concanavalin a  (Vector Laboratories)


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    Name:
    Unconjugated Concanavalin A Con A
    Description:
    Concanavalin A Con A recognizes α linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins At neutral and alkaline pH Con A exists as a tetramer of four identical subunits below pH 5 6 Con A dissociates into active dimers of 52 kDa Acetylation succinylation or other derivatizations can also produce stable forms with dimeric structures See succinylated Con A Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds Con A requires calcium or manganese ions at each of its four saccharide binding sites Although these divalent metal ions are bound tightly to the polypeptide structure buffers which can bind calcium such as phosphate generally should be avoided in diluting Con A since a gradual loss in activity may occur Inhibiting Eluting Sugar mixture of 200 mM α methylmannoside 200 mM α methylglucoside
    Catalog Number:
    l-1000
    Price:
    None
    Category:
    Proteins
    Size:
    500 mg
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    Structured Review

    Vector Laboratories concanavalin a
    Unconjugated Concanavalin A Con A
    Concanavalin A Con A recognizes α linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins At neutral and alkaline pH Con A exists as a tetramer of four identical subunits below pH 5 6 Con A dissociates into active dimers of 52 kDa Acetylation succinylation or other derivatizations can also produce stable forms with dimeric structures See succinylated Con A Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds Con A requires calcium or manganese ions at each of its four saccharide binding sites Although these divalent metal ions are bound tightly to the polypeptide structure buffers which can bind calcium such as phosphate generally should be avoided in diluting Con A since a gradual loss in activity may occur Inhibiting Eluting Sugar mixture of 200 mM α methylmannoside 200 mM α methylglucoside
    https://www.bioz.com/result/concanavalin a/product/Vector Laboratories
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    concanavalin a - by Bioz Stars, 2021-03
    94/100 stars

    Images

    1) Product Images from "GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain"

    Article Title: GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain

    Journal: eLife

    doi: 10.7554/eLife.08916

    The TM and cytoplasmic domain of GnT1IP-L does not inhibit MGAT1. ( A ) Lectin-resistance test of cloned CHO cells stably expressing GnT1IP-L/MGAT1-Myc compared to CHO cells and Lec1 CHO cells that lack MGAT1 (n = 2). ( B ) The same cloned GnT1IP-L transfectant lines were compared to CHO and Lec1 cells for resistance to Con A (n = 2). ( C ) Western analysis of CHO cell lysates from the cloned transfectants in ( A ) and ( B ). * non-specific band shows equal loading. DOI: http://dx.doi.org/10.7554/eLife.08916.007
    Figure Legend Snippet: The TM and cytoplasmic domain of GnT1IP-L does not inhibit MGAT1. ( A ) Lectin-resistance test of cloned CHO cells stably expressing GnT1IP-L/MGAT1-Myc compared to CHO cells and Lec1 CHO cells that lack MGAT1 (n = 2). ( B ) The same cloned GnT1IP-L transfectant lines were compared to CHO and Lec1 cells for resistance to Con A (n = 2). ( C ) Western analysis of CHO cell lysates from the cloned transfectants in ( A ) and ( B ). * non-specific band shows equal loading. DOI: http://dx.doi.org/10.7554/eLife.08916.007

    Techniques Used: Clone Assay, Stable Transfection, Expressing, Transfection, Western Blot

    2) Product Images from "Photogenerated Lectin Sensors Produced by Thiol-Ene/Yne Photo-Click Chemistry in Aqueous Solution"

    Article Title: Photogenerated Lectin Sensors Produced by Thiol-Ene/Yne Photo-Click Chemistry in Aqueous Solution

    Journal: Biosensors & bioelectronics

    doi: 10.1016/j.bios.2012.01.001

    Illustration of referenced binding curves of triplicate injections of Con A and RCA-I to mannose-/galactose-surfaces on a) alkyne-based surfaces and b) alkene-based surfaces.
    Figure Legend Snippet: Illustration of referenced binding curves of triplicate injections of Con A and RCA-I to mannose-/galactose-surfaces on a) alkyne-based surfaces and b) alkene-based surfaces.

    Techniques Used: Binding Assay

    3) Product Images from "Epstein-Barr virus activates F-box protein FBXO2 to limit viral infectivity by targeting glycoprotein B for degradation"

    Article Title: Epstein-Barr virus activates F-box protein FBXO2 to limit viral infectivity by targeting glycoprotein B for degradation

