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recombinant human sema3a  (R&D Systems)


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    R&D Systems recombinant human sema3a
    <t>SEMA3A</t> is highly expressed in glioblastoma (GBM) specimens compared to the normal brains. (A) REMBRANDT microarray data analysis for SEMA3A mRNA expression levels corresponding to glioma grades II-IV. WHO, World Health Organization. *** p < 0.001. (B) Kaplan-Meier survival curves of GBM patient corresponding to SEMA3A expression levels in The Cancer Genome Atlas datasets. (C) Immunohistochemistry of SEMA3A on tissue microarray. (D) Representative analysis of SEMA3A expressions in 27 GBM paired tumor and normal specimens.
    Recombinant Human Sema3a, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 59 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/s3+noncontact+microarray+printer/Recombinant+Human+Semaphorin+3A+Fc+Chimera+Protein%2C+CF/pmc06056981-41-8-14
    Average 93 stars, based on 59 article reviews
    recombinant human sema3a - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Anti-SEMA3A Antibody: A Novel Therapeutic Agent to Suppress Glioblastoma Tumor Growth"

    Article Title: Anti-SEMA3A Antibody: A Novel Therapeutic Agent to Suppress Glioblastoma Tumor Growth

    Journal: Cancer Research and Treatment : Official Journal of Korean Cancer Association

    doi: 10.4143/crt.2017.315

    SEMA3A is highly expressed in glioblastoma (GBM) specimens compared to the normal brains. (A) REMBRANDT microarray data analysis for SEMA3A mRNA expression levels corresponding to glioma grades II-IV. WHO, World Health Organization. *** p < 0.001. (B) Kaplan-Meier survival curves of GBM patient corresponding to SEMA3A expression levels in The Cancer Genome Atlas datasets. (C) Immunohistochemistry of SEMA3A on tissue microarray. (D) Representative analysis of SEMA3A expressions in 27 GBM paired tumor and normal specimens.
    Figure Legend Snippet: SEMA3A is highly expressed in glioblastoma (GBM) specimens compared to the normal brains. (A) REMBRANDT microarray data analysis for SEMA3A mRNA expression levels corresponding to glioma grades II-IV. WHO, World Health Organization. *** p < 0.001. (B) Kaplan-Meier survival curves of GBM patient corresponding to SEMA3A expression levels in The Cancer Genome Atlas datasets. (C) Immunohistochemistry of SEMA3A on tissue microarray. (D) Representative analysis of SEMA3A expressions in 27 GBM paired tumor and normal specimens.

    Techniques Used: Microarray, Expressing, Immunohistochemistry

    Identification of SEMA3A-specific single chain fragment variant (scFv) using synthetic phage library. (A) The efficacy of classical panning was evaluated by the ratio of output phage titer to input phage titer. (B) Based on enzyme-linked immunosorbent assay (ELISA) results, 52 positive clones specific to human SEMA3A were selected from among 86 clones which were selected randomly in the fourth round of the output mixture. (C) The three scFvs purified using Ni-NTA resin and poly-column were eluted by phosphate buffered saline with 200 mM imidazole (pH7.4). Molecular sizes of the three anti-SEMA3A clones (A08, C10, and F11) were verified by Coomassie blue staining. (D) hSEMA3A binding activities of three anti-SEMA antibodies and 12B (a negative control) were confirmed by indirect ELISA. 96-well plates coated with hSEMA3A (1 μg/mL) or bovine serum albumin (BSA; 1 μg/mL) were bound for three anti-SEMA3A antibodies and 12B. Then, antihemaglutinin antibody conjugated to horseradish peroxidase (HRP) was used for bound scFvs detection. The absorbance of each well for HRP reactions was measured at 450 nm. OD, optical density.
    Figure Legend Snippet: Identification of SEMA3A-specific single chain fragment variant (scFv) using synthetic phage library. (A) The efficacy of classical panning was evaluated by the ratio of output phage titer to input phage titer. (B) Based on enzyme-linked immunosorbent assay (ELISA) results, 52 positive clones specific to human SEMA3A were selected from among 86 clones which were selected randomly in the fourth round of the output mixture. (C) The three scFvs purified using Ni-NTA resin and poly-column were eluted by phosphate buffered saline with 200 mM imidazole (pH7.4). Molecular sizes of the three anti-SEMA3A clones (A08, C10, and F11) were verified by Coomassie blue staining. (D) hSEMA3A binding activities of three anti-SEMA antibodies and 12B (a negative control) were confirmed by indirect ELISA. 96-well plates coated with hSEMA3A (1 μg/mL) or bovine serum albumin (BSA; 1 μg/mL) were bound for three anti-SEMA3A antibodies and 12B. Then, antihemaglutinin antibody conjugated to horseradish peroxidase (HRP) was used for bound scFvs detection. The absorbance of each well for HRP reactions was measured at 450 nm. OD, optical density.

