chondroitinase b  (R&D Systems)

 
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    Name:
    Recombinant P heparinus Chondroitinase B Protein CF
    Description:
    The Recombinant P heparinus Chondroitinase B Protein from R D Systems is derived from E coli The Recombinant P heparinus Chondroitinase B Protein has been validated for the following applications Enzyme Activity
    Catalog Number:
    6974-gh-020
    Price:
    329
    Applications:
    Enzyme Activity
    Purity:
    >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie« Blue stain at 5 ╡g per lane
    Conjugate:
    Unconjugated
    Size:
    20 ug
    Category:
    Proteins and Enzymes
    Source:
    E. coli-derived Recombinant P. heparinus Chondroitinase B Protein
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    Structured Review

    R&D Systems chondroitinase b
    The Recombinant P heparinus Chondroitinase B Protein from R D Systems is derived from E coli The Recombinant P heparinus Chondroitinase B Protein has been validated for the following applications Enzyme Activity
    https://www.bioz.com/result/chondroitinase b/product/R&D Systems
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    chondroitinase b - by Bioz Stars, 2020-11
    93/100 stars

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    Related Articles

    other:

    Article Title: Recombinant dermatan sulfate is a potent activator of heparin cofactor II-dependent inhibition of thrombin
    Article Snippet: For recDS-4, the polysaccharides were also degraded using chondroitinase B (2 mIU, R & D Systems) in 30 μL ammonium acetate buffer (50 mM, pH 7.5) overnight at 37°C.

    SDS Page:

    Article Title: Prevention of TGFβ induction attenuates angII-stimulated vascular biglycan and atherosclerosis in Ldlr−/− mice 1 mice 1 [S]
    Article Snippet: .. Equal amounts of protein were treated with chondroitinase or heparinase III to remove GAG, then separated by SDS-PAGE using 8% gels (biglycan molecular mass 42 kDa; perlecan molecular mass 400 kDa) followed by immunoprobing with an anti-biglycan antibody (R and D Systems) or anti-perlecan antibody (Accurate Chemical, Westbury, NY). .. Blotting for β-actin (Sigma, St. Louis, MO; AF2066) served as a loading control.

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  • 93
    R&D Systems chondroitinase b
    Disaccharide composition of XylNapOH- and XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells. A , typical chromatogram from separation on an XBridge BEH Shield RP18 (2.1 × 100 mm, 2.5 μm) column of chondroitinase ABC-degraded and 2-aminoacridone-labeled XylNapOH-primed GAGs from HCC70 cells ( solid line ) and CS/DS standards ( dashed line ). The different disaccharides are indicated above the corresponding peaks. ΔUA-GlcNAc (hyaluronic acid ( HA )) is indicated but was not investigated in the study. Excitation λ = 425 nm, and emission λ = 525 nm. F.I. , fluorescence intensity. The disaccharide data presented in B–E was estimated by the corresponding chromatograms. B–E , disaccharide fingerprint from XylNapOH- and XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells after enzymatic degradation using chondroitinase ABC ( B ), chondroitinase AC-I and -II ( C ), <t>chondroitinase</t> B ( D ), and heparinase I-III ( E ). The inset in B displays the data of disaccharides ΔUA,2S-GalNAc,4S ( B ), ΔUA-GalNAc,4S,6S ( E ), and ΔUA,2S-GalNAc,6S ( D ), where the y .
    Chondroitinase B, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/chondroitinase b/product/R&D Systems
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    chondroitinase b - by Bioz Stars, 2020-11
    93/100 stars
      Buy from Supplier

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    Disaccharide composition of XylNapOH- and XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells. A , typical chromatogram from separation on an XBridge BEH Shield RP18 (2.1 × 100 mm, 2.5 μm) column of chondroitinase ABC-degraded and 2-aminoacridone-labeled XylNapOH-primed GAGs from HCC70 cells ( solid line ) and CS/DS standards ( dashed line ). The different disaccharides are indicated above the corresponding peaks. ΔUA-GlcNAc (hyaluronic acid ( HA )) is indicated but was not investigated in the study. Excitation λ = 425 nm, and emission λ = 525 nm. F.I. , fluorescence intensity. The disaccharide data presented in B–E was estimated by the corresponding chromatograms. B–E , disaccharide fingerprint from XylNapOH- and XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells after enzymatic degradation using chondroitinase ABC ( B ), chondroitinase AC-I and -II ( C ), chondroitinase B ( D ), and heparinase I-III ( E ). The inset in B displays the data of disaccharides ΔUA,2S-GalNAc,4S ( B ), ΔUA-GalNAc,4S,6S ( E ), and ΔUA,2S-GalNAc,6S ( D ), where the y .