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1007208

    N -linked high-mannose glycosylation of EBV gB is required for FBXO2 interaction. (A)  Analysis of glycan modifications of gB. gB-SFB purified from CNE2 cells stably expressing the protein was treated with endoglycosidase H (Endo H) or PNGase H or a Deglycosylation Mix before electrophoresis on 8% polyacrylamide gels. The sizes of molecular mass markers (M) are shown in kDa.  (B)  CNE2 cells stably expressing gB-SFB were treated with tunicamycin at different concentrations as indicated overnight before harvest. Con A agarose was used to enrich  N -linked glycoproteins. TCL: total cell lysates.  (C-D)  Inhibition of N-linked glycosylation of gB by tunicamycin abrogates the gB-FBXO2 association. HEK293T cells transfected with plasmids encoding Myc-FBXO2 and gB-SFB were treated with 0.25 μg/mL tunicamycin or DMSO for 24 h, and the cells were harvested and subjected to immunoprecipitation by S-protein agarose  (C)  or anti-Myc agarose  (D) .  (E)  Sequential pull-down of glycosylated gB by GST-FBXO2 followed by Con A agarose pull-down. Eight percent of the TCL of cells stably expressing gB was loaded as input; F-T: 8% of the flow-through.  (F)  Schematic diagram of glycosylation sites on gB and its N-to-Q mutants. The signal peptide (SP), furin cleavage site and transmembrane (TM) domain of gB are indicated.  (G)  Ribbon diagrams of the monomeric EBV gB structure, illustrated with the PyMol program using PDB 3FVC as the template. The glycosylation sites as shown in  (F)  are colored in magenta.  (H-I)  Con A agarose pull-down of gB single  (H)  or multiple  (I)  N-to-Q mutants.  (J-K)  Co-IP of FBXO2 with glycosylation-defective gB mutants. HEK293T cells were co-transfected with Myc-FBXO2 and gB N-to-Q mutants as indicated, and the cell lysates were subjected to immunoprecipitation by S-protein agarose  (J)  or anti-Myc agarose  (K)  and immunoblotted with anti-Myc and anti-FLAG antibodies.
    Figure Legend Snippet: N -linked high-mannose glycosylation of EBV gB is required for FBXO2 interaction. (A) Analysis of glycan modifications of gB. gB-SFB purified from CNE2 cells stably expressing the protein was treated with endoglycosidase H (Endo H) or PNGase H or a Deglycosylation Mix before electrophoresis on 8% polyacrylamide gels. The sizes of molecular mass markers (M) are shown in kDa. (B) CNE2 cells stably expressing gB-SFB were treated with tunicamycin at different concentrations as indicated overnight before harvest. Con A agarose was used to enrich N -linked glycoproteins. TCL: total cell lysates. (C-D) Inhibition of N-linked glycosylation of gB by tunicamycin abrogates the gB-FBXO2 association. HEK293T cells transfected with plasmids encoding Myc-FBXO2 and gB-SFB were treated with 0.25 μg/mL tunicamycin or DMSO for 24 h, and the cells were harvested and subjected to immunoprecipitation by S-protein agarose (C) or anti-Myc agarose (D) . (E) Sequential pull-down of glycosylated gB by GST-FBXO2 followed by Con A agarose pull-down. Eight percent of the TCL of cells stably expressing gB was loaded as input; F-T: 8% of the flow-through. (F) Schematic diagram of glycosylation sites on gB and its N-to-Q mutants. The signal peptide (SP), furin cleavage site and transmembrane (TM) domain of gB are indicated. (G) Ribbon diagrams of the monomeric EBV gB structure, illustrated with the PyMol program using PDB 3FVC as the template. The glycosylation sites as shown in (F) are colored in magenta. (H-I) Con A agarose pull-down of gB single (H) or multiple (I) N-to-Q mutants. (J-K) Co-IP of FBXO2 with glycosylation-defective gB mutants. HEK293T cells were co-transfected with Myc-FBXO2 and gB N-to-Q mutants as indicated, and the cell lysates were subjected to immunoprecipitation by S-protein agarose (J) or anti-Myc agarose (K) and immunoblotted with anti-Myc and anti-FLAG antibodies.

    Techniques Used: Purification, Stable Transfection, Expressing, Electrophoresis, Inhibition, Transfection, Immunoprecipitation, Flow Cytometry, Co-Immunoprecipitation Assay

