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Seikagaku heparitinases
Heparitinases, supplied by Seikagaku, used in various techniques. Bioz Stars score: 86/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/heparitinases/product/Seikagaku
Average 86 stars, based on 2 article reviews
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heparitinases - by Bioz Stars, 2020-09
86/100 stars

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High Performance Liquid Chromatography:

Article Title: Ancient origin of mast cells
Article Snippet: .. Employing the experimental procedures developed for analyzing mammalian heparin glycosaminoglycans [ ], purified test cell-derived heparin was digested with heparitinases (Seikagaku Corp.) and the resulting disaccharides were subjected to high performance liquid chromatography. .. After chromatographic separation of the generated disaccharides, they were reacted with 2-cyanoacetoamide as a post-column reagent.

Purification:

Article Title: Ancient origin of mast cells
Article Snippet: .. Employing the experimental procedures developed for analyzing mammalian heparin glycosaminoglycans [ ], purified test cell-derived heparin was digested with heparitinases (Seikagaku Corp.) and the resulting disaccharides were subjected to high performance liquid chromatography. .. After chromatographic separation of the generated disaccharides, they were reacted with 2-cyanoacetoamide as a post-column reagent.

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    Seikagaku heparitinase ii
    Interaction of L-selectin with suspended aortic endothelial cells: effect of treating TNF-α–activated BAEC (8 h, 100 U/ml) with heparinase I, <t>heparitinase</t> II, chondroitinase ABC, hyaluronidase, or trypsin. Unactivated BAEC were examined by indirect immunofluorescence analysis with L-selectin/μ ( solid lines ) and CD4/μ ( dotted lines ). Identical results were obtained by treating BAEC with heparinase I, II, or III. The data are representative of six experiments. Percentages of BAEC that bound to L-selectin/ μ are as follows: control, 87%; heparinase I, 39%; heparitinase II, 47%; chondroitinase, 89%; hyaluronidase, 82%; trypsin, 4%.
    Heparitinase Ii, supplied by Seikagaku, used in various techniques. Bioz Stars score: 88/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/heparitinase ii/product/Seikagaku
    Average 88 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    heparitinase ii - by Bioz Stars, 2020-09
    88/100 stars
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    Interaction of L-selectin with suspended aortic endothelial cells: effect of treating TNF-α–activated BAEC (8 h, 100 U/ml) with heparinase I, heparitinase II, chondroitinase ABC, hyaluronidase, or trypsin. Unactivated BAEC were examined by indirect immunofluorescence analysis with L-selectin/μ ( solid lines ) and CD4/μ ( dotted lines ). Identical results were obtained by treating BAEC with heparinase I, II, or III. The data are representative of six experiments. Percentages of BAEC that bound to L-selectin/ μ are as follows: control, 87%; heparinase I, 39%; heparitinase II, 47%; chondroitinase, 89%; hyaluronidase, 82%; trypsin, 4%.

    Journal: The Journal of Cell Biology

    Article Title: Monocyte Adhesion to Activated Aortic Endothelium: Role of L-Selectin and Heparan Sulfate Proteoglycans

    doi:

    Figure Lengend Snippet: Interaction of L-selectin with suspended aortic endothelial cells: effect of treating TNF-α–activated BAEC (8 h, 100 U/ml) with heparinase I, heparitinase II, chondroitinase ABC, hyaluronidase, or trypsin. Unactivated BAEC were examined by indirect immunofluorescence analysis with L-selectin/μ ( solid lines ) and CD4/μ ( dotted lines ). Identical results were obtained by treating BAEC with heparinase I, II, or III. The data are representative of six experiments. Percentages of BAEC that bound to L-selectin/ μ are as follows: control, 87%; heparinase I, 39%; heparitinase II, 47%; chondroitinase, 89%; hyaluronidase, 82%; trypsin, 4%.

