PBS, LNP-circRNA Ctrl , or LNP-circRNA CAR treatment in the MC38-HER2 tumor model. (L and M) Tumor growth curves (L) and survival curves (M) of MC38-HER2 tumor-bearing mice treated as indicated in (K). In (B), (D), (I), and (L), data were represented as the mean ± SEM, the tumor growth curves were calculated by two-way ANOVA analysis ( n = 6). In (E) and (M), data were represented as the mean ± SEM, the survival curves were calculated by Kaplan-Meier simple survival analysis ( n = 6). In (G), data were represented as the mean ± SEM, an unpaired two-sided Student’s t test was conducted for comparison. ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001. See also .

Article Snippet: The 96-well plates (Corning, #9018) were coated with recombinant human HER2 protein (MCE, #HY- P70254 ) diluted in coating solution (Bioss, #C04-01001) at 4°C overnight.

Techniques: In Vivo, Imaging, Comparison

Journal: Cell Reports Medicine

Article Title: Synergically enhanced anti-tumor immunity of in vivo panCAR by circRNA vaccine boosting

doi: 10.1016/j.xcrm.2025.102250

Figure Lengend Snippet: In vivo panCAR reshaped the tumor microenvironment to a pro-inflammatory state (A) Changes in the proportion of immune cells of spleen via flow cytometry. CD8 + T cells, CD8 + Tem cells, CD8 + Tcm cells, or CD4 + T cells were gated from CD45 + cell population, and Treg cells were gated from CD4 + T cell population. (B) Flow cytometric analysis of changes in the proportion of infiltrating immune cells in tumors. CD8 + T cells, CD4 + T cells, or MHC II + macrophages were gated from CD45 + cell population, and Treg cells were gated from CD4 + T cell population. (C and D) H&E staining (C) or IHC staining (D) of tumor tissue sections obtained from CT26-HER2 tumor-bearing mice after PBS, SORT-LNP-circRNA Ctrl , or SORT-LNP-circRNA Anti-HER2-CAR treatment. The integrated density of IHC staining was quantified using ImageJ. (E) Heatmap of gene expression patterns of immune cells extracted from tumor tissues ( n = 2). (F) Bubble chart of relevant biological processes through GO analysis ( n = 2). The size of the bubbles represented the number of genes. (G) Gene set enrichment analysis (GSEA) showing enriched pathways in immune cells extracted from tumor tissues ( n = 2). In (A), (B), and (D), data were represented as the mean ± SEM; an unpaired two-sided Student’s t test was conducted for comparison; ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001; ns, not significant. Each symbol represents an individual mouse. See also and .

Article Snippet: The 96-well plates (Corning, #9018) were coated with recombinant human HER2 protein (MCE, #HY- P70254 ) diluted in coating solution (Bioss, #C04-01001) at 4°C overnight.

Techniques: In Vivo, Flow Cytometry, Staining, Immunohistochemistry, Gene Expression, Comparison

Journal: Cell Reports Medicine

Article Title: Synergically enhanced anti-tumor immunity of in vivo panCAR by circRNA vaccine boosting

doi: 10.1016/j.xcrm.2025.102250

Figure Lengend Snippet: CircRNA vaccine synergistically boosted the anti-tumor activity of in vivo panCAR (A) Schematic illustration of circRNA VAC design. EPM, the endocytosis prevention motif; EABR, the ESCRT- and ALIX-binding region domain. (B) Flow cytometric analysis detecting the translation of circRNA HER2 in HEK293T cells ( n = 3). (C) Electron microscopy showing the vesicles secreted by HEK293T cells transfected with circRNA HER2-EPM-EABR . (D) Measurement of the endpoint titer of HER2-specific IgG with ELISA. (E) Schematic illustration of 4T1-HER2 tumor-bearing mice receiving PBS (intravenously), circRNA CAR (intravenously), circRNA VAC (intramuscularly), or circRNA CAR (intravenously) plus circRNA VAC (intramuscularly) combined therapy ( n = 5). (F) Tumor growth curves of overall mice treated as indicated in (E). (G) Tumor growth curves of individual mouse treated as indicated in (E). (H) Schematic illustration of B16F10-HER2 tumor-bearing mice receiving PBS (intravenously), circRNA CAR (intravenously), circRNA VAC (intramuscularly), or circRNA CAR (intravenously) plus circRNA VAC (intramuscularly) combined therapy ( n = 5). (I) Tumor growth curves of overall mice treated as indicated in (H). (J) Tumor growth curves of individual mouse treated as indicated in (H). (K) Survival curves of B16F10-HER2 tumor-bearing mice treated as indicated in (H). In (B), data were represented as the mean ± SEM; an unpaired two-sided Student’s t test was performed for comparison. In (D), data were represented as the geometric mean ± geometric SD; an unpaired two-sided Student’s t test was performed for comparison. In (F) and (I), data were represented as the mean ± SEM, and the tumor growth curves were calculated by two-way ANOVA analysis. In (K), the survival curves were calculated by Kaplan-Meier simple survival analysis. ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001; ns, not significant. See also ; .