    FBXO2 ubiquitinates and degrades  N -linked glycosylated gB. (A)  FBXO2 reduces the level of glycosylated gB. HEK293T cells were co-transfected with gB, along with the FL, N-terminal or C-terminal FBXO2 constructs. 48 hrs later, the glycosylated proteins were enriched by Con A agarose pull-down, and the bound proteins and total cell lysates were immunoblotted with anti-FLAG and anti-Myc antibodies.  (B)  FBXO2 did not affect the total or glycosylated levels of the glycosylation-defective 7NQ gB mutant. The experiments were conducted as in  (A) .  (C)  CNE2 cells stably expressing gB were transfected with three siRNAs targeting FBXO2 or a scramble control siRNA, and 72 h later, the cells were harvested and subjected to Con A pull-down and WB.  (D)  Effects of MG132 and bafilomycin A1 on the levels of total and glycosylated gB.  (E)  FBXO2 ubiquitinates gB  in vivo . HEK293T cells were transfected with His-ubiquitin (Ub), gB-SFB and Myc-FBXO2 or empty vector. The cells were treated with or without 20 μM MG132 for 6 h before harvest. 48 hrs post-transfection, the cells were lysed in 6 M guanidine-HCl buffer, the His-tagged ubiquitinated proteins were enriched by Ni-NTA (nickel-nitrilotriacetic acid) pull-down, and the bound proteins were eluted by SDS loading buffer and immunoblotted with antibodies as indicated.  (F)  HEK293T cells stably expressing gB were transfected with empty vector or Myc-FBXO2, and 36 h later the cells were treated with 50 μg/mL cycloheximide (CHX) to block protein synthesis and collected at the indicated time points. (top) Total cell lysates were analyzed by WB; (bottom) the degradation of gB was calculated by determining the relative quantification of gB from WB results. The mean value for vector-transfected cells at 0 h was normalized to a relative protein level of 100% (n = 3).
    Figure Legend Snippet: FBXO2 ubiquitinates and degrades N -linked glycosylated gB. (A) FBXO2 reduces the level of glycosylated gB. HEK293T cells were co-transfected with gB, along with the FL, N-terminal or C-terminal FBXO2 constructs. 48 hrs later, the glycosylated proteins were enriched by Con A agarose pull-down, and the bound proteins and total cell lysates were immunoblotted with anti-FLAG and anti-Myc antibodies. (B) FBXO2 did not affect the total or glycosylated levels of the glycosylation-defective 7NQ gB mutant. The experiments were conducted as in (A) . (C) CNE2 cells stably expressing gB were transfected with three siRNAs targeting FBXO2 or a scramble control siRNA, and 72 h later, the cells were harvested and subjected to Con A pull-down and WB. (D) Effects of MG132 and bafilomycin A1 on the levels of total and glycosylated gB. (E) FBXO2 ubiquitinates gB in vivo . HEK293T cells were transfected with His-ubiquitin (Ub), gB-SFB and Myc-FBXO2 or empty vector. The cells were treated with or without 20 μM MG132 for 6 h before harvest. 48 hrs post-transfection, the cells were lysed in 6 M guanidine-HCl buffer, the His-tagged ubiquitinated proteins were enriched by Ni-NTA (nickel-nitrilotriacetic acid) pull-down, and the bound proteins were eluted by SDS loading buffer and immunoblotted with antibodies as indicated. (F) HEK293T cells stably expressing gB were transfected with empty vector or Myc-FBXO2, and 36 h later the cells were treated with 50 μg/mL cycloheximide (CHX) to block protein synthesis and collected at the indicated time points. (top) Total cell lysates were analyzed by WB; (bottom) the degradation of gB was calculated by determining the relative quantification of gB from WB results. The mean value for vector-transfected cells at 0 h was normalized to a relative protein level of 100% (n = 3).

    Techniques Used: Transfection, Construct, Mutagenesis, Stable Transfection, Expressing, Western Blot, In Vivo, Plasmid Preparation, Blocking Assay

    4) Product Images from "Transcriptomic analyses reveal comprehensive responses of insect hemocytes to mycopathogen Beauveria bassiana, and fungal virulence-related cell wall protein assists pathogen to evade host cellular defense"

    Article Title: Transcriptomic analyses reveal comprehensive responses of insect hemocytes to mycopathogen Beauveria bassiana, and fungal virulence-related cell wall protein assists pathogen to evade host cellular defense

    Journal: Virulence

    doi: 10.1080/21505594.2020.1827886

    BbCwp protects fungus from host recognition. (a) Disruption of BbCwp resulted in an enhanced hemocyte encapsulation. Fungal strain was labeled by expressing the mCherry gene. Conidial suspension (5 µl, 10 5 conidia/ml) was injected into host. After an incubation of 3 h at 25°C, hemocyte encapsulation was examined under a fluorescence microscope. (b) Conidial lectin-binding pattern. Lectins included concanavalin A (ConA), Galanthus nivalis lectin (GNL), peanut agglutinin (PNA), and wheat germ agglutinin (WGA). Δ BbCwp mutant strain displayed a significant increase in fluorescence intensity of WGA. (c) Relative expression levels of β-1, 3-glucan recognition protein genes ( βGRP ). In G. mellonella , there are 11 βGRP genes. Comparative analyses between the wild type/Δ BbCwp were performed at different time points during infection process. Gene disruption led to a significant up-regulation of all tested genes at 1 d post infection. Tukey’s HSD was used to determine the statistical significance using a threshold of P
    Figure Legend Snippet: BbCwp protects fungus from host recognition. (a) Disruption of BbCwp resulted in an enhanced hemocyte encapsulation. Fungal strain was labeled by expressing the mCherry gene. Conidial suspension (5 µl, 10 5 conidia/ml) was injected into host. After an incubation of 3 h at 25°C, hemocyte encapsulation was examined under a fluorescence microscope. (b) Conidial lectin-binding pattern. Lectins included concanavalin A (ConA), Galanthus nivalis lectin (GNL), peanut agglutinin (PNA), and wheat germ agglutinin (WGA). Δ BbCwp mutant strain displayed a significant increase in fluorescence intensity of WGA. (c) Relative expression levels of β-1, 3-glucan recognition protein genes ( βGRP ). In G. mellonella , there are 11 βGRP genes. Comparative analyses between the wild type/Δ BbCwp were performed at different time points during infection process. Gene disruption led to a significant up-regulation of all tested genes at 1 d post infection. Tukey’s HSD was used to determine the statistical significance using a threshold of P

    Techniques Used: Labeling, Expressing, Injection, Incubation, Fluorescence, Microscopy, Binding Assay, Whole Genome Amplification, Mutagenesis, Infection

    5) Product Images from "Morniga-G, a T/Tn-Specific Lectin, Induces Leukemic Cell Death via Caspase and DR5 Receptor-Dependent Pathways"