    Techniques Used: Variant Assay, Enzyme-linked Immunosorbent Assay, Clone Assay, Purification, Saline, Staining, Binding Assay, Negative Control, Indirect ELISA

    Production of anti-SEMA3A IgG antibodies. (A) Purity of three anti-SEMA3A IgGs determined by high performance liquid chromatography. The peak at 15-16 minutes indicates γ-globulin (~150 kDa). The purity of all three anti-SEMA3A IgGs was over 98%. (B) Sizes of the anti-SEMA3A IgGs were verified in non-reducing (NR) and reducing (R) conditions by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In NR condition, fully IgG was detected whereas in R condition where cleavages disulfide bond heavy chain and light chain were observed. (C) To determinate binding activity of human and mouse SEMA3A, three anti-SEMA3A IgGs were analyzed on enzyme-linked immunosorbent assay (ELISA) plates when the presence of hSEMA3A, mSEMA3A, and bovine serum albumin (BSA) as negative control. Optical density (OD) values derived from indirect ELISA in which SEMA3A IgG was captured via anti-human Fab antibody conjugated to horseradish peroxidase. (D) Use of the BIAcore to determine the calculated K D value of three anti-SEMA3A IgGs to human and mouse SEMA3A. The assay method was Fab-based capture format via human Fab capture kit (GE Healthcare).
    Figure Legend Snippet: Production of anti-SEMA3A IgG antibodies. (A) Purity of three anti-SEMA3A IgGs determined by high performance liquid chromatography. The peak at 15-16 minutes indicates γ-globulin (~150 kDa). The purity of all three anti-SEMA3A IgGs was over 98%. (B) Sizes of the anti-SEMA3A IgGs were verified in non-reducing (NR) and reducing (R) conditions by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In NR condition, fully IgG was detected whereas in R condition where cleavages disulfide bond heavy chain and light chain were observed. (C) To determinate binding activity of human and mouse SEMA3A, three anti-SEMA3A IgGs were analyzed on enzyme-linked immunosorbent assay (ELISA) plates when the presence of hSEMA3A, mSEMA3A, and bovine serum albumin (BSA) as negative control. Optical density (OD) values derived from indirect ELISA in which SEMA3A IgG was captured via anti-human Fab antibody conjugated to horseradish peroxidase. (D) Use of the BIAcore to determine the calculated K D value of three anti-SEMA3A IgGs to human and mouse SEMA3A. The assay method was Fab-based capture format via human Fab capture kit (GE Healthcare).

    Techniques Used: High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis, Binding Assay, Activity Assay, Enzyme-linked Immunosorbent Assay, Negative Control, Derivative Assay, Indirect ELISA

