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Seikagaku heparitinase enzyme
Co-immunoprecipitation of CD81 and GPC3. The rat liver lysates without <t>heparitinase</t> treatment were incubated with anti-CD81 monoclonal antibody or control IgG, followed by precipitation with agarose A/G plus beads. Precipitates were separated by Western
Heparitinase Enzyme, supplied by Seikagaku, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Investigation of the Role of Glypican 3 in Liver Regeneration and Hepatocyte Proliferation"

Article Title: Investigation of the Role of Glypican 3 in Liver Regeneration and Hepatocyte Proliferation

Journal: The American Journal of Pathology

doi: 10.2353/ajpath.2009.081129

Co-immunoprecipitation of CD81 and GPC3. The rat liver lysates without heparitinase treatment were incubated with anti-CD81 monoclonal antibody or control IgG, followed by precipitation with agarose A/G plus beads. Precipitates were separated by Western
Figure Legend Snippet: Co-immunoprecipitation of CD81 and GPC3. The rat liver lysates without heparitinase treatment were incubated with anti-CD81 monoclonal antibody or control IgG, followed by precipitation with agarose A/G plus beads. Precipitates were separated by Western

Techniques Used: Immunoprecipitation, Incubation, Western Blot

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Article Title: Investigation of the Role of Glypican 3 in Liver Regeneration and Hepatocyte Proliferation
Article Snippet: .. For HS chain elimination, 100 μg of protein extract from freshly isolated rat hepatocytes and total rat liver was treated with 5 microunits of heparitinase enzyme (Seikagaku, Tokyo, Japan) and 1 mmol/L CaCl2 for 3 hours. .. Protein samples (20 μg) were resolved on 4 to 12% NuPAGE Bis-Tris gels with 1X 3-( N -morpholino) propanesulfonic acid running buffer (Invitrogen, CA) and then transferred to Immobilon-P membranes (Millipore, MA) in NuPAGE transfer buffer containing 10% methanol.

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    Seikagaku heparinase iii
    Characterization of endothelial cell-derived perlecan. (A) Native perlecan ( lane 1 ) and <t>heparinase</t> <t>III-treated</t> perlecan ( lane 2 ) were electrophoresed in a 3–8% SDS-PAGE gel under non-reducing conditions, electroblotted to nitrocellulose and probed with antibody CSI-076 against perlecan domain I. (B) Surface-adsorbed perlecan was treated with HNO 2 at pH 3.9 (3.75 M sodium nitrite, 0.33 M acetic acid) or with a control solution (3.75 M sodium chloride, 0.33 M acetic acid / sodium acetate, pH 3.9), then probed by ELISA using antibodies JM403, 10E4 and HepSS-1 against heparan sulfate. Data are means ± SEM (triplicate determinations from a representative experiment) and are expressed as % normal ELISA signal. * = P
    Heparinase Iii, supplied by Seikagaku, used in various techniques. Bioz Stars score: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/heparinase iii/product/Seikagaku
    Average 92 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    heparinase iii - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    85
    Seikagaku heparitinase enzyme
    Co-immunoprecipitation of CD81 and GPC3. The rat liver lysates without <t>heparitinase</t> treatment were incubated with anti-CD81 monoclonal antibody or control IgG, followed by precipitation with agarose A/G plus beads. Precipitates were separated by Western
    Heparitinase Enzyme, supplied by Seikagaku, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/heparitinase enzyme/product/Seikagaku
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    heparitinase enzyme - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

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    Characterization of endothelial cell-derived perlecan. (A) Native perlecan ( lane 1 ) and heparinase III-treated perlecan ( lane 2 ) were electrophoresed in a 3–8% SDS-PAGE gel under non-reducing conditions, electroblotted to nitrocellulose and probed with antibody CSI-076 against perlecan domain I. (B) Surface-adsorbed perlecan was treated with HNO 2 at pH 3.9 (3.75 M sodium nitrite, 0.33 M acetic acid) or with a control solution (3.75 M sodium chloride, 0.33 M acetic acid / sodium acetate, pH 3.9), then probed by ELISA using antibodies JM403, 10E4 and HepSS-1 against heparan sulfate. Data are means ± SEM (triplicate determinations from a representative experiment) and are expressed as % normal ELISA signal. * = P