    Article Title: Morniga-G, a T/Tn-Specific Lectin, Induces Leukemic Cell Death via Caspase and DR5 Receptor-Dependent Pathways

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms20010230

    Morniga-G activates healthy human lymphocytes and induces cell death in leukemia cells. PBMCs from healthy donors were cultured for 3 days: ( A ) in the presence of increasing concentrations of Morniga-M (MorM), Morniga-G (MorG), and Con A and proliferative index (from the [ 3 H]-thymidine incorporation) was calculated; and ( B ) in the presence of lectins at concentrations triggering maximal proliferation. CD25 expression was evaluated using flow cytometry, in CD3+ T lymphocytes, in CD19+ CD3- B lymphocytes, and in CD56+ CD3- NK lymphocytes. Values are means ± SD of three experiments performed with three to four different healthy donors. ( C ) Resting PBMCs and Jurkat A3 leukemic cells were incubated with anti-Tn mouse monoclonal antibody + PE-conjugated anti-mouse antibody (αTn + antiα-PE) or FITC-conjugated Morniga G (MorG-FITC) and analyzed using cytofluorimetry. Healthy peripheral lymphocytes (PBLs) were analyzed in a gate corresponding to lymphocytes as defined by the size and granularity parameters. Autofluorescence: purple histograms, dashed green histogram: fluorescent positive cells. ( D ) PBMCs of healthy donors and Jurkat A3 leukemic cells were cultured for 24 h with different concentrations of MorG, then cell viability was evaluated in 3-(4,5-dimethylthiazol)-2-5-diphenyl terazolium bromide MTT reduction assays (mean values ± SD of four independent experiments).
    Figure Legend Snippet: Morniga-G activates healthy human lymphocytes and induces cell death in leukemia cells. PBMCs from healthy donors were cultured for 3 days: ( A ) in the presence of increasing concentrations of Morniga-M (MorM), Morniga-G (MorG), and Con A and proliferative index (from the [ 3 H]-thymidine incorporation) was calculated; and ( B ) in the presence of lectins at concentrations triggering maximal proliferation. CD25 expression was evaluated using flow cytometry, in CD3+ T lymphocytes, in CD19+ CD3- B lymphocytes, and in CD56+ CD3- NK lymphocytes. Values are means ± SD of three experiments performed with three to four different healthy donors. ( C ) Resting PBMCs and Jurkat A3 leukemic cells were incubated with anti-Tn mouse monoclonal antibody + PE-conjugated anti-mouse antibody (αTn + antiα-PE) or FITC-conjugated Morniga G (MorG-FITC) and analyzed using cytofluorimetry. Healthy peripheral lymphocytes (PBLs) were analyzed in a gate corresponding to lymphocytes as defined by the size and granularity parameters. Autofluorescence: purple histograms, dashed green histogram: fluorescent positive cells. ( D ) PBMCs of healthy donors and Jurkat A3 leukemic cells were cultured for 24 h with different concentrations of MorG, then cell viability was evaluated in 3-(4,5-dimethylthiazol)-2-5-diphenyl terazolium bromide MTT reduction assays (mean values ± SD of four independent experiments).

    Techniques Used: Cell Culture, Expressing, Flow Cytometry, Cytometry, Incubation, MTT Assay

    6) Product Images from "Signal Peptide-Binding Drug as a Selective Inhibitor of Co-Translational Protein Translocation"

    Article Title: Signal Peptide-Binding Drug as a Selective Inhibitor of Co-Translational Protein Translocation

    Journal: PLoS Biology

    doi: 10.1371/journal.pbio.1002011

    CADA specifically inhibits the biogenesis of human CD4. (A, B) CADA inhibits the biosynthesis of CD4. CD4 + .CHO cells were washed and kept in methionine and cysteine-free medium in the presence or absence of 16 µM CADA for 45 min before exposure to [ 35 S]methionine/cysteine (Met/Cys) for 30 min. Pulsed-labelled cells were then washed, lysed, and analyzed directly (A) or incubated in normal medium for up to 4 h (chase) in the presence or absence of 16 µM CADA (B). At specified time points cell lysates were immunoprecipitated for CD4. The flow through fraction (FT) of the CD4-immunoprecipitated samples is also presented. Note that the weaker CD4 bands in the control samples at longer chase time points are the result of the high turnover of hCD4 in CHO cells. Molecular mass is in kDa. (C–F) CD4 negative and stably CD4-YFP transfected CHO cells were pretreated with CADA (5 µM) or DMSO for 1 h before starvation in Met/Cys free medium with CADA, DMSO, or 50 µg/ml CHX. Cells were pulsed for 30 min, washed, and incubated in fresh medium without serum for 90 min. After collection of supernatant proteins (Media) cells were first permeabilized with digitonin buffer to obtain the cytosolic cell fraction before lysis in NP-40 buffer to collect the membrane proteins. Membrane fractions were further incubated with Concanavalin A (ConA) agarose beads (Glycosylated). Molecular mass is in kDa. (D) Quantification of 35 S incorporation in (C) by scintillation counting ( n = 4). NS, not significant; * p
    Figure Legend Snippet: CADA specifically inhibits the biogenesis of human CD4. (A, B) CADA inhibits the biosynthesis of CD4. CD4 + .CHO cells were washed and kept in methionine and cysteine-free medium in the presence or absence of 16 µM CADA for 45 min before exposure to [ 35 S]methionine/cysteine (Met/Cys) for 30 min. Pulsed-labelled cells were then washed, lysed, and analyzed directly (A) or incubated in normal medium for up to 4 h (chase) in the presence or absence of 16 µM CADA (B). At specified time points cell lysates were immunoprecipitated for CD4. The flow through fraction (FT) of the CD4-immunoprecipitated samples is also presented. Note that the weaker CD4 bands in the control samples at longer chase time points are the result of the high turnover of hCD4 in CHO cells. Molecular mass is in kDa. (C–F) CD4 negative and stably CD4-YFP transfected CHO cells were pretreated with CADA (5 µM) or DMSO for 1 h before starvation in Met/Cys free medium with CADA, DMSO, or 50 µg/ml CHX. Cells were pulsed for 30 min, washed, and incubated in fresh medium without serum for 90 min. After collection of supernatant proteins (Media) cells were first permeabilized with digitonin buffer to obtain the cytosolic cell fraction before lysis in NP-40 buffer to collect the membrane proteins. Membrane fractions were further incubated with Concanavalin A (ConA) agarose beads (Glycosylated). Molecular mass is in kDa. (D) Quantification of 35 S incorporation in (C) by scintillation counting ( n = 4). NS, not significant; * p

