Structured Review

Seikagaku mu heparinase iii
Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with <t>heparinase</t> <t>III</t> (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.
Mu Heparinase Iii, supplied by Seikagaku, used in various techniques. Bioz Stars score: 80/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mu heparinase iii/product/Seikagaku
Average 80 stars, based on 2 article reviews
Price from $9.99 to $1999.99
mu heparinase iii - by Bioz Stars, 2020-11
80/100 stars

Images

1) Product Images from "cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs"

Article Title: cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs

Journal: The Journal of Cell Biology

doi:

Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with heparinase III (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.
Figure Legend Snippet: Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with heparinase III (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.

Techniques Used: Western Blot, Affinity Purification, Migration

Glycanation of the NH 2 -terminal region of bamacan domain V. Autoradiogram of 5–15% gradient SDS-PAGE of protein A–bamacan fusion protein, heparinase III treated (lane 1 ), chondroitinase ABC treated (lane 2 ), or untreated (lane 5 ). Only after chondroitinase ABC treatment is a discrete protein resolved ( arrows denote fusion protein of M r ∼ 50K). (Lane 3 ) Result from transfection of empty pRK5F10 vector; (lane 4 ) equivalent from empty pcDNA 3 vector (which fails to bind Ig-agarose).
Figure Legend Snippet: Glycanation of the NH 2 -terminal region of bamacan domain V. Autoradiogram of 5–15% gradient SDS-PAGE of protein A–bamacan fusion protein, heparinase III treated (lane 1 ), chondroitinase ABC treated (lane 2 ), or untreated (lane 5 ). Only after chondroitinase ABC treatment is a discrete protein resolved ( arrows denote fusion protein of M r ∼ 50K). (Lane 3 ) Result from transfection of empty pRK5F10 vector; (lane 4 ) equivalent from empty pcDNA 3 vector (which fails to bind Ig-agarose).

Techniques Used: SDS Page, Transfection, Plasmid Preparation

2) Product Images from "cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs"

Article Title: cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs

Journal: The Journal of Cell Biology

doi:

Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with heparinase III (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.
Figure Legend Snippet: Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with heparinase III (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.

Techniques Used: Western Blot, Affinity Purification, Migration

Glycanation of the NH 2 -terminal region of bamacan domain V. Autoradiogram of 5–15% gradient SDS-PAGE of protein A–bamacan fusion protein, heparinase III treated (lane 1 ), chondroitinase ABC treated (lane 2 ), or untreated (lane 5 ). Only after chondroitinase ABC treatment is a discrete protein resolved ( arrows denote fusion protein of M r ∼ 50K). (Lane 3 ) Result from transfection of empty pRK5F10 vector; (lane 4 ) equivalent from empty pcDNA 3 vector (which fails to bind Ig-agarose).
Figure Legend Snippet: Glycanation of the NH 2 -terminal region of bamacan domain V. Autoradiogram of 5–15% gradient SDS-PAGE of protein A–bamacan fusion protein, heparinase III treated (lane 1 ), chondroitinase ABC treated (lane 2 ), or untreated (lane 5 ). Only after chondroitinase ABC treatment is a discrete protein resolved ( arrows denote fusion protein of M r ∼ 50K). (Lane 3 ) Result from transfection of empty pRK5F10 vector; (lane 4 ) equivalent from empty pcDNA 3 vector (which fails to bind Ig-agarose).