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    Article Title: Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan

    doi: 10.1016/j.matbio.2009.09.005

    Figure Lengend Snippet: Characterization of endothelial cell-derived perlecan. (A) Native perlecan ( lane 1 ) and heparinase III-treated perlecan ( lane 2 ) were electrophoresed in a 3–8% SDS-PAGE gel under non-reducing conditions, electroblotted to nitrocellulose and probed with antibody CSI-076 against perlecan domain I. (B) Surface-adsorbed perlecan was treated with HNO 2 at pH 3.9 (3.75 M sodium nitrite, 0.33 M acetic acid) or with a control solution (3.75 M sodium chloride, 0.33 M acetic acid / sodium acetate, pH 3.9), then probed by ELISA using antibodies JM403, 10E4 and HepSS-1 against heparan sulfate. Data are means ± SEM (triplicate determinations from a representative experiment) and are expressed as % normal ELISA signal. * = P

    Article Snippet: Mouse mAbs against heparan sulfate (HepSS-1, JM403, 10E4), Δ-heparan sulfate stubs generated by heparinase III (3G10) and keratan sulfate (5D4) were from Seikagaku.

    Techniques: Derivative Assay, SDS Page, Enzyme-linked Immunosorbent Assay

    Binding of MPO by perlecan. Surface-bound perlecan, in gelatin-blocked microplate wells, was incubated with MPO and probed by ELISA using antibody 2C7 against MPO. (A) Binding of MPO to perlecan and effect of prior treatment of perlecan with heparinase III and chondrotinase ABC. (B) Confirmation of heparan sulfate removal by heparinase III by loss of recognition by 10E4 and gain in recognition by 3G10 against heparinase III-derived heparan sulfate stubs. (C) Effect of heparin, heparin sulfate and chondroitin sulfate (100 µg/ml, 10 min, 22°C) on binding of MPO by perlecan. Data are means ± SEM (triplicate determinations from a representative experiment) and are expressed as % normal MPO binding, % normal ELISA signal (10E4 and CSI-076) or % maximal ELISA signal (3G10). In (A) and (B), ELISA signals were corrected for values obtained with non-perlecan coated wells; in (B), ELISA signals were corrected for values obtained with non-perlecan coated wells (blocked with fish gelatin) subject to identical treatments. Treatment with glycosaminoglycans did not significantly reverse background binding of MPO to non-perlecan coated wells (data not shown). * = P

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    Article Title: Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan

    doi: 10.1016/j.matbio.2009.09.005

    Figure Lengend Snippet: Binding of MPO by perlecan. Surface-bound perlecan, in gelatin-blocked microplate wells, was incubated with MPO and probed by ELISA using antibody 2C7 against MPO. (A) Binding of MPO to perlecan and effect of prior treatment of perlecan with heparinase III and chondrotinase ABC. (B) Confirmation of heparan sulfate removal by heparinase III by loss of recognition by 10E4 and gain in recognition by 3G10 against heparinase III-derived heparan sulfate stubs. (C) Effect of heparin, heparin sulfate and chondroitin sulfate (100 µg/ml, 10 min, 22°C) on binding of MPO by perlecan. Data are means ± SEM (triplicate determinations from a representative experiment) and are expressed as % normal MPO binding, % normal ELISA signal (10E4 and CSI-076) or % maximal ELISA signal (3G10). In (A) and (B), ELISA signals were corrected for values obtained with non-perlecan coated wells; in (B), ELISA signals were corrected for values obtained with non-perlecan coated wells (blocked with fish gelatin) subject to identical treatments. Treatment with glycosaminoglycans did not significantly reverse background binding of MPO to non-perlecan coated wells (data not shown). * = P

    Article Snippet: Mouse mAbs against heparan sulfate (HepSS-1, JM403, 10E4), Δ-heparan sulfate stubs generated by heparinase III (3G10) and keratan sulfate (5D4) were from Seikagaku.

