lentil lectin agarose Search Results


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  • 88
    Vector Laboratories agarose bound lens culinaris agglutinin
    Agarose Bound Lens Culinaris Agglutinin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/agarose bound lens culinaris agglutinin/product/Vector Laboratories
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    90
    Millipore lentil lectin sepharose 4b
    Lentil Lectin Sepharose 4b, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lentil lectin sepharose 4b/product/Millipore
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    88
    GE Healthcare lentil lectin sepharose 4b
    Transient expression of various sF constructs. 293 T cells were transfected with various sF constructs in the promoter modified pcDNA 3.1 Hygro (+) vector. Cell lysate and supernatant were precipitated with S-protein <t>agarose.</t> Western blot detection was
    Lentil Lectin Sepharose 4b, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lentil lectin sepharose 4b/product/GE Healthcare
    Average 88 stars, based on 33 article reviews
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    94
    Vector Laboratories lens culinaris agglutinin lca
    Transient expression of various sF constructs. 293 T cells were transfected with various sF constructs in the promoter modified pcDNA 3.1 Hygro (+) vector. Cell lysate and supernatant were precipitated with S-protein <t>agarose.</t> Western blot detection was
    Lens Culinaris Agglutinin Lca, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lens culinaris agglutinin lca/product/Vector Laboratories
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    85
    GE Healthcare lentil lectin sepharose 4b beads
    Site-directed mutagenesis and <t>lectin</t> affinity purification analyses reveal α 1D -AR is dually glycosylated at N65 and N82. ( A ) Lysate from HEK293 cells expressing WT SNAP-α 1D ( input ) was incubated with lentil lectin <t>sepharose</t> beads to isolate glycosylated proteins. Bound protein was eluted with methyl-α-D-mannopyranoside ( bound ), and analyzed using PAGE NIR. SNAP-α 1D monomers (►) and higher order oligomers, as well as the previously described N-terminal cleavage product, are present in the elutant. ( B ) Schematic and ( C ) PAGE NIR of HEK293 cell lysate expressing WT, single glycosylation mutants (N65Q and N82Q), and double glycosylation mutant (NQQ) SNAP-α 1D species. ( D ) HEK293 cells expressing WT SNAP-α 1D were incubated for 16 hr with vehicle (−) or tunicamycin (TUN, +), and analyzed with PAGE NIR. A signal at 43 kDa was observed in the tunicamycin treated samples (○). ( E ) PAGE NIR of HEK293 cell lysate transfected with N-terminal SNAP-epitope ( λ = 800 nm, green ) and C-terminal CLIP-epitope ( λ = 700 nm, red ) dual tagged WT (S-WT-C) and NQQ (S-NQQ-C) α 1D -AR constructs. ( F,I ) PAGE NIR of HEK293 cell lysate expressing S-WT-C or ( G,J ) S-NQQ-C following 24 hr bortezomib (BTZ) ( F,G ) or protease inhibitor (PI) treatment ( I,J ). ( H ) Quantitation of signals from F and G normalized to vehicle. ( K ) Quantitation of fluorescent signals from I and J normalized to vehicle. All gels are representative images from n = 3 experiments. For F and G, data are represented as mean ± SEM; Unpaired t tests, ***p
    Lentil Lectin Sepharose 4b Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lentil lectin sepharose 4b beads/product/GE Healthcare
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    92
    Millipore lens culinaris lectin