    Anti-SEMA3A IgG antibody impedes migration and proliferation of patient-derived glioblastoma (GBM) cells. (A) The concentration of SEMA3A secreted for a day was measured by sandwich enzyme-linked immunosorbent assay (ELISA) in various cell types. GBM patient cells and U87-MG cells as a positive control and neural progenitor cell and medium as negative controls. (B) Neutralization assay of three anti-SEMA3A IgGs in U87-MG cells. The evaluate method is same method for U87-MG cells were incubated with anti-SEMA3A IgG and the amount of SEMA3A in medium was measured by sandwich ELISA. (C) While the migration rate of cells (U87-MG, 131, and 83) treated with control human IgG remains unchanged, migration rates of cells treated with anti-SEMA3A IgGs for 1 day were impeded significantly. Each antibody treatment concentration was 10 μg/mL and macroscopic observation of the transwell chambers. *p < 0.05, **p < 0.01. (D) Inhibition of migration activity by anti-SEMA3A F11 for one day was evaluated using Oris cell migration assay. The level of migration activity inhibition was proportional to the concentration gradient of anti-SEMA3A F11. Migration activity was reduced by 52% compared to the control IgG-treated cells in the max concentration of F11 (200 nM) treated cells. (E) Comparison of the effect of anti-SEMA3A F11 and control human IgG (2 μM) on in-vitro proliferation of 131 cells. On the 9 days after F11 treatment, 131 proliferation was inhibited by 60% of control human IgG treated cells. (F) Immunoblots of phospho-ERK and ERK in control human IgG or F11 IgG treated 131 and 559 cells. The SEMA3A hypersecreting 131 cells decreased ERK phosphorylation during F11 treatment and remained unchanged for ERK phosphorylation of 559 cells that secretes less SEMA3A.
    Figure Legend Snippet: Anti-SEMA3A IgG antibody impedes migration and proliferation of patient-derived glioblastoma (GBM) cells. (A) The concentration of SEMA3A secreted for a day was measured by sandwich enzyme-linked immunosorbent assay (ELISA) in various cell types. GBM patient cells and U87-MG cells as a positive control and neural progenitor cell and medium as negative controls. (B) Neutralization assay of three anti-SEMA3A IgGs in U87-MG cells. The evaluate method is same method for U87-MG cells were incubated with anti-SEMA3A IgG and the amount of SEMA3A in medium was measured by sandwich ELISA. (C) While the migration rate of cells (U87-MG, 131, and 83) treated with control human IgG remains unchanged, migration rates of cells treated with anti-SEMA3A IgGs for 1 day were impeded significantly. Each antibody treatment concentration was 10 μg/mL and macroscopic observation of the transwell chambers. *p < 0.05, **p < 0.01. (D) Inhibition of migration activity by anti-SEMA3A F11 for one day was evaluated using Oris cell migration assay. The level of migration activity inhibition was proportional to the concentration gradient of anti-SEMA3A F11. Migration activity was reduced by 52% compared to the control IgG-treated cells in the max concentration of F11 (200 nM) treated cells. (E) Comparison of the effect of anti-SEMA3A F11 and control human IgG (2 μM) on in-vitro proliferation of 131 cells. On the 9 days after F11 treatment, 131 proliferation was inhibited by 60% of control human IgG treated cells. (F) Immunoblots of phospho-ERK and ERK in control human IgG or F11 IgG treated 131 and 559 cells. The SEMA3A hypersecreting 131 cells decreased ERK phosphorylation during F11 treatment and remained unchanged for ERK phosphorylation of 559 cells that secretes less SEMA3A.

    Techniques Used: Migration, Derivative Assay, Concentration Assay, Sandwich ELISA, Enzyme-linked Immunosorbent Assay, Positive Control, Neutralization, Incubation, Control, Inhibition, Activity Assay, Cell Migration Assay, Comparison, In Vitro, Western Blot, Phospho-proteomics

    In vivo effects of anti-SEMA3A antibody on the glioblastoma (GBM) tumor growth. (A) Antitumor activity of antiSEMA3A F11 in GBM patient cell 131 xenograft model. When tumors were approximately 80 mm 3 , the patient-derived xenograft tumors were randomly assigned into study groups (n=7 mice/group) and were participated in the dosing phase of the study. Treatment of F11 was administered intravenously at 5 mg/kg and 25 mg/kg with all treatments well tolerated and anti-SEMA3A F11 injections were stopped at day 28. *p < 0.05. (B) Mass weight variation of mice was similar to mass size affected by anti-SEMA3A F11 within groups. *p < 0.05. (C, D) Representative immunofluorescence images of SEMA3A, p-ERK, terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) and Iba1 staining using paraffin sections of tumors. Scale bars=20 μm (white), 100 μm (red).
    Figure Legend Snippet: In vivo effects of anti-SEMA3A antibody on the glioblastoma (GBM) tumor growth. (A) Antitumor activity of antiSEMA3A F11 in GBM patient cell 131 xenograft model. When tumors were approximately 80 mm 3 , the patient-derived xenograft tumors were randomly assigned into study groups (n=7 mice/group) and were participated in the dosing phase of the study. Treatment of F11 was administered intravenously at 5 mg/kg and 25 mg/kg with all treatments well tolerated and anti-SEMA3A F11 injections were stopped at day 28. *p < 0.05. (B) Mass weight variation of mice was similar to mass size affected by anti-SEMA3A F11 within groups. *p < 0.05. (C, D) Representative immunofluorescence images of SEMA3A, p-ERK, terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) and Iba1 staining using paraffin sections of tumors. Scale bars=20 μm (white), 100 μm (red).