Techniques Used: SDS Page, Transfection, Plasmid Preparation

Related Articles

Centrifugation:

Article Title: Pentosan Polysulfate: Oral Versus Subcutaneous Injection in Mucopolysaccharidosis Type I Dogs
Article Snippet: .. After centrifugation, the 96-well bottom plate was replaced for a new plate and the samples were incubated with a mixture of: 60 μl of 50mM Tris HCL (pH 7.0), 10 μl of 5 μg/ml of internal standard (IS, Chondrosine), 10 μl of 1 mU chondroitinase B (in BSA 1%), 10 μl of 1 mU heparitinase (in BSA 1%), and 10 μl of 1 mU keratanase II (in BSA 1%) (enzymes and IS were provided by Seikagaku Co, Tokyo). .. Samples were incubated overnight in a 37°C water bath, followed by a centrifugation for 15 min at 2200 rcf and then injected to the LC-MS/MS.

other:

Article Title: cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs
Article Snippet: Samples were digested overnight at 37°C in 15 μl heparinase buffer (0.1 M sodium acetate, 0.1 mM calcium acetate, 0.1% Tween 20, pH 7.0), containing 0.5–1 mU heparinase III and/or 1–2 mU chondroitinase ABC.

Incubation:

Article Title: Pentosan Polysulfate: Oral Versus Subcutaneous Injection in Mucopolysaccharidosis Type I Dogs
Article Snippet: .. After centrifugation, the 96-well bottom plate was replaced for a new plate and the samples were incubated with a mixture of: 60 μl of 50mM Tris HCL (pH 7.0), 10 μl of 5 μg/ml of internal standard (IS, Chondrosine), 10 μl of 1 mU chondroitinase B (in BSA 1%), 10 μl of 1 mU heparitinase (in BSA 1%), and 10 μl of 1 mU keratanase II (in BSA 1%) (enzymes and IS were provided by Seikagaku Co, Tokyo). .. Samples were incubated overnight in a 37°C water bath, followed by a centrifugation for 15 min at 2200 rcf and then injected to the LC-MS/MS.

Purification:

Article Title: Specific collagen XVIII isoforms promote adipose tissue accrual via mechanisms determining adipocyte number and affect fat deposition
Article Snippet: .. When indicated, purified DUF-Fz-Tsp1 (7.5 µg) was digested with 0.33 mU heparitinase I/µg of protein units (Seikagaku) at 37 °C for 2 h. .. Murine Wnt10b cDNA was inserted into pcDNA3.1/V5-HIS (Invitrogen) and transfected into specified HEK293 cell lines.

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    Seikagaku mu heparinase iii
    Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with <t>heparinase</t> <t>III</t> (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.
    Mu Heparinase Iii, supplied by Seikagaku, used in various techniques. Bioz Stars score: 80/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mu heparinase iii/product/Seikagaku
    Average 80 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    mu heparinase iii - by Bioz Stars, 2020-11
    80/100 stars
      Buy from Supplier

    88
    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, 2020-11
    88/100 stars
      Buy from Supplier

    Image Search Results


    Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with heparinase III (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.

    Journal: The Journal of Cell Biology

    Article Title: cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs

    doi:

    Figure Lengend Snippet: Western blot of total L2 proteoglycans probed with affinity-purified R664 polyclonal antibodies against a fusion protein prepared using clone F15a (see Fig. 1 ). The proteoglycans were untreated (lane 1 ) or pretreated with heparinase III (lanes 2 and 3 ) and/or chondroitinase ABC (lanes 3 and 4 ). A core protein is only clearly resolved after removal of chondroitin sulfate chains. The migration of molecular mass markers in kD is shown.

    Article Snippet: These were digested with 10 mU chondroitinase ABC (EC 4.2.2.4) or 20 mU heparinase III (EC 4.2.2.8; Seikagaku America, Ijamsville, MD) for 3 h or overnight at 37°C, respectively.

    Techniques: Western Blot, Affinity Purification, Migration

    Glycanation of the NH 2 -terminal region of bamacan domain V. Autoradiogram of 5–15% gradient SDS-PAGE of protein A–bamacan fusion protein, heparinase III treated (lane 1 ), chondroitinase ABC treated (lane 2 ), or untreated (lane 5 ). Only after chondroitinase ABC treatment is a discrete protein resolved ( arrows denote fusion protein of M r ∼ 50K). (Lane 3 ) Result from transfection of empty pRK5F10 vector; (lane 4 ) equivalent from empty pcDNA 3 vector (which fails to bind Ig-agarose).