    Site-directed mutagenesis and <t>lectin</t> affinity purification analyses reveal α 1D -AR is dually glycosylated at N65 and N82. ( A ) Lysate from HEK293 cells expressing WT SNAP-α 1D ( input ) was incubated with lentil lectin <t>sepharose</t> beads to isolate glycosylated proteins. Bound protein was eluted with methyl-α-D-mannopyranoside ( bound ), and analyzed using PAGE NIR. SNAP-α 1D monomers (►) and higher order oligomers, as well as the previously described N-terminal cleavage product, are present in the elutant. ( B ) Schematic and ( C ) PAGE NIR of HEK293 cell lysate expressing WT, single glycosylation mutants (N65Q and N82Q), and double glycosylation mutant (NQQ) SNAP-α 1D species. ( D ) HEK293 cells expressing WT SNAP-α 1D were incubated for 16 hr with vehicle (−) or tunicamycin (TUN, +), and analyzed with PAGE NIR. A signal at 43 kDa was observed in the tunicamycin treated samples (○). ( E ) PAGE NIR of HEK293 cell lysate transfected with N-terminal SNAP-epitope ( λ = 800 nm, green ) and C-terminal CLIP-epitope ( λ = 700 nm, red ) dual tagged WT (S-WT-C) and NQQ (S-NQQ-C) α 1D -AR constructs. ( F,I ) PAGE NIR of HEK293 cell lysate expressing S-WT-C or ( G,J ) S-NQQ-C following 24 hr bortezomib (BTZ) ( F,G ) or protease inhibitor (PI) treatment ( I,J ). ( H ) Quantitation of signals from F and G normalized to vehicle. ( K ) Quantitation of fluorescent signals from I and J normalized to vehicle. All gels are representative images from n = 3 experiments. For F and G, data are represented as mean ± SEM; Unpaired t tests, ***p
    Lens Culinaris Lectin, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lens culinaris lectin/product/Millipore
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    85
    GE Healthcare lentil lectin sepharose 4b column
    Site-directed mutagenesis and <t>lectin</t> affinity purification analyses reveal α 1D -AR is dually glycosylated at N65 and N82. ( A ) Lysate from HEK293 cells expressing WT SNAP-α 1D ( input ) was incubated with lentil lectin <t>sepharose</t> beads to isolate glycosylated proteins. Bound protein was eluted with methyl-α-D-mannopyranoside ( bound ), and analyzed using PAGE NIR. SNAP-α 1D monomers (►) and higher order oligomers, as well as the previously described N-terminal cleavage product, are present in the elutant. ( B ) Schematic and ( C ) PAGE NIR of HEK293 cell lysate expressing WT, single glycosylation mutants (N65Q and N82Q), and double glycosylation mutant (NQQ) SNAP-α 1D species. ( D ) HEK293 cells expressing WT SNAP-α 1D were incubated for 16 hr with vehicle (−) or tunicamycin (TUN, +), and analyzed with PAGE NIR. A signal at 43 kDa was observed in the tunicamycin treated samples (○). ( E ) PAGE NIR of HEK293 cell lysate transfected with N-terminal SNAP-epitope ( λ = 800 nm, green ) and C-terminal CLIP-epitope ( λ = 700 nm, red ) dual tagged WT (S-WT-C) and NQQ (S-NQQ-C) α 1D -AR constructs. ( F,I ) PAGE NIR of HEK293 cell lysate expressing S-WT-C or ( G,J ) S-NQQ-C following 24 hr bortezomib (BTZ) ( F,G ) or protease inhibitor (PI) treatment ( I,J ). ( H ) Quantitation of signals from F and G normalized to vehicle. ( K ) Quantitation of fluorescent signals from I and J normalized to vehicle. All gels are representative images from n = 3 experiments. For F and G, data are represented as mean ± SEM; Unpaired t tests, ***p
    Lentil Lectin Sepharose 4b Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lentil lectin sepharose 4b column/product/GE Healthcare
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    Thermo Fisher lentil lectin coupled sepharose 4b
    Site-directed mutagenesis and <t>lectin</t> affinity purification analyses reveal α 1D -AR is dually glycosylated at N65 and N82. ( A ) Lysate from HEK293 cells expressing WT SNAP-α 1D ( input ) was incubated with lentil lectin <t>sepharose</t> beads to isolate glycosylated proteins. Bound protein was eluted with methyl-α-D-mannopyranoside ( bound ), and analyzed using PAGE NIR. SNAP-α 1D monomers (►) and higher order oligomers, as well as the previously described N-terminal cleavage product, are present in the elutant. ( B ) Schematic and ( C ) PAGE NIR of HEK293 cell lysate expressing WT, single glycosylation mutants (N65Q and N82Q), and double glycosylation mutant (NQQ) SNAP-α 1D species. ( D ) HEK293 cells expressing WT SNAP-α 1D were incubated for 16 hr with vehicle (−) or tunicamycin (TUN, +), and analyzed with PAGE NIR. A signal at 43 kDa was observed in the tunicamycin treated samples (○). ( E ) PAGE NIR of HEK293 cell lysate transfected with N-terminal SNAP-epitope ( λ = 800 nm, green ) and C-terminal CLIP-epitope ( λ = 700 nm, red ) dual tagged WT (S-WT-C) and NQQ (S-NQQ-C) α 1D -AR constructs. ( F,I ) PAGE NIR of HEK293 cell lysate expressing S-WT-C or ( G,J ) S-NQQ-C following 24 hr bortezomib (BTZ) ( F,G ) or protease inhibitor (PI) treatment ( I,J ). ( H ) Quantitation of signals from F and G normalized to vehicle. ( K ) Quantitation of fluorescent signals from I and J normalized to vehicle. All gels are representative images from n = 3 experiments. For F and G, data are represented as mean ± SEM; Unpaired t tests, ***p
