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Seikagaku heparitinase iii
Heparitinase Iii, supplied by Seikagaku, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/heparitinase iii/product/Seikagaku
Average 91 stars, based on 1 article reviews
Price from $9.99 to $1999.99
heparitinase iii - by Bioz Stars, 2020-11
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Concentration Assay:

Article Title: Functional abnormalities of heparan sulfate in mucopolysaccharidosis-I are associated with defective biologic activity of FGF-2 on human multipotent progenitor cells
Article Snippet: .. Heparitinase III (EC 4.2.2.7; Seikagaku America) was then added at the same concentration and calcium increased to 1 mM. .. After 1 hour incubation, the cell layer was washed and the 125 I-FGF-2 binding assay performed as described above in this section.

Incubation:

Article Title: A translational block to HSPG synthesis permits BMP signaling in the early Drosophila embryo
Article Snippet: .. Embryo lysates were treated with 0.25 mU of heparitinase III (Seikagaku Corporation) for 1 hour at 37 °C before the digestion was terminated by addition of 25 µl 4X sample buffer, 10 µl β-mercaptoethanol and incubation at 95°C. ..

other:

Article Title: Functional analysis of Leishmania major cyclophilin
Article Snippet: Heparitinase III, which cleaves heparin at α-N-acetylglucosaminide-L-iduronic acid linkage, was purchased from Seikagaku America (Falmouth, MA).

Article Title: Saccharide Primers Comprising Xylosyl-Serine Primed Phosphorylated Oligosaccharides Act as Intermediates in Glycosaminoglycan Biosynthesis
Article Snippet: Enzymatic Digestion of the Glycosylated Products C-ABC, C-ACII, heparitinase I, heparitinase II, and heparitinase III were purchased from Seikagaku Corporation. β-d -Galactosidase was purchased from Wako Pure Chemical Industries. α2-3 Sialidase was purchased from Takara Bio and α2,3-6 sialidase from Nakarai Tesque.

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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 21 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 21 article reviews
    Price from $9.99 to $1999.99
    heparitinase ii - by Bioz Stars, 2020-11
    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

    Complexes formed between perlecan, FGF18 and FGFR3 or perlecan and FGFR3. Perlecans were adsorbed onto wells of a 96 well plate and were either undigested or digested in situ with heparinase III, mammalian heparanase or chondroitinase ABC before performing

    Journal: Biochemistry

    Article Title: Heparan sulfate dependent signaling of fibroblast growth factor (FGF) 18 by chondrocyte-derived perlecan

    doi: 10.1021/bi1005199

    Figure Lengend Snippet: Complexes formed between perlecan, FGF18 and FGFR3 or perlecan and FGFR3. Perlecans were adsorbed onto wells of a 96 well plate and were either undigested or digested in situ with heparinase III, mammalian heparanase or chondroitinase ABC before performing

    Article Snippet: Antibodies against HS (10E4) and heparinase III generated HS-stubs (3G10) were purchased from Seikagaku Corp., Tokyo, Japan.

    Techniques: In Situ

    Ternary complexes formed between perlecan, either FGF2 or FGF18 and either FGF receptor type 1 or 3. Perlecans were adsorbed onto wells of a 96 well plate and were either undigested or digested in situ with heparinase III, mammalian heparanase or chondroitinase

    Journal: Biochemistry

    Article Title: Heparan sulfate dependent signaling of fibroblast growth factor (FGF) 18 by chondrocyte-derived perlecan

    doi: 10.1021/bi1005199

    Figure Lengend Snippet: Ternary complexes formed between perlecan, either FGF2 or FGF18 and either FGF receptor type 1 or 3. Perlecans were adsorbed onto wells of a 96 well plate and were either undigested or digested in situ with heparinase III, mammalian heparanase or chondroitinase

    Article Snippet: Antibodies against HS (10E4) and heparinase III generated HS-stubs (3G10) were purchased from Seikagaku Corp., Tokyo, Japan.

    Techniques: In Situ