biotinylated lectins concanavalin cona  (Vector Laboratories)

Journal: ACS Omega

Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

doi: 10.1021/acsomega.5c00867

Figure Lengend Snippet: Lectin detection profiles. A total of 12 plasmon shift values, measured after 15 min of immobilization, were recorded for each lectin, with the average and standard deviation values represented by each band in the graph. Each lectin is used to create the LPS profiles for each bacterial species injected at 100 μg/mL, as well as a PBS buffer blank reference. The lectins chosen are Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA). These lectins will be referred by their abbreviation for the next figures to avoid unnecessary length in the legend.

Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

Techniques: Standard Deviation, Injection

Journal: ACS Omega

Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

doi: 10.1021/acsomega.5c00867

Figure Lengend Snippet: Feature importance coefficient. Each bar illustrates the mean importance coefficients for the 7 features associated with 7 lectins, calculated from 10 randomly selected train/test splits of the data set using a Random Forest model with 100 trees.

Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

Techniques:

Journal: ACS Omega

Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

doi: 10.1021/acsomega.5c00867

Figure Lengend Snippet: Feature reduction for RF and SVM machine learning models. The best-performing lectin set from the combination of increasing number of lectins (1 to 7, from left to right) is used in a 10 repeated 3-fold cross-validation to determine the accuracy for each model. Significant differences are assessed with a t -test ( p > 0.05). An asterisk indicates a distribution with a statistically significant difference in performance compared to a distribution without it.

Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

Techniques:

Journal: ACS Omega

Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

doi: 10.1021/acsomega.5c00867

Figure Lengend Snippet: Classification Report for Different Profile Lengths with the SVM Model

Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

Techniques:

Journal: ACS Omega

Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

doi: 10.1021/acsomega.5c00867

Figure Lengend Snippet: Classification Report for Different Profile Lengths with the RF Model

Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

Techniques:

Journal: Nature Metabolism

Article Title: Feeding-regulated glycogen metabolism drives rhythmic liver protein secretion

doi: 10.1038/s42255-026-01453-8

Figure Lengend Snippet: a , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in vivo. WT mice under a regular 12 h light–dark cycle and NR feeding were subcutaneously injected with either vehicle (Veh) or CP-91149 at ZT0 for tissue collections at ZT3, ZT6, ZT9, ZT12 and ZT24. b , Average food consumption of WT mice ( n = 4 biological replicates) 24 h after CP-91149 injection. c , Temporal profiles of glycogen in the liver of Veh-injected and CP-91149-injected mice ( n = 20 (5 timepoints × 4 biological replicates)). d , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated mouse liver were determined by lectin blot analysis with concanavalin A (ConA, n = 20 (5 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (right). e , C3 levels in mouse serum as assessed by ELISA ( n = 20 (5 timepoints × 4 biological replicates)). f , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in AML12 mouse hepatocytes. Treatment with Veh or CP-91149 (67 µM) was performed for 3, 6, 12 and 24 h. g , h , Kinetic profiles of UDP-glucose + UDP-galactose levels ( g ), cytidine 5′-monophospho-N-acetyl neuraminic acid (CMP-Neu5Ac) ( h , left) and uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) ( h , right) in AML12 cells upon CP-91149 treatment ( n = 16 (4 timepoints × 4 biological replicates)). i , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated AML12 cells were determined by lectin blot analysis with ConA ( n = 16 (4 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (bottom). j , ALB, FN1 and C3 levels in cell medium determined by ELISA ( n = 22–24 (4 timepoints × 6 biological replicates, with ALB 14 h Veh and 24 h CP-91149 n = 5)). k , Experimental design (created with BioRender.com ). AML12 cells were treated with Veh or CP-91149 for 14 h in the absence or presence of supplemental UDP-glucose (UDPG; 2 mM). l , m , ALB and C3 levels in cell medium ( l ) and lysates ( m ) as determined by ELISA ( n = 6 biological replicates, except for ALB under CP-91149 treatment ( n = 5)). Data are displayed as means; error bars, s.e.m. Boxplots show the median (centre line), interquartile range (box) and minimum to maximum values (whiskers). A detailed description of the statistical analysis is available in Source Data Fig. . See also Extended Data Fig. .