    Journal: The Journal of Cell Biology

    Article Title: cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs

    doi:

    Figure Lengend Snippet: Glycanation of the NH 2 -terminal region of bamacan domain V. Autoradiogram of 5–15% gradient SDS-PAGE of protein A–bamacan fusion protein, heparinase III treated (lane 1 ), chondroitinase ABC treated (lane 2 ), or untreated (lane 5 ). Only after chondroitinase ABC treatment is a discrete protein resolved ( arrows denote fusion protein of M r ∼ 50K). (Lane 3 ) Result from transfection of empty pRK5F10 vector; (lane 4 ) equivalent from empty pcDNA 3 vector (which fails to bind Ig-agarose).

    Article Snippet: These were digested with 10 mU chondroitinase ABC (EC 4.2.2.4) or 20 mU heparinase III (EC 4.2.2.8; Seikagaku America, Ijamsville, MD) for 3 h or overnight at 37°C, respectively.

    Techniques: SDS Page, Transfection, Plasmid Preparation

    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: Heparinase I ( Sigma Chemical Co. ) was used at 600 mU, and heparitinase II (Seikagaku Corporation, Tokyo, Japan) was used at 4 mU.

    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: Heparinase I ( Sigma Chemical Co. ) was used at 600 mU, and heparitinase II (Seikagaku Corporation, Tokyo, Japan) was used at 4 mU.

    Techniques: Immunofluorescence, Staining

    CXCL6 is present in healthy articular cartilage and its expression is associated with chondrocyte differentiation. (A) Immunofluorescence staining for CXCL6 (green) in normal and early osteoarthritis (moderate Mankin score) articular cartilage. Nuclei are stained using propidium iodide (red). Scale bar, 100 μm. (B) Densitometric quantification of CXCL6 staining (n=3). (C) Immunofluorescence staining for CXCL6 (red) in mouse articular cartilage of sham-operated control and destabilisation of the medial meniscus (DMM) operated mice, with 4′,6-diamidino-2-phenylindole staining the nuclei. Scale bar, 100 μm. (D) Densitometric quantification of CXCL6 staining (n=4). (E) Western blot analysis of CXCL6 release into supernatant from vehicle control or heparitinase treated, freeze-thawed wild-type mouse hip caps. (F) Real-time RT-PCR for CXCL6 mRNA in early and late passage human articular chondrocytes (n=3), *** p

    Journal: Annals of the Rheumatic Diseases

    Article Title: A homeostatic function of CXCR2 signalling in articular cartilage

    doi: 10.1136/annrheumdis-2014-205546

    Figure Lengend Snippet: CXCL6 is present in healthy articular cartilage and its expression is associated with chondrocyte differentiation. (A) Immunofluorescence staining for CXCL6 (green) in normal and early osteoarthritis (moderate Mankin score) articular cartilage. Nuclei are stained using propidium iodide (red). Scale bar, 100 μm. (B) Densitometric quantification of CXCL6 staining (n=3). (C) Immunofluorescence staining for CXCL6 (red) in mouse articular cartilage of sham-operated control and destabilisation of the medial meniscus (DMM) operated mice, with 4′,6-diamidino-2-phenylindole staining the nuclei. Scale bar, 100 μm. (D) Densitometric quantification of CXCL6 staining (n=4). (E) Western blot analysis of CXCL6 release into supernatant from vehicle control or heparitinase treated, freeze-thawed wild-type mouse hip caps. (F) Real-time RT-PCR for CXCL6 mRNA in early and late passage human articular chondrocytes (n=3), *** p

    Article Snippet: Hip caps were incubated overnight at 37°C either in phosphate buffered saline (PBS) or in PBS containing 5 mU/mL heparitinase (Seikagaku).

    Techniques: Expressing, Immunofluorescence, Staining, Mouse Assay, Western Blot, Quantitative RT-PCR