    Article Snippet: Although trypsin treatment completely inhibited the reaction (Fig. , bottom right ), activated BAEC exposure to heparinase I, heparitinase II, or heparitinase III only had moderate inhibitory effects on L-selectin binding (Fig. , top right and middle ).

    Techniques: Immunofluorescence

    Interaction of L-selectin with suspended aortic endothelial cells: effect of treating unstimulated BAEC with heparinase I, heparitinase II, chondroitinase ABC, hyaluronidase, or trypsin. Unactivated BAEC were examined by indirect immunofluorescence analysis with L-selectin/μ ( solid lines ) and CD4/μ ( dotted lines ). Identical results were obtained by treating BAEC with heparinase I, II, or III. The data are representative of six experiments. Percentages of BAEC that bound to L-selectin/μ were as follows: control, 86%; heparinase I, 54%; heparitinase II, 56%; chondroitinase, 89%; hyaluronidase, 90%; trypsin, 7%. The background staining with CD4/μ chimera was

    Journal: The Journal of Cell Biology

    Article Title: Monocyte Adhesion to Activated Aortic Endothelium: Role of L-Selectin and Heparan Sulfate Proteoglycans

    doi:

    Figure Lengend Snippet: Interaction of L-selectin with suspended aortic endothelial cells: effect of treating unstimulated BAEC with heparinase I, heparitinase II, chondroitinase ABC, hyaluronidase, or trypsin. Unactivated BAEC were examined by indirect immunofluorescence analysis with L-selectin/μ ( solid lines ) and CD4/μ ( dotted lines ). Identical results were obtained by treating BAEC with heparinase I, II, or III. The data are representative of six experiments. Percentages of BAEC that bound to L-selectin/μ were as follows: control, 86%; heparinase I, 54%; heparitinase II, 56%; chondroitinase, 89%; hyaluronidase, 90%; trypsin, 7%. The background staining with CD4/μ chimera was

    Article Snippet: Although trypsin treatment completely inhibited the reaction (Fig. , bottom right ), activated BAEC exposure to heparinase I, heparitinase II, or heparitinase III only had moderate inhibitory effects on L-selectin binding (Fig. , top right and middle ).

    Techniques: Immunofluorescence, Staining

    Recombinant BAEBL/Fc binds to erythrocytes via HS and sialic acid. A , binding inhibition of BAEBL/Fc to enzyme-treated erythrocytes. Erythrocytes (10 5 cells) were pretreated with buffer; 0.0016, 0.016, 0.16, or 1.6 milliunits of heparitinase; or 0.004,

    Journal:

    Article Title: Plasmodium falciparum BAEBL Binds to Heparan Sulfate Proteoglycans on the Human Erythrocyte Surface *

    doi: 10.1074/jbc.M109.021576

    Figure Lengend Snippet: Recombinant BAEBL/Fc binds to erythrocytes via HS and sialic acid. A , binding inhibition of BAEBL/Fc to enzyme-treated erythrocytes. Erythrocytes (10 5 cells) were pretreated with buffer; 0.0016, 0.016, 0.16, or 1.6 milliunits of heparitinase; or 0.004,

    Article Snippet: Erythrocytes (2.5 × 105 ) were treated with heparitinase from Flavobacterium heparinum (EC 4.2.2.8; Seikagaku Corp., Tokyo, Japan) or neuraminidase from Vibrio cholerae (EC 3.2.1.18; Sigma) for 1 h at 37 °C, and then washed in fluorescence-activated cell sorting buffer (2% fetal calf serum and 0.1% NaN3 in phosphate-buffered saline).