    Lentil Lectin Coupled Sepharose 4b, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lentil lectin coupled sepharose 4b/product/Thermo Fisher
    Average 85 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    lentil lectin coupled sepharose 4b - by Bioz Stars, 2020-08
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    85
    GE Healthcare lentil lectin sepharose chromatography
    Site-directed mutagenesis and <t>lectin</t> affinity purification analyses reveal α 1D -AR is dually glycosylated at N65 and N82. ( A ) Lysate from HEK293 cells expressing WT SNAP-α 1D ( input ) was incubated with lentil lectin <t>sepharose</t> beads to isolate glycosylated proteins. Bound protein was eluted with methyl-α-D-mannopyranoside ( bound ), and analyzed using PAGE NIR. SNAP-α 1D monomers (►) and higher order oligomers, as well as the previously described N-terminal cleavage product, are present in the elutant. ( B ) Schematic and ( C ) PAGE NIR of HEK293 cell lysate expressing WT, single glycosylation mutants (N65Q and N82Q), and double glycosylation mutant (NQQ) SNAP-α 1D species. ( D ) HEK293 cells expressing WT SNAP-α 1D were incubated for 16 hr with vehicle (−) or tunicamycin (TUN, +), and analyzed with PAGE NIR. A signal at 43 kDa was observed in the tunicamycin treated samples (○). ( E ) PAGE NIR of HEK293 cell lysate transfected with N-terminal SNAP-epitope ( λ = 800 nm, green ) and C-terminal CLIP-epitope ( λ = 700 nm, red ) dual tagged WT (S-WT-C) and NQQ (S-NQQ-C) α 1D -AR constructs. ( F,I ) PAGE NIR of HEK293 cell lysate expressing S-WT-C or ( G,J ) S-NQQ-C following 24 hr bortezomib (BTZ) ( F,G ) or protease inhibitor (PI) treatment ( I,J ). ( H ) Quantitation of signals from F and G normalized to vehicle. ( K ) Quantitation of fluorescent signals from I and J normalized to vehicle. All gels are representative images from n = 3 experiments. For F and G, data are represented as mean ± SEM; Unpaired t tests, ***p
    Lentil Lectin Sepharose Chromatography, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lentil lectin sepharose chromatography/product/GE Healthcare
    Average 85 stars, based on 9 article reviews
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    85
    GE Healthcare lentil lectin affinity matrix
    Identification of <t>FLAG-tag</t> tyrosine-sulfation. <t>Lectin</t> purified TB-Hokkaido NA was incubated with different PTM-cleaving enzymes. The anti-FLAG WB is shown in Fig. 3 A. Addition of sulfatase made the FLAG tag accessible to the anti-FLAG mAb. Desulfation kinetics of Lectin/IEX-purified pN1/2009 NA using sulfatase type VIII (Abalone entrails) are shown in 3B. Activity of all 4 sulfatases tested was efficiently inhibited by the addition of vanadate-phenyl-Ester (3C). Fig. 3 D shows the negative linear mode MS of the sulfated control peptide CCK-8 at 1143.5 Da and its non-sulfated form at 1063.3 Da (−80 Da). The Thrombin cleaved FLAG tag was detected in its sulfated and non-sulfated form at a molecular weight of 1690.9 and 1611.1 Da (−80 Da), respectively. Fig. 3 E shows the same sample measured in positive linear mode. Only the non-sulfated peptides (−80 Da) were detected with an additional weight due to protonation (+1 Da). Fig. 3 F shows the WB of FLAG- and Lectin-purified NA (pN1/2009) detected with different anti-FLAG antibodies as well as the Coomassie stained gel of the same samples.
    Lentil Lectin Affinity Matrix, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lentil lectin affinity matrix/product/GE Healthcare
    Average 85 stars, based on 24 article reviews
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    Image Search Results