    Journal: The Journal of Biological Chemistry

    Article Title: Xyloside-primed Chondroitin Sulfate/Dermatan Sulfate from Breast Carcinoma Cells with a Defined Disaccharide Composition Has Cytotoxic Effects in Vitro *

    doi: 10.1074/jbc.M116.716829

    Figure Lengend Snippet: Disaccharide composition of XylNapOH- and XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells. A , typical chromatogram from separation on an XBridge BEH Shield RP18 (2.1 × 100 mm, 2.5 μm) column of chondroitinase ABC-degraded and 2-aminoacridone-labeled XylNapOH-primed GAGs from HCC70 cells ( solid line ) and CS/DS standards ( dashed line ). The different disaccharides are indicated above the corresponding peaks. ΔUA-GlcNAc (hyaluronic acid ( HA )) is indicated but was not investigated in the study. Excitation λ = 425 nm, and emission λ = 525 nm. F.I. , fluorescence intensity. The disaccharide data presented in B–E was estimated by the corresponding chromatograms. B–E , disaccharide fingerprint from XylNapOH- and XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells after enzymatic degradation using chondroitinase ABC ( B ), chondroitinase AC-I and -II ( C ), chondroitinase B ( D ), and heparinase I-III ( E ). The inset in B displays the data of disaccharides ΔUA,2S-GalNAc,4S ( B ), ΔUA-GalNAc,4S,6S ( E ), and ΔUA,2S-GalNAc,6S ( D ), where the y .

    Article Snippet: The xyloside-primed GAGs were degraded using chondroitinase ABC, chondroitinase AC-I and -II, chondroitinase B, or heparinase I-III followed by 2-aminoacridone labeling of the disaccharides and separation of these on HPLC ( A ).

    Techniques: Labeling, Fluorescence

    Relative proportions of CS/DS and HS and disaccharide composition of XylNap-primed CS/DS from HCC70 cells and CCD-1095Sk cells. A , relative proportions of GlcUA in CS/DS (CS/DS GlcUA ), IdoUA in CS/DS distributed as alternating or single IdoUA-containing units (CS/DS IdoUA_Alt/single ), IdoUA in CS/DS distributed as blocks (CS/DS IdoUA_ChB ), and HS of XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells, respectively. B and C , disaccharide composition of XylNap-primed GAGs from HCC70 cells ( B ) and CCD-1095Sk cells ( C ) after depolymerization with chondroitinase ABC (total), chondroitinase AC-I and -II ( ChAC ), chondroitinase B ( ChB ), and the remaining disaccharides degraded by chondroitinase ABC but not by chondroitinase AC-I and -II and chondroitinase B ( Ch ( ABC-AC-B .

    Journal: The Journal of Biological Chemistry

    Article Title: LC–MS/MS characterization of xyloside-primed glycosaminoglycans with cytotoxic properties reveals structural diversity and novel glycan modifications

    doi: 10.1074/jbc.RA118.002971

    Figure Lengend Snippet: Relative proportions of CS/DS and HS and disaccharide composition of XylNap-primed CS/DS from HCC70 cells and CCD-1095Sk cells. A , relative proportions of GlcUA in CS/DS (CS/DS GlcUA ), IdoUA in CS/DS distributed as alternating or single IdoUA-containing units (CS/DS IdoUA_Alt/single ), IdoUA in CS/DS distributed as blocks (CS/DS IdoUA_ChB ), and HS of XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells, respectively. B and C , disaccharide composition of XylNap-primed GAGs from HCC70 cells ( B ) and CCD-1095Sk cells ( C ) after depolymerization with chondroitinase ABC (total), chondroitinase AC-I and -II ( ChAC ), chondroitinase B ( ChB ), and the remaining disaccharides degraded by chondroitinase ABC but not by chondroitinase AC-I and -II and chondroitinase B ( Ch ( ABC-AC-B .

    Article Snippet: After 24 h of plating, the cells were allowed to grow in DME/F-12 medium supplemented with increasing concentrations of XylNap-primed GAGs degraded using either heparinase II and III, heparinase II and III and chondroitinase ABC, heparinase II and III and chondroitinase AC-I and -II, or heparinase II and III and chondroitinase B.

    Techniques:

    Growth of HCC70 cells in the presence of enzymatically degraded XylNap-primed CS/DS from HCC70 cells. The growth of HCC70 cells after 96 h of treatment with XylNap-primed GAGs degraded with heparinase II and III ( Hep ; black ), heparinase II and III and chondroitinase ABC ( Hep + ChABC ; gray ), heparinase II and III and chondroitinase AC-I and -II ( Hep + ChAC ; blue ), or heparinase II and III and chondroitinase B ( Hep + ChB ; white ). The concentrations of the GAGs administered to the cells were de facto lower than the indicated concentrations, as the indicated concentrations correspond to the concentrations of the GAGs before enzymatic degradation. The data points are the means ± S.D., in which n = 3. UT , untreated.