    Techniques: Recombinant, Binding Assay, Inhibition

    HS-dependent binding is involved in merozoite invasion. A , inhibition of merozoite invasion of enzyme-treated erythrocytes. Erythrocytes (10 7 cells) were treated with buffer, with 0.016, 0.16, 1.6, or 16 milliunits ( mU ) of heparitinase, or with 0.04,

    Journal:

    Article Title: Plasmodium falciparum BAEBL Binds to Heparan Sulfate Proteoglycans on the Human Erythrocyte Surface *

    doi: 10.1074/jbc.M109.021576

    Figure Lengend Snippet: HS-dependent binding is involved in merozoite invasion. A , inhibition of merozoite invasion of enzyme-treated erythrocytes. Erythrocytes (10 7 cells) were treated with buffer, with 0.016, 0.16, 1.6, or 16 milliunits ( mU ) of heparitinase, or with 0.04,

    Article Snippet: Erythrocytes (2.5 × 105 ) were treated with heparitinase from Flavobacterium heparinum (EC 4.2.2.8; Seikagaku Corp., Tokyo, Japan) or neuraminidase from Vibrio cholerae (EC 3.2.1.18; Sigma) for 1 h at 37 °C, and then washed in fluorescence-activated cell sorting buffer (2% fetal calf serum and 0.1% NaN3 in phosphate-buffered saline).

    Techniques: Binding Assay, Inhibition

    Western blotting analysis of DRM fractions isolated from a rat parathyroid cell line. DRMs were prepared from confluent PTr cells as described in Materials and Methods . Collected fractions, were concentrated, treated with heparitinase I and subjected to SDS-PAGE and WB analysis. A. Staining with anti-ΔHS (3G10) antibodies confirmed the presence of HSPGs in low-density fractions. Equal volumes (13 µl) of each fraction were analyzed. Fractions 13 and 14, bottom fraction (pooled fractions 15 and 16, B) and lysate (L) were diluted 16, 62 and 56 times, respectively, prior to the analysis. Bands marked with (*) represent non-specific staining due to the presence of BSA at high concentration. B. Staining with antibodies against DRM markers, Lyn and Giα defined the low-density fractions as DRMs. Equal volumes (33 µl) of each fraction were used for analysis. Fractions 13 through 14, bottom fraction (pooled fractions 15 and 16, B) and lysate (L) were diluted 18, 72 and 64 times, respectively, prior the analysis due to high protein content. Staining for transferrin receptor (TfR) was used as a control for the successful preparation. C. Graphic representation of the distribution of TfR, Lyn, Giα and HSPGs in fractions obtained from sucrose-density gradient ultracentrifugation. Density of bands detected in WB analysis (A and C) was measured and expressed as arbitrary units. TfR (○); Lyn (▪); Giα (◊) and HSPG (▴).

    Journal: PLoS ONE

    Article Title: Syndecans Reside in Sphingomyelin-Enriched Low-Density Fractions of the Plasma Membrane Isolated from a Parathyroid Cell Line

    doi: 10.1371/journal.pone.0032351

    Figure Lengend Snippet: Western blotting analysis of DRM fractions isolated from a rat parathyroid cell line. DRMs were prepared from confluent PTr cells as described in Materials and Methods . Collected fractions, were concentrated, treated with heparitinase I and subjected to SDS-PAGE and WB analysis. A. Staining with anti-ΔHS (3G10) antibodies confirmed the presence of HSPGs in low-density fractions. Equal volumes (13 µl) of each fraction were analyzed. Fractions 13 and 14, bottom fraction (pooled fractions 15 and 16, B) and lysate (L) were diluted 16, 62 and 56 times, respectively, prior to the analysis. Bands marked with (*) represent non-specific staining due to the presence of BSA at high concentration. B. Staining with antibodies against DRM markers, Lyn and Giα defined the low-density fractions as DRMs. Equal volumes (33 µl) of each fraction were used for analysis. Fractions 13 through 14, bottom fraction (pooled fractions 15 and 16, B) and lysate (L) were diluted 18, 72 and 64 times, respectively, prior the analysis due to high protein content. Staining for transferrin receptor (TfR) was used as a control for the successful preparation. C. Graphic representation of the distribution of TfR, Lyn, Giα and HSPGs in fractions obtained from sucrose-density gradient ultracentrifugation. Density of bands detected in WB analysis (A and C) was measured and expressed as arbitrary units. TfR (○); Lyn (▪); Giα (◊) and HSPG (▴).