    Techniques Used: Incubation, Immunoprecipitation, Flow Cytometry, Stable Transfection, Transfection, Lysis

    7) Product Images from "Rapid CB1 cannabinoid receptor desensitization defines the time course of ERK1/2 MAP kinase signaling"

    Article Title: Rapid CB1 cannabinoid receptor desensitization defines the time course of ERK1/2 MAP kinase signaling

    Journal: Neuropharmacology

    doi: 10.1016/j.neuropharm.2007.06.005

    S426A/S430A CB 1 receptor internalization and pharmacological blockade of CB 1 receptor internalization with Concanavalin A
    Figure Legend Snippet: S426A/S430A CB 1 receptor internalization and pharmacological blockade of CB 1 receptor internalization with Concanavalin A

    Techniques Used:

    8) Product Images from "Role of IL-6 in Angiotensin II-Induced Retinal Vascular Inflammation"

    Article Title: Role of IL-6 in Angiotensin II-Induced Retinal Vascular Inflammation

    Journal: Investigative Ophthalmology & Visual Science

    doi: 10.1167/iovs.09-3375

    Suppression of angiotensin II–induced increases in retinal vascular leukostasis in IL-6–deficient mice. ( A ) Flatmount images of concanavalin A–labeled retinas showing adherent leukocytes ( arrows ) within the retinal vessels of wild-type
    Figure Legend Snippet: Suppression of angiotensin II–induced increases in retinal vascular leukostasis in IL-6–deficient mice. ( A ) Flatmount images of concanavalin A–labeled retinas showing adherent leukocytes ( arrows ) within the retinal vessels of wild-type

    Techniques Used: Mouse Assay, Labeling

    IL-6 induced leukostasis in both wild-type and IL-6–deficient mice. ( A ) Flatmount images of concanavalin A–labeled retinas showing adherent leukocytes ( arrows ) within the retinal vessels of wild-type (WT) and IL-6–deficient (IL-6ko)
    Figure Legend Snippet: IL-6 induced leukostasis in both wild-type and IL-6–deficient mice. ( A ) Flatmount images of concanavalin A–labeled retinas showing adherent leukocytes ( arrows ) within the retinal vessels of wild-type (WT) and IL-6–deficient (IL-6ko)

    Techniques Used: Mouse Assay, Labeling

    9) Product Images from "Glycoprofiling as a novel tool in serological assays of systemic sclerosis: A comparative study with three bioanalytical methods"

    Article Title: Glycoprofiling as a novel tool in serological assays of systemic sclerosis: A comparative study with three bioanalytical methods

    Journal: Analytica chimica acta

    doi: 10.1016/j.aca.2014.10.029

    AFM images (1x1 μm) of unmodified microarray slide (upper image with R q =0.5 nm) and the same slide after the sample spotting and incubation with a lectin (bottom image with R q =2.4 nm). Isolated islets of the proteins (INV, Con A and streptavidin
    Figure Legend Snippet: AFM images (1x1 μm) of unmodified microarray slide (upper image with R q =0.5 nm) and the same slide after the sample spotting and incubation with a lectin (bottom image with R q =2.4 nm). Isolated islets of the proteins (INV, Con A and streptavidin

    Techniques Used: Microarray, Incubation, Isolation

    Related Articles

    Incubation:

    Article Title: Signal Peptide-Binding Drug as a Selective Inhibitor of Co-Translational Protein Translocation
    Article Snippet: Permeabilized cells were then washed in digitonin buffer and further lysed in ice-cold lysis buffer (25 mM Tris, 150 mM NaCl, 1 mM EDTA, 1% NP-40, 5% glycerol, pH 7.4, supplemented with 0.4 µM PMSF and protease inhibitor cocktail). .. To isolate glycosylated proteins, total cell lysates or digitonin-resistant membrane fractions were further incubated with Concanavalin A (Vector Laboratories) agarose beads overnight at 4°C by gentle rotation. .. Cell-Free Translation Full length cDNAs and truncated CD4-pPL nascent chains generated by PCR were transcribed in vitro using T7 RNA polymerase, and translated in rabbit reticulocyte lysate (Promega) in the presence of [35 S]methionine (Perkin Elmer).