    Journal: The Journal of Biological Chemistry

    Article Title: LC–MS/MS characterization of xyloside-primed glycosaminoglycans with cytotoxic properties reveals structural diversity and novel glycan modifications

    doi: 10.1074/jbc.RA118.002971

    Figure Lengend Snippet: Growth of HCC70 cells in the presence of enzymatically degraded XylNap-primed CS/DS from HCC70 cells. The growth of HCC70 cells after 96 h of treatment with XylNap-primed GAGs degraded with heparinase II and III ( Hep ; black ), heparinase II and III and chondroitinase ABC ( Hep + ChABC ; gray ), heparinase II and III and chondroitinase AC-I and -II ( Hep + ChAC ; blue ), or heparinase II and III and chondroitinase B ( Hep + ChB ; white ). The concentrations of the GAGs administered to the cells were de facto lower than the indicated concentrations, as the indicated concentrations correspond to the concentrations of the GAGs before enzymatic degradation. The data points are the means ± S.D., in which n = 3. UT , untreated.

    Article Snippet: After 24 h of plating, the cells were allowed to grow in DME/F-12 medium supplemented with increasing concentrations of XylNap-primed GAGs degraded using either heparinase II and III, heparinase II and III and chondroitinase ABC, heparinase II and III and chondroitinase AC-I and -II, or heparinase II and III and chondroitinase B.

    Techniques:

    Base peak chromatograms of chondroitinase AC-I– and -II–degraded and chondroitinase B–degraded XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells. A and B , degradation products of XylNap-primed GAGs from HCC70 cells ( A ) and CCD-1095Sk cells ( B ) generated after chondroitinase AC-I and -II ( gray ) or chondroitinase B ( pink ) treatment, containing disaccharides (dp2), oligosaccharides (dp4 and dp6), and linkage regions ( L4 to L10 ) carrying one to three sulfate groups ( S1–S3 ) and/or one Neu5Ac ( SA1 ).

    Journal: The Journal of Biological Chemistry

    Article Title: LC–MS/MS characterization of xyloside-primed glycosaminoglycans with cytotoxic properties reveals structural diversity and novel glycan modifications

    doi: 10.1074/jbc.RA118.002971

    Figure Lengend Snippet: Base peak chromatograms of chondroitinase AC-I– and -II–degraded and chondroitinase B–degraded XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells. A and B , degradation products of XylNap-primed GAGs from HCC70 cells ( A ) and CCD-1095Sk cells ( B ) generated after chondroitinase AC-I and -II ( gray ) or chondroitinase B ( pink ) treatment, containing disaccharides (dp2), oligosaccharides (dp4 and dp6), and linkage regions ( L4 to L10 ) carrying one to three sulfate groups ( S1–S3 ) and/or one Neu5Ac ( SA1 ).

    Article Snippet: After 24 h of plating, the cells were allowed to grow in DME/F-12 medium supplemented with increasing concentrations of XylNap-primed GAGs degraded using either heparinase II and III, heparinase II and III and chondroitinase ABC, heparinase II and III and chondroitinase AC-I and -II, or heparinase II and III and chondroitinase B.

    Techniques: Generated

    Total ion chromatograms of enzymatically degraded XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells and MS 1 of intact XylNap-primed CS/DS. A–F , degradation products of XylNap-primed GAGs from HCC70 cells ( A , C , and E ) and CCD-1095Sk cells ( B, D, and F ) generated after heparinase II and III ( A and B ), chondroitinase AC-I and -II ( C and D ), or chondroitinase B ( E and F ) treatment. G–I , full MS spectra of the peaks in A eluting at 41.81–42.40 min ( G ), 43.61–44.11 min ( H ), and 45.99–46.98 min ( I ), corresponding to intact XylNap-primed CS/DS ( L11 to L19 ) carrying five to seven sulfate groups ( S5–S7 ) and/or one Neu5Ac ( SA1 ). DBA, dibutylamine.

    Journal: The Journal of Biological Chemistry

    Article Title: LC–MS/MS characterization of xyloside-primed glycosaminoglycans with cytotoxic properties reveals structural diversity and novel glycan modifications

    doi: 10.1074/jbc.RA118.002971

    Figure Lengend Snippet: Total ion chromatograms of enzymatically degraded XylNap-primed GAGs from HCC70 cells and CCD-1095Sk cells and MS 1 of intact XylNap-primed CS/DS. A–F , degradation products of XylNap-primed GAGs from HCC70 cells ( A , C , and E ) and CCD-1095Sk cells ( B, D, and F ) generated after heparinase II and III ( A and B ), chondroitinase AC-I and -II ( C and D ), or chondroitinase B ( E and F ) treatment. G–I , full MS spectra of the peaks in A eluting at 41.81–42.40 min ( G ), 43.61–44.11 min ( H ), and 45.99–46.98 min ( I ), corresponding to intact XylNap-primed CS/DS ( L11 to L19 ) carrying five to seven sulfate groups ( S5–S7 ) and/or one Neu5Ac ( SA1 ). DBA, dibutylamine.