Article Snippet: The 96-well plates (Corning, #9018) were coated with recombinant human HER2 protein (MCE, #HY- P70254 ) diluted in coating solution (Bioss, #C04-01001) at 4°C overnight.

Techniques: Activity Assay, In Vivo, Binding Assay, Electron Microscopy, Transfection, Enzyme-linked Immunosorbent Assay, Comparison

Journal: Cell Reports Medicine

Article Title: Synergically enhanced anti-tumor immunity of in vivo panCAR by circRNA vaccine boosting

doi: 10.1016/j.xcrm.2025.102250

Figure Lengend Snippet: In vivo panCAR enhanced the anti-tumor activity via antibody-mediated cellular cytotoxicity (A) Measurement of HER2-specific IgG, IgG1, IgG2A, IgG2B, or IgG2C-binding antibodies with ELISA ( n = 5 or 6). (B and C) HER2-specific antibodies in (A) mediated cellular cytotoxicity against SK-OV-3 (B) and MC38-HER2 (C) tumor cells in J774A.1. (D and E) HER2-specific antibodies in (A) mediated cellular cytotoxicity against SK-OV-3 (D) and MC38-HER2 (E) tumor cells in RAW 264.7. (F) Tumor growth curves of overall CT26 tumor-bearing mice treated with PBS, in vivo panCAR-VAC, or in vivo panCAR-VAC plus anti-NK1.1 antibodies to deplete NK cells ( n = 5). (G) Tumor growth curves of individual mouse treated as indicated in (F). (H) Survival curves of mice treated as indicated in (F). (I) Tumor growth curves of overall CT26 tumor-bearing mice treated with PBS, in vivo panCAR-VAC, or in vivo panCAR-VAC plus anti-CSF1R antibody to deplete macrophages ( n = 5). (J) Tumor growth curves of individual mouse treated as indicated in (I). (K) Survival curves of mice treated as indicated in (I). (L) The potential mechanism diagram of synergistic in vivo panCAR-VAC immunotherapy. In (A), data are shown as the mean ± SEM; In (B)–(E), data were represented as the mean ± SEM; an unpaired two-sided Student’s t test was performed for comparison. In (F) and (I), tumor growth curves were calculated by two-way ANOVA analysis ( n = 5). In (H) and (K), survival curves were calculated by Kaplan-Meier simple survival analysis ( n = 5). ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001; ns, not significant. See also .

Article Snippet: The 96-well plates (Corning, #9018) were coated with recombinant human HER2 protein (MCE, #HY- P70254 ) diluted in coating solution (Bioss, #C04-01001) at 4°C overnight.

Techniques: In Vivo, Activity Assay, Binding Assay, Enzyme-linked Immunosorbent Assay, Comparison

Journal: The Journal of Biological Chemistry

Article Title: Production of site-specific antibody conjugates using metabolic glycoengineering and novel Fc glycovariants

doi: 10.1016/j.jbc.2024.108005

Figure Lengend Snippet: Fc glycovariants demonstrate potent tumor cell killing upon formulation as antibody-drug conjugates. A , biolayer interferometry studies of the equilibrium binding between immobilized human epidermal growth factor receptor 2 (HER2) and soluble trastuzumab glycovariant antibodies. B , cytotoxicity of single mutant trastuzumab glycovariant antibody-drug conjugates (ADCs) against HER2-expressing SKBR3 human breast cancer cells. DBCO-linked monomethyl auristatin E (MMAE) was used as the drug payload only control. C – E , cytotoxicity of a single and triple mutant trastuzumab glycovariant ADCs against HER2 + SKBR3 ( C ), HER2 + HCC1954 ( D ), or HER2 - MDA-MB-231 ( E ) human breast cancer cells. DBCO-linked MMAE was used as the drug payload only control. Error bars represent standard deviation (n = 4).