    Techniques: Binding Assay, Incubation, Enzyme-linked Immunosorbent Assay, Derivative Assay, Fluorescence In Situ Hybridization

    EGF and VEGF are retained under flow. (A) EGF (1.49 ng) was injected into the input reservoir, pumped through the system at 0.61 mL/min (1.22 mm/sec), and EGF quantified in the output flow by ELISA. Data shown are from the same cartridge either untreated (○) or enzyme-treated (•). FGF-2 (1.01ng - x) is shown for comparison. (B) VEGF was injected into the input reservoir of untreated (0.95ng - ○) or heparinase-treated (0.98ng -•) cartridges, run through the system at 0.66 mL/min (1.32 mm/sec), and VEGF quantified in the output flow by ELISA. Data are representative of at least three runs quantified in Table 4 .

    Journal: PLoS Computational Biology

    Article Title: Endothelial Cell Capture of Heparin-Binding Growth Factors under Flow

    doi: 10.1371/journal.pcbi.1000971

    Figure Lengend Snippet: EGF and VEGF are retained under flow. (A) EGF (1.49 ng) was injected into the input reservoir, pumped through the system at 0.61 mL/min (1.22 mm/sec), and EGF quantified in the output flow by ELISA. Data shown are from the same cartridge either untreated (○) or enzyme-treated (•). FGF-2 (1.01ng - x) is shown for comparison. (B) VEGF was injected into the input reservoir of untreated (0.95ng - ○) or heparinase-treated (0.98ng -•) cartridges, run through the system at 0.66 mL/min (1.32 mm/sec), and VEGF quantified in the output flow by ELISA. Data are representative of at least three runs quantified in Table 4 .

    Article Snippet: Heparinase III (0.01 unit/0.11mL, Seikagaku Corp., Japan; 0.2unit/0.11mL, Sigma Aldrich, St. Louis, MO), chondroitinase ABC (0.2 unit/0.11mL, Seikagaku Corp., Japan) and keratanase (0.33unit/0.11mL, Sigma Aldrich, St. Louis, MO) were utilized to observe their effect on growth factor flow and binding.

    Techniques: Flow Cytometry, Injection, Size-exclusion Chromatography, Enzyme-linked Immunosorbent Assay

    Fibronectin on exosomes isolated from multiple myeloma patients facilitates interaction with bone marrow stromal cells. A , characterization of exosomes from serum of treatment naïve multiple myeloma patients. Exosomes were purified from serum of myeloma patients by ExoQuick precipitation followed by isolation using anti-CD63 conjugated beads. Particle size was analyzed by nanoparticle tracking using a NanoSight 300. Histogram shows two lines representing duplicate analyses. B , ELISA quantification of the levels of fibronectin in exosomes isolated from serum of three myeloma patients. C , syndecan-1 and fibronectin are present on the surface of myeloma patient derived exosomes. Exosomes purified from the serum of myeloma patients using ExoQuick precipitation followed by anti-CD63 magnetic bead isolation were subjected to flow cytometry analysis using an affinity-purified polyclonal goat anti-syndecan-1 IgG antibody ( blue ) or mouse monoclonal PE-conjugated anti-fibronectin antibody ( blue ). Normal goat IgG and mouse IgG1 isotype were used as control ( red ), respectively. Note that syndecan-1 (core protein) was detected on the surface of exosomes only after removal of heparan sulfate chains by heparitinase treatment to expose the epitope. D and E , removal of heparan sulfate chains removes most of the fibronectin from exosomes isolated from the serum of myeloma patients. Exosomes isolated from patient serum were either not treated or treated with heparitinase, and fibronectin levels were quantified by ELISA ( D ) and compared by Western blot ( E ). #, p