    Transient expression of various sF constructs. 293 T cells were transfected with various sF constructs in the promoter modified pcDNA 3.1 Hygro (+) vector. Cell lysate and supernatant were precipitated with S-protein agarose. Western blot detection was

    Journal: Methods in Molecular Biology (Clifton, N.j.)

    Article Title: Preparation of Recombinant Viral Glycoproteins for Novel and Therapeutic Antibody Discovery

    doi: 10.1007/978-1-59745-554-1_2

    Figure Lengend Snippet: Transient expression of various sF constructs. 293 T cells were transfected with various sF constructs in the promoter modified pcDNA 3.1 Hygro (+) vector. Cell lysate and supernatant were precipitated with S-protein agarose. Western blot detection was

    Article Snippet: Lentil lectin Sepharose™ 4B (GE Healthcare).

    Techniques: Expressing, Construct, Transfection, Modification, Plasmid Preparation, Western Blot

    SDS-PAGE followed by coomassie stain analysis of S-protein agarose purified HeV and NiV sF GCN. 0.5 μL and 1.0 μL of protein purified from DMEM supplemented by 10% calf serum (DMEM-10) and reduced serum medium (OptiMEM) was analyzed on

    Journal: Methods in Molecular Biology (Clifton, N.j.)

    Article Title: Preparation of Recombinant Viral Glycoproteins for Novel and Therapeutic Antibody Discovery

    doi: 10.1007/978-1-59745-554-1_2

    Figure Lengend Snippet: SDS-PAGE followed by coomassie stain analysis of S-protein agarose purified HeV and NiV sF GCN. 0.5 μL and 1.0 μL of protein purified from DMEM supplemented by 10% calf serum (DMEM-10) and reduced serum medium (OptiMEM) was analyzed on

    Article Snippet: Lentil lectin Sepharose™ 4B (GE Healthcare).

    Techniques: SDS Page, Staining, Purification

    Site-directed mutagenesis and lectin affinity purification analyses reveal α 1D -AR is dually glycosylated at N65 and N82. ( A ) Lysate from HEK293 cells expressing WT SNAP-α 1D ( input ) was incubated with lentil lectin sepharose beads to isolate glycosylated proteins. Bound protein was eluted with methyl-α-D-mannopyranoside ( bound ), and analyzed using PAGE NIR. SNAP-α 1D monomers (►) and higher order oligomers, as well as the previously described N-terminal cleavage product, are present in the elutant. ( B ) Schematic and ( C ) PAGE NIR of HEK293 cell lysate expressing WT, single glycosylation mutants (N65Q and N82Q), and double glycosylation mutant (NQQ) SNAP-α 1D species. ( D ) HEK293 cells expressing WT SNAP-α 1D were incubated for 16 hr with vehicle (−) or tunicamycin (TUN, +), and analyzed with PAGE NIR. A signal at 43 kDa was observed in the tunicamycin treated samples (○). ( E ) PAGE NIR of HEK293 cell lysate transfected with N-terminal SNAP-epitope ( λ = 800 nm, green ) and C-terminal CLIP-epitope ( λ = 700 nm, red ) dual tagged WT (S-WT-C) and NQQ (S-NQQ-C) α 1D -AR constructs. ( F,I ) PAGE NIR of HEK293 cell lysate expressing S-WT-C or ( G,J ) S-NQQ-C following 24 hr bortezomib (BTZ) ( F,G ) or protease inhibitor (PI) treatment ( I,J ). ( H ) Quantitation of signals from F and G normalized to vehicle. ( K ) Quantitation of fluorescent signals from I and J normalized to vehicle. All gels are representative images from n = 3 experiments. For F and G, data are represented as mean ± SEM; Unpaired t tests, ***p