    Article Title: Complete B Cell Deficiency Reduces Allograft Inflammation and Intragraft Macrophages a Rat Kidney Transplant Model
    Article Snippet: .. For IFN-γ ELISPOT assay, splenocytes were incubated overnight at 37° C with media or the stimulant Concanavalin A (final concentration 10 μg/mL, Vector Labs). .. After incubation, plates were washed and IFN-γ biotinylated antibody was added (R & D Systems).

    other:

    Article Title: Rapid CB1 cannabinoid receptor desensitization defines the time course of ERK1/2 MAP kinase signaling
    Article Snippet: Concanavalin A, was purchased from Vector Laboratories (Burlingame, CA).

    Enzyme-linked Immunospot:

    Article Title: Complete B Cell Deficiency Reduces Allograft Inflammation and Intragraft Macrophages a Rat Kidney Transplant Model
    Article Snippet: .. For IFN-γ ELISPOT assay, splenocytes were incubated overnight at 37° C with media or the stimulant Concanavalin A (final concentration 10 μg/mL, Vector Labs). .. After incubation, plates were washed and IFN-γ biotinylated antibody was added (R & D Systems).

    Concentration Assay:

    Article Title: Complete B Cell Deficiency Reduces Allograft Inflammation and Intragraft Macrophages a Rat Kidney Transplant Model
    Article Snippet: .. For IFN-γ ELISPOT assay, splenocytes were incubated overnight at 37° C with media or the stimulant Concanavalin A (final concentration 10 μg/mL, Vector Labs). .. After incubation, plates were washed and IFN-γ biotinylated antibody was added (R & D Systems).

    Labeling:

    Article Title: Role of IL-6 in Angiotensin II-Induced Retinal Vascular Inflammation
    Article Snippet: The samples were boiled in sodium dodecyl sulfate sample buffer (100°C, 10 minutes), to elute the proteins, which were then electrophoresed in 4% to 20% Tris-HCl gradient gels (Bio-Rad Laboratories), transferred to nitrocellulose membranes, and probed with anti-VEGF antibody (Oncogene, San Diego, CA). .. Retinal leukostasis was assayed by labeling the adherent leukocytes with concanavalin A (Vector Laboratories, Burlingame, CA), according to a published method. ..

    Article Title: Adiponectin Suppresses Pathological Microvessel Formation in Retina Through Modulation of Tumor Necrosis Factor-α Expression
    Article Snippet: Recombinant mouse adiponectin protein (3.0 μ g/g body weight) (n=9 to 10) or vehicle (n=9) was intraperitoneally injected into WT and APN-KO mice at the day of ischemic induction (P12) or P13 and daily until P17. .. The retinal vasculature and adherent leukocytes were labeled with FITC-conjugated concanavalin A (Con A) lectin (Vector laboratory)., In brief, mice were perfused with PBS to remove the erythrocytes and nonadherent leukocytes in the retinal vasculature and then perfused with FITC–Con A lectin, followed by perfusion with PBS to remove unbound Con A lectin (n=12 to 20 for each experiment). ..

    Mouse Assay:

    Article Title: Adiponectin Suppresses Pathological Microvessel Formation in Retina Through Modulation of Tumor Necrosis Factor-α Expression
    Article Snippet: Recombinant mouse adiponectin protein (3.0 μ g/g body weight) (n=9 to 10) or vehicle (n=9) was intraperitoneally injected into WT and APN-KO mice at the day of ischemic induction (P12) or P13 and daily until P17. .. The retinal vasculature and adherent leukocytes were labeled with FITC-conjugated concanavalin A (Con A) lectin (Vector laboratory)., In brief, mice were perfused with PBS to remove the erythrocytes and nonadherent leukocytes in the retinal vasculature and then perfused with FITC–Con A lectin, followed by perfusion with PBS to remove unbound Con A lectin (n=12 to 20 for each experiment). ..

    Article Title: BTBR ob/ob mouse model of type 2 diabetes exhibits early loss of retinal function and retinal inflammation followed by late vascular changes
    Article Snippet: .. After inducing deep anaesthesia with 200 mg/kg pentobarbital sodium (Euthatal, Merial, Harlow, UK), the mice were cardiac perfused with rhodamine-conjugated concanavalin A (Rho-Con A; Vector Laboratories), followed by PBS. ..

    Staining:

    Article Title: Ischaemia-induced retinal neovascularisation and diabetic retinopathy in mice with conditional knockout of hypoxia-inducible factor-1 in retinal Müller cells
    Article Snippet: Briefly, mice were perfused through the left ventricle to remove circulating leucocytes in blood vessels. .. The adherent leucocytes in the vasculature were stained by perfusion with FITC-conjugated concanavalin-A (40 μg/ml; Vector Laboratories) and counted. .. The quantitative data were analysed and compared with those from wild-type mice using unpaired Student’s t test (two-tailed test).