    Journal: The Journal of Biological Chemistry

    Article Title: Fibronectin on the Surface of Myeloma Cell-derived Exosomes Mediates Exosome-Cell Interactions *

    doi: 10.1074/jbc.M115.686295

    Figure Lengend Snippet: Fibronectin on exosomes isolated from multiple myeloma patients facilitates interaction with bone marrow stromal cells. A , characterization of exosomes from serum of treatment naïve multiple myeloma patients. Exosomes were purified from serum of myeloma patients by ExoQuick precipitation followed by isolation using anti-CD63 conjugated beads. Particle size was analyzed by nanoparticle tracking using a NanoSight 300. Histogram shows two lines representing duplicate analyses. B , ELISA quantification of the levels of fibronectin in exosomes isolated from serum of three myeloma patients. C , syndecan-1 and fibronectin are present on the surface of myeloma patient derived exosomes. Exosomes purified from the serum of myeloma patients using ExoQuick precipitation followed by anti-CD63 magnetic bead isolation were subjected to flow cytometry analysis using an affinity-purified polyclonal goat anti-syndecan-1 IgG antibody ( blue ) or mouse monoclonal PE-conjugated anti-fibronectin antibody ( blue ). Normal goat IgG and mouse IgG1 isotype were used as control ( red ), respectively. Note that syndecan-1 (core protein) was detected on the surface of exosomes only after removal of heparan sulfate chains by heparitinase treatment to expose the epitope. D and E , removal of heparan sulfate chains removes most of the fibronectin from exosomes isolated from the serum of myeloma patients. Exosomes isolated from patient serum were either not treated or treated with heparitinase, and fibronectin levels were quantified by ELISA ( D ) and compared by Western blot ( E ). #, p

    Article Snippet: For detection of syndecan-1, exosomes bound to anti-CD63 beads were treated with bacterial heparitinase (Seikagaku) for 2 h at 37 °C followed by extensive washing.

    Techniques: Isolation, Purification, Enzyme-linked Immunosorbent Assay, Derivative Assay, Flow Cytometry, Cytometry, Affinity Purification, Western Blot

    Fibronectin is present on the exosome surface and its removal inhibits exosome interaction with target cells. A , fibronectin is present on the surface of exosomes. Exosomes from aggressive CAG cells, purified by ultracentrifugation and excluded by an iodixanol cushion, were captured either using anti-CD63 magnetic beads ( left panel ) or using heparin-agarose beads ( right panel ) and subjected to flow cytometry analysis using a mouse monoclonal PE-conjugated anti-fibronectin antibody ( blue histogram ). PE-conjugated isotype-matched antibody was used as a control ( orange histogram ). B , removal of heparan sulfate from the exosome surface removes most of the fibronectin associated with the exosome. Left panel , exosomes were either not treated or treated with bacterial heparitinase (1.5 millunits/ml heparitinase for 3 h at 37 °C followed by addition of fresh enzyme and incubation overnight), a heparan sulfate degrading enzyme, and fibronectin levels were quantified by ELISA. The data are expressed as means ± S.D. #, p

    Journal: The Journal of Biological Chemistry

    Article Title: Fibronectin on the Surface of Myeloma Cell-derived Exosomes Mediates Exosome-Cell Interactions *

    doi: 10.1074/jbc.M115.686295

    Figure Lengend Snippet: Fibronectin is present on the exosome surface and its removal inhibits exosome interaction with target cells. A , fibronectin is present on the surface of exosomes. Exosomes from aggressive CAG cells, purified by ultracentrifugation and excluded by an iodixanol cushion, were captured either using anti-CD63 magnetic beads ( left panel ) or using heparin-agarose beads ( right panel ) and subjected to flow cytometry analysis using a mouse monoclonal PE-conjugated anti-fibronectin antibody ( blue histogram ). PE-conjugated isotype-matched antibody was used as a control ( orange histogram ). B , removal of heparan sulfate from the exosome surface removes most of the fibronectin associated with the exosome. Left panel , exosomes were either not treated or treated with bacterial heparitinase (1.5 millunits/ml heparitinase for 3 h at 37 °C followed by addition of fresh enzyme and incubation overnight), a heparan sulfate degrading enzyme, and fibronectin levels were quantified by ELISA. The data are expressed as means ± S.D. #, p

    Article Snippet: For detection of syndecan-1, exosomes bound to anti-CD63 beads were treated with bacterial heparitinase (Seikagaku) for 2 h at 37 °C followed by extensive washing.