Article Snippet: For biolayer interferometry studies using an Octet instrument, biotinylated human interleukin-2 (IL-2), produced via HEK 293F cell secretion, as previously described , human neonatal Fc receptor (FcRn) (Sino Biological), human Fcγ receptor I (FcγRI) (Sino Biological), human FcγRIIa (Sino Biological), and human epidermal growth factor receptor 2 (HER2) (Sino Biological) were immobilized to streptavidin-coated biosensors (Sartorius).

Techniques: Formulation, Binding Assay, Mutagenesis, Expressing, Control, Standard Deviation

Journal: The Journal of Biological Chemistry

Article Title: Production of site-specific antibody conjugates using metabolic glycoengineering and novel Fc glycovariants

doi: 10.1016/j.jbc.2024.108005

Figure Lengend Snippet: Fc glycovariant conjugation to biomaterials enables targeted gene delivery. A , schematic of detection scheme for flow cytometry analysis of azido-modified trastuzumab glycovariants linked to DBCO-coated magnetic microparticles. Antibody conjugation is detected with a fluorescent anti-Fab antibody and target antigen binding is detected using biotinylated HER2 and secondary fluorescent streptavidin staining. Representative flow cytometry plots are shown below. B , cartoon depicting poly(beta-amino ester) (PBAE) nanoparticle encapsulating cyanine-5 (Cy5)-labeled enhanced green fluorescent protein (eGFP)-encoding mRNA conjugated to trastuzumab glycovariant antibodies. C and D , nanoparticle uptake in transfected HER2 + SKBR3 ( C ) and HER2 - MDA-MB-231 ( D ) cells, normalized to the unconjugated control for each concentration. E and F , eGFP expression in transfected SKBR3 ( E ) and MDA-MB-231 ( F ) cells, normalized to the unconjugated control for each concentration. Statistical significance was determined by two-way ANOVA with a Dunnett post hoc test. ∗ p ≤ 0.05, ∗∗ p ≤ 0.01, ∗∗∗ p ≤ 0.001, and ∗∗∗∗ p ≤ 0.0001 (n = 4).

Article Snippet: For biolayer interferometry studies using an Octet instrument, biotinylated human interleukin-2 (IL-2), produced via HEK 293F cell secretion, as previously described , human neonatal Fc receptor (FcRn) (Sino Biological), human Fcγ receptor I (FcγRI) (Sino Biological), human FcγRIIa (Sino Biological), and human epidermal growth factor receptor 2 (HER2) (Sino Biological) were immobilized to streptavidin-coated biosensors (Sartorius).

Techniques: Conjugation Assay, Flow Cytometry, Modification, Binding Assay, Staining, Labeling, Transfection, Control, Concentration Assay, Expressing

Journal: ACS Measurement Science Au

Article Title: Electrochemical Cellulase-Linked ELASA for Rapid Liquid Biopsy Testing of Serum HER-2/ neu

doi: 10.1021/acsmeasuresciau.2c00067

Figure Lengend Snippet: Scheme of e-ELISA (left) and e-ELASA (right) for HER-2/ neu detection. Left panel: Ab-modified MBs capture the protein, further reacting with second biotinylated Ab linked via streptavidin to biotinylated cellulase; Right panel: aptamer-modified MBs capture the protein, further reacting with the second aptamer bioconjugated to cellulase. Cellulase-labeled sandwiches on MBs are applied onto the nitrocellulose-modified graphite electrode, and cellulase digestion of insulating nitrocellulose film results in the electrochemical signal change proportional to the concentration of the protein in a sample.

Article Snippet: Recombinant Human HER-2/ neu protein expressed in HEK293 cells (contains 636 amino acids corresponding to the extracellular domain ECD of HER-2/ErbB2, glycosylated, MW 110 kDa) was from SinoBiological Inc. (Beijing, P.R.

Techniques: Enzyme-linked Immunosorbent Assay, Modification, Labeling, Concentration Assay