    Techniques Used: In Vivo, Activity Assay, Derivative Assay, Immunofluorescence, TUNEL Assay, Staining

    Related Articles

    Cell Culture:

    Article Title: Modulation of DRG neurons response to semaphorin 3A via substrate stiffness.
    Article Snippet: Semaphorin 3A (Sema3a) is a chemotropic protein that acts as a neuronal guidance cue and plays a major role in dorsal root ganglion (DRG) sensory neurons projection during embryo development.. The present study evaluated the impact of stiffness in the repulsive response of DRG neurons to Sema3a when cultured over substrates of variable stiffness.. Stiffness modified DRG neurons morphology and regulated their response to Sema3a, reducing the collapse of growth cones when they were cultured on softer substrates.

    Incubation:

    Article Title: Modulation of DRG neurons response to semaphorin 3A via substrate stiffness.
    Article Snippet: Semaphorin 3A (Sema3a) is a chemotropic protein that acts as a neuronal guidance cue and plays a major role in dorsal root ganglion (DRG) sensory neurons projection during embryo development.. The present study evaluated the impact of stiffness in the repulsive response of DRG neurons to Sema3a when cultured over substrates of variable stiffness.. Stiffness modified DRG neurons morphology and regulated their response to Sema3a, reducing the collapse of growth cones when they were cultured on softer substrates.

    Article Title: Paradoxical expression of NRP1 in decidual stromal and immune cells reveals a novel inflammation balancing mechanism during early pregnancy.
    Article Snippet: Objective and design To investigate the balancing mechanisms between decidualization-associated inflammation and pregnancy-related immunotolerance.. Material or subjects Decidual samples from women with normal pregnancy (n = 58) or unexplained spontaneous miscarriage (n = 13), peripheral blood from normal pregnancy and endometria from non-pregnancy (n = 10) were collected.. Primary endometrial stromal cells (ESCs), decidual stromal cells (DSCs), decidual immune cells (DICs) and peripheral blood mononuclear cells (PBMCs) were isolated.

    Recombinant:

    Article Title: Modulation of DRG neurons response to semaphorin 3A via substrate stiffness.
    Article Snippet: Semaphorin 3A (Sema3a) is a chemotropic protein that acts as a neuronal guidance cue and plays a major role in dorsal root ganglion (DRG) sensory neurons projection during embryo development.. The present study evaluated the impact of stiffness in the repulsive response of DRG neurons to Sema3a when cultured over substrates of variable stiffness.. Stiffness modified DRG neurons morphology and regulated their response to Sema3a, reducing the collapse of growth cones when they were cultured on softer substrates.

    Article Title: Osseointegration of Titanium Implants in a Botox-Induced Muscle Paralysis Rat Model Is Sensitive to Surface Topography and Semaphorin 3A Treatment
    Article Snippet: .. Recombinant human sema3A (R&D Systems) was reconstituted with the PEG-DBCO crosslinker solution. ..

    Article Title: Paradoxical expression of NRP1 in decidual stromal and immune cells reveals a novel inflammation balancing mechanism during early pregnancy.
    Article Snippet: Objective and design To investigate the balancing mechanisms between decidualization-associated inflammation and pregnancy-related immunotolerance.. Material or subjects Decidual samples from women with normal pregnancy (n = 58) or unexplained spontaneous miscarriage (n = 13), peripheral blood from normal pregnancy and endometria from non-pregnancy (n = 10) were collected.. Primary endometrial stromal cells (ESCs), decidual stromal cells (DSCs), decidual immune cells (DICs) and peripheral blood mononuclear cells (PBMCs) were isolated.

    Article Title: Compositions and methods for treating and preventing inflammation
    Article Snippet: Recombinant mouse CCL2/JE/MCP-1 (from E. coli) (R&D Systems) concentration used in vitro 100 ng/ml. .. Recombinant human SEMA3A Fc chimera (from murine myeloma cell line, NS0) (R&D Systems) concentration used in vitro 100 ng/ml. .. Wild-type mice subjected to OIR were intravitreally injected with rmNRP1 trap-1 (FIGS. 19C and 20X-20Y, SEQ ID NO: 25) from plasmid (29) or R&D Systems at P12.

    Control:

    Article Title: Modulation of DRG neurons response to semaphorin 3A via substrate stiffness.
    Article Snippet: Semaphorin 3A (Sema3a) is a chemotropic protein that acts as a neuronal guidance cue and plays a major role in dorsal root ganglion (DRG) sensory neurons projection during embryo development.. The present study evaluated the impact of stiffness in the repulsive response of DRG neurons to Sema3a when cultured over substrates of variable stiffness.. Stiffness modified DRG neurons morphology and regulated their response to Sema3a, reducing the collapse of growth cones when they were cultured on softer substrates.