    Journal: Scientific Reports

    Article Title: N-glycosylation of α1D-adrenergic receptor N-terminal domain is required for correct trafficking, function, and biogenesis

    doi: 10.1038/s41598-020-64102-4

    Figure Lengend Snippet: Site-directed mutagenesis and lectin affinity purification analyses reveal α 1D -AR is dually glycosylated at N65 and N82. ( A ) Lysate from HEK293 cells expressing WT SNAP-α 1D ( input ) was incubated with lentil lectin sepharose beads to isolate glycosylated proteins. Bound protein was eluted with methyl-α-D-mannopyranoside ( bound ), and analyzed using PAGE NIR. SNAP-α 1D monomers (►) and higher order oligomers, as well as the previously described N-terminal cleavage product, are present in the elutant. ( B ) Schematic and ( C ) PAGE NIR of HEK293 cell lysate expressing WT, single glycosylation mutants (N65Q and N82Q), and double glycosylation mutant (NQQ) SNAP-α 1D species. ( D ) HEK293 cells expressing WT SNAP-α 1D were incubated for 16 hr with vehicle (−) or tunicamycin (TUN, +), and analyzed with PAGE NIR. A signal at 43 kDa was observed in the tunicamycin treated samples (○). ( E ) PAGE NIR of HEK293 cell lysate transfected with N-terminal SNAP-epitope ( λ = 800 nm, green ) and C-terminal CLIP-epitope ( λ = 700 nm, red ) dual tagged WT (S-WT-C) and NQQ (S-NQQ-C) α 1D -AR constructs. ( F,I ) PAGE NIR of HEK293 cell lysate expressing S-WT-C or ( G,J ) S-NQQ-C following 24 hr bortezomib (BTZ) ( F,G ) or protease inhibitor (PI) treatment ( I,J ). ( H ) Quantitation of signals from F and G normalized to vehicle. ( K ) Quantitation of fluorescent signals from I and J normalized to vehicle. All gels are representative images from n = 3 experiments. For F and G, data are represented as mean ± SEM; Unpaired t tests, ***p

    Article Snippet: The soluble fraction was incubated with Lentil Lectin Sepharose 4B beads (GE Healthcare, Chicago, IL) and 1 μL of 25 μL BG-782 for 1 hr at room temperature.

    Techniques: Mutagenesis, Affinity Purification, Expressing, Incubation, Polyacrylamide Gel Electrophoresis, Transfection, Cross-linking Immunoprecipitation, Construct, Protease Inhibitor, Quantitation Assay

    Identification of FLAG-tag tyrosine-sulfation. Lectin purified TB-Hokkaido NA was incubated with different PTM-cleaving enzymes. The anti-FLAG WB is shown in Fig. 3 A. Addition of sulfatase made the FLAG tag accessible to the anti-FLAG mAb. Desulfation kinetics of Lectin/IEX-purified pN1/2009 NA using sulfatase type VIII (Abalone entrails) are shown in 3B. Activity of all 4 sulfatases tested was efficiently inhibited by the addition of vanadate-phenyl-Ester (3C). Fig. 3 D shows the negative linear mode MS of the sulfated control peptide CCK-8 at 1143.5 Da and its non-sulfated form at 1063.3 Da (−80 Da). The Thrombin cleaved FLAG tag was detected in its sulfated and non-sulfated form at a molecular weight of 1690.9 and 1611.1 Da (−80 Da), respectively. Fig. 3 E shows the same sample measured in positive linear mode. Only the non-sulfated peptides (−80 Da) were detected with an additional weight due to protonation (+1 Da). Fig. 3 F shows the WB of FLAG- and Lectin-purified NA (pN1/2009) detected with different anti-FLAG antibodies as well as the Coomassie stained gel of the same samples.