    Article Snippet: After 24 h of plating, the cells were allowed to grow in DME/F-12 medium supplemented with increasing concentrations of XylNap-primed GAGs degraded using either heparinase II and III, heparinase II and III and chondroitinase ABC, heparinase II and III and chondroitinase AC-I and -II, or heparinase II and III and chondroitinase B.

    Techniques: Mass Spectrometry, Generated

    Proposed distribution of GlcUA and IdoUA in CS/DS from HCC70 cells and CCD-1095Sk cells primed on XylNap. A and B , proposed structures of XylNap-primed CS/DS from HCC70 cells ( A ) and CCD-1095Sk cells ( B ). The distribution of IdoUA and GlcUA was based on the MS data of the main products generated after chondroitinase AC-I and -II and chondroitinase B degradation. Two parallel lines indicate that the chain either ends or continues with the following polysaccharide. B ), corresponding to an average length of 30 disaccharides. Sulfation was not taken into consideration.

    Journal: The Journal of Biological Chemistry

    Article Title: LC–MS/MS characterization of xyloside-primed glycosaminoglycans with cytotoxic properties reveals structural diversity and novel glycan modifications

    doi: 10.1074/jbc.RA118.002971

    Figure Lengend Snippet: Proposed distribution of GlcUA and IdoUA in CS/DS from HCC70 cells and CCD-1095Sk cells primed on XylNap. A and B , proposed structures of XylNap-primed CS/DS from HCC70 cells ( A ) and CCD-1095Sk cells ( B ). The distribution of IdoUA and GlcUA was based on the MS data of the main products generated after chondroitinase AC-I and -II and chondroitinase B degradation. Two parallel lines indicate that the chain either ends or continues with the following polysaccharide. B ), corresponding to an average length of 30 disaccharides. Sulfation was not taken into consideration.

    Article Snippet: After 24 h of plating, the cells were allowed to grow in DME/F-12 medium supplemented with increasing concentrations of XylNap-primed GAGs degraded using either heparinase II and III, heparinase II and III and chondroitinase ABC, heparinase II and III and chondroitinase AC-I and -II, or heparinase II and III and chondroitinase B.

    Techniques: Mass Spectrometry, Generated

    Down-regulation of DS-epi2 in MCF 10a cells results in decrease of both epimerases and IdoA content in CS/DS chains. A and B , after DS-epi2 down-regulation by siRNA in MCF 10a cells, ( A ) DS-epi2 and DS-epi1 RNA were quantified by qRT-PCR; data are expressed relative to the control siRNA and normalized to GAPDH expression (mean ± S.D.); and ( B ) proteins were visualized by Western blotting. C , cells were labeled by 35 S, and the resulting purified 35 S-CS/DS chains were depolymerized with chondroitinase B and applied to a Superdex Peptide size-permeation column. Filled circles , control siRNA; empty circles , DS-epi2 siRNA. D , from the size pattern in C , content of IdoA was calculated (mean ± S.D.).

    Journal: The Journal of Biological Chemistry

    Article Title: Dermatan sulfate epimerase 1 and dermatan 4-O-sulfotransferase 1 form complexes that generate long epimerized 4-O-sulfated blocks

    doi: 10.1074/jbc.RA118.003875

    Figure Lengend Snippet: Down-regulation of DS-epi2 in MCF 10a cells results in decrease of both epimerases and IdoA content in CS/DS chains. A and B , after DS-epi2 down-regulation by siRNA in MCF 10a cells, ( A ) DS-epi2 and DS-epi1 RNA were quantified by qRT-PCR; data are expressed relative to the control siRNA and normalized to GAPDH expression (mean ± S.D.); and ( B ) proteins were visualized by Western blotting. C , cells were labeled by 35 S, and the resulting purified 35 S-CS/DS chains were depolymerized with chondroitinase B and applied to a Superdex Peptide size-permeation column. Filled circles , control siRNA; empty circles , DS-epi2 siRNA. D , from the size pattern in C , content of IdoA was calculated (mean ± S.D.).

    Article Snippet: Quantification and spatial arrangement of IdoA along the chain was analyzed by cleaving 20,000 dpm of CS/DS with 2 mIU of chondroitinase B (R & D Systems) in 20 m m HEPES, pH 7.2, 50 m m NaCl, 4 m m CaCl2 , and 0.1 mg/ml BSA overnight at 37 °C.

    Techniques: Quantitative RT-PCR, Expressing, Western Blot, Labeling, Purification