    Techniques: Purification, Magnetic Beads, Flow Cytometry, Cytometry, Incubation, Enzyme-linked Immunosorbent Assay

    Model of exosome-target cell interaction mediated by fibronectin. Step 1 , fibronectin ( FN ) is captured on the surface of exosomes by heparan sulfate proteoglycans ( HSPG ). Step 2 , fibronectin, on exosomes binds to heparan sulfate ( HS ) on the surface of the target cell. Step 3 , removal of exosome heparan sulfate or cell surface heparan sulfate with heparitinase, addition of exogenous heparin or heparin mimetics, addition of Hep-II domain-containing fragment of fibronectin, or exposure to antibody against the Hep-II domain of fibronectin dramatically diminishes exosome interaction with target cells.

    Journal: The Journal of Biological Chemistry

    Article Title: Fibronectin on the Surface of Myeloma Cell-derived Exosomes Mediates Exosome-Cell Interactions *

    doi: 10.1074/jbc.M115.686295

    Figure Lengend Snippet: Model of exosome-target cell interaction mediated by fibronectin. Step 1 , fibronectin ( FN ) is captured on the surface of exosomes by heparan sulfate proteoglycans ( HSPG ). Step 2 , fibronectin, on exosomes binds to heparan sulfate ( HS ) on the surface of the target cell. Step 3 , removal of exosome heparan sulfate or cell surface heparan sulfate with heparitinase, addition of exogenous heparin or heparin mimetics, addition of Hep-II domain-containing fragment of fibronectin, or exposure to antibody against the Hep-II domain of fibronectin dramatically diminishes exosome interaction with target cells.

    Article Snippet: For detection of syndecan-1, exosomes bound to anti-CD63 beads were treated with bacterial heparitinase (Seikagaku) for 2 h at 37 °C followed by extensive washing.

    Techniques:

    Exosome-target cell interaction mediated by fibronectin impacts cell behavior. A , exosome interaction with RPMI-8226 cells activates p38 and ERK signaling. An antibody array that simultaneously examines the phosphorylation levels of 43 different protein kinases was utilized to determine what signaling pathways were activated when myeloma-derived exosomes interacted with target cells. RPMI-8226 cells were incubated with or without exosomes isolated from aggressive myeloma cells (CAG cells expressing high heparanase), cell lysates were exposed to membranes, and the membranes were probed with a phosphotyrosine specific antibody. Phosphorylated p38 and ERK ( circled ) were enhanced in cells incubated with the exosomes. The different phospho kinases that are activated in RPMI-8226 cells independent of the addition of exosomes are shown by arrows. Duplicate dots at the corners represent phosphotyrosine positive controls. B , RPMI-8226 cells were treated with exosomes (100 μg/ml) secreted by control or aggressive myeloma cells for 20 min and analyzed for phosphorylated p38 by Western blot. Total p38 serves as the loading control. To determine the role of cell surface heparan sulfate in mediating exosome-induced signaling, RPMI-8266 cells were treated with bacterial heparitinase for 2 h prior to the addition of exosomes from aggressive myeloma cells. C , MMP-9 and DKK1, two downstream target genes of activated p38, are up-regulated following the interaction of myeloma-derived exosomes with the RPMI 8226 cells. RPMI 8266 myeloma cells were incubated with or without exosomes, and DKK1 and MMP-9 mRNA expression in these cells was assessed using real time PCR and normalized using actin expression. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Fibronectin on the Surface of Myeloma Cell-derived Exosomes Mediates Exosome-Cell Interactions *