    Article Title: Cochlear hair cell innervation is dependent on a modulatory function of Semaphorin-3A.
    Article Snippet: Department of Biology, Georgetown University, Washington, District of Columbia, USA Interdisciplinary Program in Neuroscience, Georgetown University, Washington, District of Columbia, USA Department of Pharmacology, Georgetown University School of Medicine, Washington, District of Columbia, USA Institute for Auditory Neuroscience and InnerEarLab, University Medical Center, and Auditory Neuroscience & Synaptic Nanophysiology Group, Max Planck Institute for Multidisciplinary Sciences, and Cluster of Excellence “Multiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells” (MBExC), Göttingen, Germany

    Purification:

    Article Title: Paradoxical expression of NRP1 in decidual stromal and immune cells reveals a novel inflammation balancing mechanism during early pregnancy.
    Article Snippet: Objective and design To investigate the balancing mechanisms between decidualization-associated inflammation and pregnancy-related immunotolerance.. Material or subjects Decidual samples from women with normal pregnancy (n = 58) or unexplained spontaneous miscarriage (n = 13), peripheral blood from normal pregnancy and endometria from non-pregnancy (n = 10) were collected.. Primary endometrial stromal cells (ESCs), decidual stromal cells (DSCs), decidual immune cells (DICs) and peripheral blood mononuclear cells (PBMCs) were isolated.

    Isolation:

    Article Title: Paradoxical expression of NRP1 in decidual stromal and immune cells reveals a novel inflammation balancing mechanism during early pregnancy.
    Article Snippet: Objective and design To investigate the balancing mechanisms between decidualization-associated inflammation and pregnancy-related immunotolerance.. Material or subjects Decidual samples from women with normal pregnancy (n = 58) or unexplained spontaneous miscarriage (n = 13), peripheral blood from normal pregnancy and endometria from non-pregnancy (n = 10) were collected.. Primary endometrial stromal cells (ESCs), decidual stromal cells (DSCs), decidual immune cells (DICs) and peripheral blood mononuclear cells (PBMCs) were isolated.

    Concentration Assay:

    Article Title: Compositions and methods for treating and preventing inflammation
    Article Snippet: Recombinant mouse CCL2/JE/MCP-1 (from E. coli) (R&D Systems) concentration used in vitro 100 ng/ml. .. Recombinant human SEMA3A Fc chimera (from murine myeloma cell line, NS0) (R&D Systems) concentration used in vitro 100 ng/ml. .. Wild-type mice subjected to OIR were intravitreally injected with rmNRP1 trap-1 (FIGS. 19C and 20X-20Y, SEQ ID NO: 25) from plasmid (29) or R&D Systems at P12.

    In Vitro:

    Article Title: Compositions and methods for treating and preventing inflammation
    Article Snippet: Recombinant mouse CCL2/JE/MCP-1 (from E. coli) (R&D Systems) concentration used in vitro 100 ng/ml. .. Recombinant human SEMA3A Fc chimera (from murine myeloma cell line, NS0) (R&D Systems) concentration used in vitro 100 ng/ml. .. Wild-type mice subjected to OIR were intravitreally injected with rmNRP1 trap-1 (FIGS. 19C and 20X-20Y, SEQ ID NO: 25) from plasmid (29) or R&D Systems at P12.



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    Microarray analysis reveals the effects of GFAP mAb treatment on key inflammatory mediators in glaucomatous retina. ( A - C ) The expression of TLR4 and S100A8 was significantly downregulated by 25–50 µg GFAP mAb treatment compared to the vehicle. The marker for microglial activation, CD68, was significantly decreased in the 25 µg GFAP mAb treatment group. ( D - F ) Proteins of the inflammasome pathway, NLRP3, GSDMD and Caspase-1 were significantly downregulated in the 25 µg GFAP mAb treatment group. With the 50 µg dose, these protein expressions showed a similar downward trend, but without statistical significance. ( G ) Expression profiling of inflammation-associated mediators showed that 25 µg GFAP mAb significantly decreased pro-inflammatory factors (TNF-α, IL-1β, IL-8, MMP9, and IFN-γ), and increased the anti-inflammatory cytokine IL-10 compared to the vehicle group. In contrast, the 50 µg dose significantly reduced IFN-γ only. ( H ) Representative images of spots showing IL-1β levels in the subarrays for each group. Image analysis was conducted with Imagene software, using the median intensity from each spot to calculate the mean of the triplicate spots for each marker. For CD68 and TLR4, due to significant heterogeneity in SDs, statistical analysis was performed using Welch’s ANOVA followed by the Tamhane T2 post hoc test. All other data were analyzed using one-way ANOVA with Tukey’s post hoc test. Data are presented as the mean ± SD; n = 4 per group; * p < 0.05, ** p < 0.01, *** p < 0.001; ns = not significant. TLR4 – Toll-Like Receptor 4. S100A8 – S100 Calcium Binding Protein A8. NLRP3 – NLR Family Pyrin Domain Containing 3. GSDMD – Gasdermin D