Article Snippet: Primary antibodies were used at the following dilutions: 1:1,000 for ATF4 (Cell Signaling Technologies, 11815), ARFGAP1 (Cell Signaling Technologies, 14608), Phospho-RPS6 (Cell Signaling Technologies, 2211), Total-RPS6 (Cell Signaling Technologies, 2217), GABARAPL1 (Genetex, GTX132664) and ConA Lectin (Vector Laboratories, B-1005) and 1:2,000 for STX4 (ProteinTech, 14988-1-AP).

Techniques: Inhibition, In Vivo, Injection, Glycoproteomics, Staining, Control, Enzyme-linked Immunosorbent Assay

Journal: Biomolecules

Article Title: Thyroid Carcinoma Glycoproteins Express Altered N-Glycans with 3-O-Sulfated Galactose Residues

doi: 10.3390/biom14121482

Figure Lengend Snippet: Figure 1. Lectin blot of normal human thyroid tissue and papillary thyroid cancer (PTC). Normal and PTC extracts of a single patient sample examined after reducing SDS-PAGE and transfer for interactions by Western blot techniques with a variety of plant lectins and the O6 mAb, whose glycan specificities are indicated in the graphic at left. Prior to gel electrophoresis, the samples were treated with or without PNGaseF (see graphic), neuraminidase A (NeuA) or neuraminidase S (NeuS) (remove sialic acid), or O-glycanase (removes core 1 O-glycans), and proteins resolved on SDS-PAGE. Gels stained with either Coomassie Brilliant Blue solution (CBB, a) or analyzed by Western/lectin blot probed with ConA (b), SNA (c), MAL-I (d), O6 VLR antibody (e), PHA-L (f), or PHA-E (g). (a) serves as a loading control for (b–g). This set of gels is a representative set from 1 patient sample of 5 patients (one sample did not have enough material remaining after processing to perform these assays). Original western blots can be found at Supplementary Materials.

Article Snippet: Membranes were incubated with 5% (w/v) bovine serum albumin (BSA) in TRIS-buffer saline with 0.05% Tween 20 (TBST) for 1 h at room temperature followed by incubation with biotinylated lectins concanavalin A (ConA), Sambucus nigra agglutinin (SNA), Maackia amurensis lectin (MAL-I), Phaseolus vulgaris leucoagglutinin (PHA-L), Phaseolus vulgaris erythroagglutinin (PHA-E) (Vector Labs, Newark, CA, USA) and the 06 antibody (lamprey-derived recombinant anti-3-0-sulfo-Gal) [30].

Techniques: SDS Page, Western Blot, Glycoproteomics, Nucleic Acid Electrophoresis, Staining, Control

Journal: Biomolecules

Article Title: Thyroid Carcinoma Glycoproteins Express Altered N-Glycans with 3-O-Sulfated Galactose Residues

doi: 10.3390/biom14121482

Figure Lengend Snippet: Figure 2. Lectin blot cross-comparison of four paired normal and cancerous human thyroid tissue homogenates. Tissue extracts from four of six specimens for normal and PTC were resolved on SDS-PAGE and stained with CBB (a), as in Figure 1, and in analyzed by Western/lectin blot using ConA (b), SNA (c), MAL-I (d), O6 VLR antibody (e), PHA-L (f), or PHA-E (g). (a) serves as a loading control for (b–g). Original western blots can be found at Supplementary Materials.

Article Snippet: Membranes were incubated with 5% (w/v) bovine serum albumin (BSA) in TRIS-buffer saline with 0.05% Tween 20 (TBST) for 1 h at room temperature followed by incubation with biotinylated lectins concanavalin A (ConA), Sambucus nigra agglutinin (SNA), Maackia amurensis lectin (MAL-I), Phaseolus vulgaris leucoagglutinin (PHA-L), Phaseolus vulgaris erythroagglutinin (PHA-E) (Vector Labs, Newark, CA, USA) and the 06 antibody (lamprey-derived recombinant anti-3-0-sulfo-Gal) [30].

Techniques: Comparison, SDS Page, Staining, Western Blot, Control