Journal: ACS Measurement Science Au

Article Title: Electrochemical Cellulase-Linked ELASA for Rapid Liquid Biopsy Testing of Serum HER-2/ neu

doi: 10.1021/acsmeasuresciau.2c00067

Figure Lengend Snippet: E-ELISA and e-ELASA for HER-2/ neu detection in 0.1 M PBS, pH 7.4, by CC at 0 mV, 10 s pulse. (A) Time and sample volume optimization of e-ELISA (MBs-(Ab)-Ab): (1) 1 h with 1 pM HER-2/ neu in 100 μL, 1 h with secondary Ab and 40 min of electrode digestion; (2) 30 min with HER-2/ neu in 100 μL, 30 min with secondary Ab and 40 min on electrodes; (3) 30 min with HER-2/ neu in 100 μL, 30 min with secondary Ab, and 20 min on electrodes; (4) 30 min with HER-2/ neu in 1 mL, 30 min with secondary Ab, and 20 min on electrodes. (B) Responses of sandwich assays: (green) MBs-(Ab)-Ab, (purple) MB-(aptamer)-aptamer, and (yellow) MBs-(Ab)-aptamer. (C) Selectivity of the e-ELASA using the biotinylated aptamer as a reporter for (purple) HER-2/ neu ; (red) HSA, (green) UpA, and (orange) thrombin. (D): Response of e-ELASA with (purple) biotinylated aptamers reacting with biotinylated cellulase via streptavidin (max. 3 cellulase molecules per sandwich) and (red) aptamer-cellulase bioconjugate (1 cellulase per sandwich). In e-ELASA, a homo-trimer aptamer sequence was used. In MB-(apt)-apt and MB-(Ab)-apt notations, MBs are modified with the receptor in brackets.

Article Snippet: Recombinant Human HER-2/ neu protein expressed in HEK293 cells (contains 636 amino acids corresponding to the extracellular domain ECD of HER-2/ErbB2, glycosylated, MW 110 kDa) was from SinoBiological Inc. (Beijing, P.R.

Techniques: Enzyme-linked Immunosorbent Assay, Sequencing, Modification

Journal: ACS Measurement Science Au

Article Title: Electrochemical Cellulase-Linked ELASA for Rapid Liquid Biopsy Testing of Serum HER-2/ neu

doi: 10.1021/acsmeasuresciau.2c00067

Figure Lengend Snippet: (A) Responses of the MB-(Ab)-aptamer assays with different reporter aptamers, recorded by CC at 0 mV in 0.1 M PBS, pH 7.4: (purple) trimer, (blue) dimer, (orange) monomer-9T, and (yellow) monomer. (B) Responses of e-ELASA to the increasing concentration of HER-2/ neu for the (purple) MB-(trimer)-trimer and (green) MB-(dimer)-dimer and (blue) MB-(dimer)-trimer sandwich. (C) Secondary structures of the trimer, dimer, and monomer aptamer sequences specific for HER-2/ neu predicted by mfold software in 0.154 M NaCl at 25 °C; drawn with VARNAgui 3–9 version. The mfold generated structures are the first approximation of oligonucleotide structures but not their accurate resolution.

Article Snippet: Recombinant Human HER-2/ neu protein expressed in HEK293 cells (contains 636 amino acids corresponding to the extracellular domain ECD of HER-2/ErbB2, glycosylated, MW 110 kDa) was from SinoBiological Inc. (Beijing, P.R.

Techniques: Concentration Assay, Software, Generated

Journal: ACS Measurement Science Au

Article Title: Electrochemical Cellulase-Linked ELASA for Rapid Liquid Biopsy Testing of Serum HER-2/ neu

doi: 10.1021/acsmeasuresciau.2c00067

Figure Lengend Snippet: E-ELASA for HER-2/ neu detection in the human serum performed by CC at 0 V, in 0.1 M PBS pH 7.4. (A) Representative CC responses of nitrocellulose modified Gr electrodes (1) in non-spiked 10% human serum and (2–9) after the exposure to MB-(dimer)-dimer sandwich assembled in 10% human serum containing (2) 0.1 fM, (3) 0.5 fM, (4) 1 fM, (5) 10 fM, (6) 100 fM, (7) 1 pM, (8) 10 pM, and (9) 100 pM HER-2/ neu . (B) Calibration curves for HER-2/ neu detection constructed with CC data for MB-(dimer)-dimer sandwich assembly in (red) PBS and (yellow) 10% human serum. (C) Background signals corresponding to different blank dilutions of human serum (pale orange) 1:10, (light orange) 1:5, (orange) 1:1, (dark orange) undiluted and (brick red) 1fM HER-2/ neu detection in PBS obtained for the MB-(dimer)-dimer sandwich assembly in the absence of HER-2/ neu . Δ Q was calculated as a Q response in the assay performed in the media not-containing the analyte (“blank”) minus Q recorded with the same nitrocellulose-modified electrode prior the “blank” assay.

Article Snippet: Recombinant Human HER-2/ neu protein expressed in HEK293 cells (contains 636 amino acids corresponding to the extracellular domain ECD of HER-2/ErbB2, glycosylated, MW 110 kDa) was from SinoBiological Inc. (Beijing, P.R.