    Article Snippet: Biotinylated mouse anti-ΔHS (3G10) antibodies, recognizing HS neo-epitope, generated by the digestion with heparitinase I from Flavobacterium heparinum and heparitinase I (Flavobacterium heparinum ) were purchased from Seikagaku Corporation, (Tokyo, Japan).

    Techniques: Western Blot, Isolation, SDS Page, Staining, Concentration Assay

    Identification of HSPGs expressed by a rat parathyroid cell line. A. RT-PCR analysis of PTr cells using syndecan-specific primers (see Materials and Methods for details). Total RNA was isolated from confluent cells and subjected to RT-PCR analysis. Amplified products were run on 2% agarose gel, stained with ethidium bromide and photographed under UV transilluminator. Lanes: M – 100 bp marker; SN1 – amplification with syndecan-1 specific primers; SN2 – amplification with syndecan-2 specific primers; SN3 – amplification with syndecan-3 specific primers; SN4 – amplification with syndecan-4 specific primers; G – amplification with GAPHD specific primers; (-) – negative controls containing no cDNA. B. Identification of HSPGs present in DRM fractions using WB analysis. Proteoglycans were isolated from confluent rat parathyroid cells and partially purified using Q-Sepharose anion-exchange chromatography. A proteoglycan-enriched fraction was incubated in the presence or absence of heparitinase I, subjected to SDS-PAGE and immunoblotted with anti-syndecan-1, anti-syndecan-4 or anti-ΔHS (3G10) antibodies. Lanes: 1, 4 and 7 represent the heparitinase I only; 2, 5 and 8 correspond to the control samples, incubated without heparitinase I; 3, 6, 8 correspond to the heparitinase-treated samples.

    Journal: PLoS ONE

    Article Title: Syndecans Reside in Sphingomyelin-Enriched Low-Density Fractions of the Plasma Membrane Isolated from a Parathyroid Cell Line

    doi: 10.1371/journal.pone.0032351

    Figure Lengend Snippet: Identification of HSPGs expressed by a rat parathyroid cell line. A. RT-PCR analysis of PTr cells using syndecan-specific primers (see Materials and Methods for details). Total RNA was isolated from confluent cells and subjected to RT-PCR analysis. Amplified products were run on 2% agarose gel, stained with ethidium bromide and photographed under UV transilluminator. Lanes: M – 100 bp marker; SN1 – amplification with syndecan-1 specific primers; SN2 – amplification with syndecan-2 specific primers; SN3 – amplification with syndecan-3 specific primers; SN4 – amplification with syndecan-4 specific primers; G – amplification with GAPHD specific primers; (-) – negative controls containing no cDNA. B. Identification of HSPGs present in DRM fractions using WB analysis. Proteoglycans were isolated from confluent rat parathyroid cells and partially purified using Q-Sepharose anion-exchange chromatography. A proteoglycan-enriched fraction was incubated in the presence or absence of heparitinase I, subjected to SDS-PAGE and immunoblotted with anti-syndecan-1, anti-syndecan-4 or anti-ΔHS (3G10) antibodies. Lanes: 1, 4 and 7 represent the heparitinase I only; 2, 5 and 8 correspond to the control samples, incubated without heparitinase I; 3, 6, 8 correspond to the heparitinase-treated samples.

    Article Snippet: Biotinylated mouse anti-ΔHS (3G10) antibodies, recognizing HS neo-epitope, generated by the digestion with heparitinase I from Flavobacterium heparinum and heparitinase I (Flavobacterium heparinum ) were purchased from Seikagaku Corporation, (Tokyo, Japan).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Isolation, Amplification, Agarose Gel Electrophoresis, Staining, Marker, Western Blot, Purification, Chromatography, Incubation, SDS Page