    Whole Genome Amplification:

    Article Title: Glycoprofiling as a novel tool in serological assays of systemic sclerosis: A comparative study with three bioanalytical methods
    Article Snippet: Phosphate buffer saline tablets (PBST) were from Merck (Slovakia). .. Eight biotinylated lectins Aleuria aurantia lectin (AAL) , Lens culinaris agglutinin (LCA) , Maackia amurensis lectin (MAL) , Phaseolus vulgaris agglutinin (PHAE) , Ricinus communis agglutinin and Sambucus nigra agglutinin, concanavalin A and wheat-germ agglutinin (WGA); and avidin-peroxidase (AV-HRP) were purchased from Vector Laboratories (USA). .. CF555-streptavidin fluorescent label was purchased from Biotium (USA).

    Avidin-Biotin Assay:

    Article Title: Glycoprofiling as a novel tool in serological assays of systemic sclerosis: A comparative study with three bioanalytical methods
    Article Snippet: Phosphate buffer saline tablets (PBST) were from Merck (Slovakia). .. Eight biotinylated lectins Aleuria aurantia lectin (AAL) , Lens culinaris agglutinin (LCA) , Maackia amurensis lectin (MAL) , Phaseolus vulgaris agglutinin (PHAE) , Ricinus communis agglutinin and Sambucus nigra agglutinin, concanavalin A and wheat-germ agglutinin (WGA); and avidin-peroxidase (AV-HRP) were purchased from Vector Laboratories (USA). .. CF555-streptavidin fluorescent label was purchased from Biotium (USA).

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  • 93
    Vector Laboratories vascular label fitc concanavalin a
    Epithelial debridement induces rapid and consistent corneal angiogenesis and inflammation by 3 days. A , representative <t>FITC-concanavalin</t> A-injected corneal flat mounts at various times over 20 days following epithelial debridement. B , quantification of total vascular area per cornea normalized to control (undebrided) limbal vessel areas ( n = 10 corneas/group). Error bars indicate S.E. NV Area , neovascular area. C , H E-stained corneal sections showing the progression of re-epithelialization over a matter of days. The images are all oriented with the limbus to the left ( L ) and the central cornea to the right ( C ). Note the repair epithelium at the wound edge ( arrowhead ) accompanied by underlying inflammatory infiltrates. By day 7, the cornea completely resurfaced with a stratified epithelium ( E ) but includes the presence of new shallow stromal vessels ( S ) ( arrows ). The presence of inflammatory cells was reduced by this time (20×).
    Vascular Label Fitc Concanavalin A, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vascular label fitc concanavalin a/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    vascular label fitc concanavalin a - by Bioz Stars, 2021-03
    93/100 stars
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    94
    Vector Laboratories fitc conjugated concanavalin a
    Exacerbated retinal leukostasis in APN-KO mice. A, Representative photographs of retinal vasculature and adherent leukocytes (arrows) labeled with <t>FITC-conjugated</t> Con A lectin in WT (left) and APN-KO (right) mice at P15. B, Quantitative analysis of leukocyte
    Fitc Conjugated Concanavalin A, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fitc conjugated concanavalin a/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fitc conjugated concanavalin a - by Bioz Stars, 2021-03
    94/100 stars
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    93
    Vector Laboratories agarose bound lectins
    Schematic of the work flow implemented in the study. Synovial fluid samples were collected from 20 RA patients. Equal amounts of proteins were taken from all samples and pooled together followed by two sets of protein enrichment: glycoprotein enrichment using multiple <t>lectins</t> and depletion of abundant proteins using MARS14. The enriched proteins were thereafter taken for fractionation and trypsin digestion. The fractionated tryptic peptides were then analyzed in a high resolution mass spectrometer. The data acquired were processed and subsequently analyzed using appropriate software
    Agarose Bound Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/agarose bound lectins/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    agarose bound lectins - by Bioz Stars, 2021-03
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    Image Search Results


    Epithelial debridement induces rapid and consistent corneal angiogenesis and inflammation by 3 days. A , representative FITC-concanavalin A-injected corneal flat mounts at various times over 20 days following epithelial debridement. B , quantification of total vascular area per cornea normalized to control (undebrided) limbal vessel areas ( n = 10 corneas/group). Error bars indicate S.E. NV Area , neovascular area. C , H E-stained corneal sections showing the progression of re-epithelialization over a matter of days. The images are all oriented with the limbus to the left ( L ) and the central cornea to the right ( C ). Note the repair epithelium at the wound edge ( arrowhead ) accompanied by underlying inflammatory infiltrates. By day 7, the cornea completely resurfaced with a stratified epithelium ( E ) but includes the presence of new shallow stromal vessels ( S ) ( arrows ). The presence of inflammatory cells was reduced by this time (20×).