Techniques: Modification, Construct

Journal: ACS Measurement Science Au

Article Title: Electrochemical Cellulase-Linked ELASA for Rapid Liquid Biopsy Testing of Serum HER-2/ neu

doi: 10.1021/acsmeasuresciau.2c00067

Figure Lengend Snippet: Concordance between the ELISA and e-ELASA detection of HER-2/ neu in human serum samples ( N = 28) showing background levels of HER-2/ neu . The dashed red line represents a 100% concordance. Error bars correspond to 3 independent measurements from 3 different electrodes.

Article Snippet: Recombinant Human HER-2/ neu protein expressed in HEK293 cells (contains 636 amino acids corresponding to the extracellular domain ECD of HER-2/ErbB2, glycosylated, MW 110 kDa) was from SinoBiological Inc. (Beijing, P.R.

Techniques: Enzyme-linked Immunosorbent Assay

Journal: bioRxiv

Article Title: A unified peptide array platform for antibody epitope binning, mapping, specificity and predictive off-target binding

doi: 10.1101/2022.06.22.497251

Figure Lengend Snippet:

Article Snippet: A 1:60 dilution of HER2 expressing whole cell lysate in RIPA buffer (Origene LY417979), or a lysate control (Origene LY500001), was spiked in as a competitor between replicate arrays.

Techniques:

Journal: bioRxiv

Article Title: A unified peptide array platform for antibody epitope binning, mapping, specificity and predictive off-target binding

doi: 10.1101/2022.06.22.497251

Figure Lengend Snippet: Top peptide position-level sequence conservation scores (y-axis) were generated for each anti-HER2 clone using in the methods section. Scored conserved motifs, shown as Weblogos, were pairwise aligned to the HER2 primary sequence (x-axis) to generate putative epitope bins.

Article Snippet: A 1:60 dilution of HER2 expressing whole cell lysate in RIPA buffer (Origene LY417979), or a lysate control (Origene LY500001), was spiked in as a competitor between replicate arrays.

Techniques: Sequencing, Generated

Journal: bioRxiv

Article Title: A unified peptide array platform for antibody epitope binning, mapping, specificity and predictive off-target binding

doi: 10.1101/2022.06.22.497251

Figure Lengend Snippet: Top peptides for each clone aligned to the Her2 sequence (x-axis) are shown. Each aligned position is scored for target coverage (y-axis) using in the methods section and those scores are used to generate Weblogos. Relative array binding signal for each top peptide for the (+/-)HER2 competitor lysate conditions is shown in the table to the right of each alignment and logo.

Article Snippet: A 1:60 dilution of HER2 expressing whole cell lysate in RIPA buffer (Origene LY417979), or a lysate control (Origene LY500001), was spiked in as a competitor between replicate arrays.

Techniques: Sequencing, Binding Assay

Journal: bioRxiv

Article Title: A unified peptide array platform for antibody epitope binning, mapping, specificity and predictive off-target binding

doi: 10.1101/2022.06.22.497251

Figure Lengend Snippet: Top peptides for each clone aligned to the HER2 sequence (x-axis) are shown. Each aligned position is scored for target coverage (y-axis) using in the methods section and those scores are used to generate Weblogos. Relative array binding signal for each top peptide for the (+/-)HER2 competitor lysate conditions is shown in the table to the right of each alignment and logo.

Article Snippet: A 1:60 dilution of HER2 expressing whole cell lysate in RIPA buffer (Origene LY417979), or a lysate control (Origene LY500001), was spiked in as a competitor between replicate arrays.

Techniques: Sequencing, Binding Assay

Journal: bioRxiv

Article Title: A unified peptide array platform for antibody epitope binning, mapping, specificity and predictive off-target binding

doi: 10.1101/2022.06.22.497251

Figure Lengend Snippet: Top peptides for each clone aligned to the HER2 sequence (x-axis) are shown. Each aligned position is scored for target coverage (y-axis) using in the methods section and those scores are used to generate Weblogos. Relative array binding signal for each top peptide for the (+/-)HER2 competitor lysate conditions is shown in the table to the right of each alignment and logo.

Article Snippet: A 1:60 dilution of HER2 expressing whole cell lysate in RIPA buffer (Origene LY417979), or a lysate control (Origene LY500001), was spiked in as a competitor between replicate arrays.

Techniques: Sequencing, Binding Assay