    Journal: PLoS ONE

    Article Title: Taking down the FLAG! How Insect Cell Expression Challenges an Established Tag-System

    doi: 10.1371/journal.pone.0037779

    Figure Lengend Snippet: Identification of FLAG-tag tyrosine-sulfation. Lectin purified TB-Hokkaido NA was incubated with different PTM-cleaving enzymes. The anti-FLAG WB is shown in Fig. 3 A. Addition of sulfatase made the FLAG tag accessible to the anti-FLAG mAb. Desulfation kinetics of Lectin/IEX-purified pN1/2009 NA using sulfatase type VIII (Abalone entrails) are shown in 3B. Activity of all 4 sulfatases tested was efficiently inhibited by the addition of vanadate-phenyl-Ester (3C). Fig. 3 D shows the negative linear mode MS of the sulfated control peptide CCK-8 at 1143.5 Da and its non-sulfated form at 1063.3 Da (−80 Da). The Thrombin cleaved FLAG tag was detected in its sulfated and non-sulfated form at a molecular weight of 1690.9 and 1611.1 Da (−80 Da), respectively. Fig. 3 E shows the same sample measured in positive linear mode. Only the non-sulfated peptides (−80 Da) were detected with an additional weight due to protonation (+1 Da). Fig. 3 F shows the WB of FLAG- and Lectin-purified NA (pN1/2009) detected with different anti-FLAG antibodies as well as the Coomassie stained gel of the same samples.

    Article Snippet: Briefly, the FLAG-depleted media was run through the lentil lectin affinity matrix (lentil lectin Sepharose 4B; GE Healthcare, Rydalmere, NSW, Australia) overnight at 4°C.

    Techniques: FLAG-tag, Purification, Incubation, Western Blot, Activity Assay, Mass Spectrometry, CCK-8 Assay, Molecular Weight, Staining

    Expression and purification of recombinant NA in insect cells. The expression and secretion of GCN-pLI and TB-based soluble Hokkaido NA was monitored by anti-FLAG WB (2A, B) and by NA activity assays (2C). The gel filtration chromatogram for both NA constructs is shown in 2D. 2E shows the processed insect cell media before and after anti-FLAG affinity purification in a Coomassie stained gel (2E left panel) and corresponding WB (2E right panel). Figure 2F shows the FLAG- and Lectin/IEX-purified pN1/2009 NA loaded onto an SDS-PAGE and stained by Coomassie (2F left panel) or detected by anti-FLAG WB (2F right panel). The amino acid sequence obtained by N-terminal sequencing of both enzymes is shown in 2G.

    Journal: PLoS ONE

    Article Title: Taking down the FLAG! How Insect Cell Expression Challenges an Established Tag-System

    doi: 10.1371/journal.pone.0037779

    Figure Lengend Snippet: Expression and purification of recombinant NA in insect cells. The expression and secretion of GCN-pLI and TB-based soluble Hokkaido NA was monitored by anti-FLAG WB (2A, B) and by NA activity assays (2C). The gel filtration chromatogram for both NA constructs is shown in 2D. 2E shows the processed insect cell media before and after anti-FLAG affinity purification in a Coomassie stained gel (2E left panel) and corresponding WB (2E right panel). Figure 2F shows the FLAG- and Lectin/IEX-purified pN1/2009 NA loaded onto an SDS-PAGE and stained by Coomassie (2F left panel) or detected by anti-FLAG WB (2F right panel). The amino acid sequence obtained by N-terminal sequencing of both enzymes is shown in 2G.

    Article Snippet: Briefly, the FLAG-depleted media was run through the lentil lectin affinity matrix (lentil lectin Sepharose 4B; GE Healthcare, Rydalmere, NSW, Australia) overnight at 4°C.

    Techniques: Expressing, Purification, Recombinant, Western Blot, Activity Assay, Filtration, Construct, Affinity Purification, Staining, SDS Page, Sequencing