    Journal: The Journal of Biological Chemistry

    Article Title: Pharmacologic Uncoupling of Angiogenesis and Inflammation during Initiation of Pathological Corneal Neovascularization *

    doi: 10.1074/jbc.M111.294967

    Figure Lengend Snippet: Epithelial debridement induces rapid and consistent corneal angiogenesis and inflammation by 3 days. A , representative FITC-concanavalin A-injected corneal flat mounts at various times over 20 days following epithelial debridement. B , quantification of total vascular area per cornea normalized to control (undebrided) limbal vessel areas ( n = 10 corneas/group). Error bars indicate S.E. NV Area , neovascular area. C , H E-stained corneal sections showing the progression of re-epithelialization over a matter of days. The images are all oriented with the limbus to the left ( L ) and the central cornea to the right ( C ). Note the repair epithelium at the wound edge ( arrowhead ) accompanied by underlying inflammatory infiltrates. By day 7, the cornea completely resurfaced with a stratified epithelium ( E ) but includes the presence of new shallow stromal vessels ( S ) ( arrows ). The presence of inflammatory cells was reduced by this time (20×).

    Article Snippet: Prior to euthanasia, all animals were injected with 100 μl of the vascular label FITC-concanavalin A (Vector Laboratories, Burlingame, CA) intravenously.

    Techniques: Injection, Staining

    Exacerbated retinal leukostasis in APN-KO mice. A, Representative photographs of retinal vasculature and adherent leukocytes (arrows) labeled with FITC-conjugated Con A lectin in WT (left) and APN-KO (right) mice at P15. B, Quantitative analysis of leukocyte

    Journal: Circulation research

    Article Title: Adiponectin Suppresses Pathological Microvessel Formation in Retina Through Modulation of Tumor Necrosis Factor-α Expression

    doi: 10.1161/CIRCRESAHA.109.194506

    Figure Lengend Snippet: Exacerbated retinal leukostasis in APN-KO mice. A, Representative photographs of retinal vasculature and adherent leukocytes (arrows) labeled with FITC-conjugated Con A lectin in WT (left) and APN-KO (right) mice at P15. B, Quantitative analysis of leukocyte

    Article Snippet: The retinal vasculature and adherent leukocytes were labeled with FITC-conjugated concanavalin A (Con A) lectin (Vector laboratory)., In brief, mice were perfused with PBS to remove the erythrocytes and nonadherent leukocytes in the retinal vasculature and then perfused with FITC–Con A lectin, followed by perfusion with PBS to remove unbound Con A lectin (n=12 to 20 for each experiment).

    Techniques: Mouse Assay, Labeling

    Schematic of the work flow implemented in the study. Synovial fluid samples were collected from 20 RA patients. Equal amounts of proteins were taken from all samples and pooled together followed by two sets of protein enrichment: glycoprotein enrichment using multiple lectins and depletion of abundant proteins using MARS14. The enriched proteins were thereafter taken for fractionation and trypsin digestion. The fractionated tryptic peptides were then analyzed in a high resolution mass spectrometer. The data acquired were processed and subsequently analyzed using appropriate software

    Journal: Clinical Proteomics

    Article Title: Synovial fluid proteome in rheumatoid arthritis

    doi: 10.1186/s12014-016-9113-1

    Figure Lengend Snippet: Schematic of the work flow implemented in the study. Synovial fluid samples were collected from 20 RA patients. Equal amounts of proteins were taken from all samples and pooled together followed by two sets of protein enrichment: glycoprotein enrichment using multiple lectins and depletion of abundant proteins using MARS14. The enriched proteins were thereafter taken for fractionation and trypsin digestion. The fractionated tryptic peptides were then analyzed in a high resolution mass spectrometer. The data acquired were processed and subsequently analyzed using appropriate software

    Article Snippet: Multiple lectin affinity chromatography Glycoprotein enrichment from 20 pooled synovial fluid samples containing 2.5 mg proteins was carried out by using a mixture of three agarose-bound lectins, Wheat Germ Agglutinin, Concanavalin A and Jacalin (Vector laboratories, USA), as described previously by our group [ , ].

    Techniques: Flow Cytometry, Protein Enrichment, Fractionation, Mass Spectrometry, Software

    Lectin pull-down assays for wild-type ASBT and glycosylation deficient N10Q mutant ASBT protein samples. Equal amounts protein from total cellular lysate were incubated with agarose-bound lectins (4°C) overnight along with protease inhibitor cocktail. After washing with RIPA buffer, bound samples were eluted by boiling with 2X Laemmli buffer and used for Western blotting with anti-V5 antibody. Top panel shows the pull-down fractions and bottom panel shows unbound proteins in the supernatant.

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: N-glycosylation is essential for ileal ASBT function and protection against proteases

    doi: 10.1152/ajpcell.00023.2015

    Figure Lengend Snippet: Lectin pull-down assays for wild-type ASBT and glycosylation deficient N10Q mutant ASBT protein samples. Equal amounts protein from total cellular lysate were incubated with agarose-bound lectins (4°C) overnight along with protease inhibitor cocktail. After washing with RIPA buffer, bound samples were eluted by boiling with 2X Laemmli buffer and used for Western blotting with anti-V5 antibody. Top panel shows the pull-down fractions and bottom panel shows unbound proteins in the supernatant.

    Article Snippet: Agarose-bound lectins were purchased from Vector Laboratories (Burlingame, CA).

    Techniques: Mutagenesis, Incubation, Protease Inhibitor, Western Blot