    doi: 10.1074/jbc.M115.686295

    Figure Lengend Snippet: Exosome-target cell interaction mediated by fibronectin impacts cell behavior. A , exosome interaction with RPMI-8226 cells activates p38 and ERK signaling. An antibody array that simultaneously examines the phosphorylation levels of 43 different protein kinases was utilized to determine what signaling pathways were activated when myeloma-derived exosomes interacted with target cells. RPMI-8226 cells were incubated with or without exosomes isolated from aggressive myeloma cells (CAG cells expressing high heparanase), cell lysates were exposed to membranes, and the membranes were probed with a phosphotyrosine specific antibody. Phosphorylated p38 and ERK ( circled ) were enhanced in cells incubated with the exosomes. The different phospho kinases that are activated in RPMI-8226 cells independent of the addition of exosomes are shown by arrows. Duplicate dots at the corners represent phosphotyrosine positive controls. B , RPMI-8226 cells were treated with exosomes (100 μg/ml) secreted by control or aggressive myeloma cells for 20 min and analyzed for phosphorylated p38 by Western blot. Total p38 serves as the loading control. To determine the role of cell surface heparan sulfate in mediating exosome-induced signaling, RPMI-8266 cells were treated with bacterial heparitinase for 2 h prior to the addition of exosomes from aggressive myeloma cells. C , MMP-9 and DKK1, two downstream target genes of activated p38, are up-regulated following the interaction of myeloma-derived exosomes with the RPMI 8226 cells. RPMI 8266 myeloma cells were incubated with or without exosomes, and DKK1 and MMP-9 mRNA expression in these cells was assessed using real time PCR and normalized using actin expression. *, p

    Article Snippet: For detection of syndecan-1, exosomes bound to anti-CD63 beads were treated with bacterial heparitinase (Seikagaku) for 2 h at 37 °C followed by extensive washing.

    Techniques: Ab Array, Derivative Assay, Incubation, Isolation, Expressing, Western Blot, Real-time Polymerase Chain Reaction

    Exosome-target cell interaction is mediated by heparan sulfate chains on target cells. A , confocal microscopy analysis of polarized or nonpolarized CAG myeloma cells following addition of CD63-RFP exosomes. Exosomes preferentially interact with heparan sulfate-rich uropods of polarized cells but are widely distributed on nonpolarized cells. B , depletion of heparan sulfate chains on myeloma cells decreases exosome-target cell interaction. RPMI-8226 cells were untreated or treated with heparitinase and washed, and their interactions with exosomes were analyzed by confocal microscopy. Right panel , quantitative data from a similar experiment analyzed by flow cytometry. #, p

    Journal: The Journal of Biological Chemistry

    Article Title: Fibronectin on the Surface of Myeloma Cell-derived Exosomes Mediates Exosome-Cell Interactions *

    doi: 10.1074/jbc.M115.686295

    Figure Lengend Snippet: Exosome-target cell interaction is mediated by heparan sulfate chains on target cells. A , confocal microscopy analysis of polarized or nonpolarized CAG myeloma cells following addition of CD63-RFP exosomes. Exosomes preferentially interact with heparan sulfate-rich uropods of polarized cells but are widely distributed on nonpolarized cells. B , depletion of heparan sulfate chains on myeloma cells decreases exosome-target cell interaction. RPMI-8226 cells were untreated or treated with heparitinase and washed, and their interactions with exosomes were analyzed by confocal microscopy. Right panel , quantitative data from a similar experiment analyzed by flow cytometry. #, p

    Article Snippet: For detection of syndecan-1, exosomes bound to anti-CD63 beads were treated with bacterial heparitinase (Seikagaku) for 2 h at 37 °C followed by extensive washing.

    Techniques: Confocal Microscopy, Flow Cytometry, Cytometry

    Co-immunoprecipitation of CD81 and GPC3. The rat liver lysates without heparitinase treatment were incubated with anti-CD81 monoclonal antibody or control IgG, followed by precipitation with agarose A/G plus beads. Precipitates were separated by Western

    Journal: The American Journal of Pathology

    Article Title: Investigation of the Role of Glypican 3 in Liver Regeneration and Hepatocyte Proliferation

    doi: 10.2353/ajpath.2009.081129

    Figure Lengend Snippet: Co-immunoprecipitation of CD81 and GPC3. The rat liver lysates without heparitinase treatment were incubated with anti-CD81 monoclonal antibody or control IgG, followed by precipitation with agarose A/G plus beads. Precipitates were separated by Western

    Article Snippet: For HS chain elimination, 100 μg of protein extract from freshly isolated rat hepatocytes and total rat liver was treated with 5 microunits of heparitinase enzyme (Seikagaku, Tokyo, Japan) and 1 mmol/L CaCl2 for 3 hours.

    Techniques: Immunoprecipitation, Incubation, Western Blot