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    doi: 10.1186/s12974-025-03482-8

    Figure Lengend Snippet: Microarray analysis reveals the effects of GFAP mAb treatment on key inflammatory mediators in glaucomatous retina. ( A - C ) The expression of TLR4 and S100A8 was significantly downregulated by 25–50 µg GFAP mAb treatment compared to the vehicle. The marker for microglial activation, CD68, was significantly decreased in the 25 µg GFAP mAb treatment group. ( D - F ) Proteins of the inflammasome pathway, NLRP3, GSDMD and Caspase-1 were significantly downregulated in the 25 µg GFAP mAb treatment group. With the 50 µg dose, these protein expressions showed a similar downward trend, but without statistical significance. ( G ) Expression profiling of inflammation-associated mediators showed that 25 µg GFAP mAb significantly decreased pro-inflammatory factors (TNF-α, IL-1β, IL-8, MMP9, and IFN-γ), and increased the anti-inflammatory cytokine IL-10 compared to the vehicle group. In contrast, the 50 µg dose significantly reduced IFN-γ only. ( H ) Representative images of spots showing IL-1β levels in the subarrays for each group. Image analysis was conducted with Imagene software, using the median intensity from each spot to calculate the mean of the triplicate spots for each marker. For CD68 and TLR4, due to significant heterogeneity in SDs, statistical analysis was performed using Welch’s ANOVA followed by the Tamhane T2 post hoc test. All other data were analyzed using one-way ANOVA with Tukey’s post hoc test. Data are presented as the mean ± SD; n = 4 per group; * p < 0.05, ** p < 0.01, *** p < 0.001; ns = not significant. TLR4 – Toll-Like Receptor 4. S100A8 – S100 Calcium Binding Protein A8. NLRP3 – NLR Family Pyrin Domain Containing 3. GSDMD – Gasdermin D

    Article Snippet: Briefly, the microarray was prepared using a noncontact microarray printer (SciFLEXARRAYER S3; Scienion, Berlin, Germany).

    Techniques: Microarray, Expressing, Marker, Activation Assay, Software, Binding Assay

    Probing receptor binding specificities of A(H3N2) and A(H1N1)pdm09. a) Collection of glycans printed on succinimide reactive microarray slides. Glycan binding data of b) early A(H3N2) and A(H3N2) 3C.2 viruses; c) A (H3N2) 3C.3 viruses; and d) A(H1N1)pdm09 viruses. Whole viruses were exposed to a glycan microarray, and binding was visualized antistalk antibodies. Bars represent the average relative fluorescence units (RFU) of four replicates ± SD.

    Journal: JACS Au

    Article Title: Asymmetrical Biantennary Glycans Prepared by a Stop-and-Go Strategy Reveal Receptor Binding Evolution of Human Influenza A Viruses

    doi: 10.1021/jacsau.3c00695

    Figure Lengend Snippet: Probing receptor binding specificities of A(H3N2) and A(H1N1)pdm09. a) Collection of glycans printed on succinimide reactive microarray slides. Glycan binding data of b) early A(H3N2) and A(H3N2) 3C.2 viruses; c) A (H3N2) 3C.3 viruses; and d) A(H1N1)pdm09 viruses. Whole viruses were exposed to a glycan microarray, and binding was visualized antistalk antibodies. Bars represent the average relative fluorescence units (RFU) of four replicates ± SD.

    Article Snippet: The glycans, which have an α-amine at the anomeric asparagine moiety, were printed on amine reactive NHS activated glass slides using a noncontact microarray printer ( S3 , Scienion, Inc.).

    Techniques: Binding Assay, Microarray, Glycoproteomics, Fluorescence