proteinase k Millipore Search Results


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  • 95
    Millipore proteinase k
    Recognition of blastospores, conidia, and beads by Manduca hemocytes in vitro . Monolayers were exposed to wild-type (WT) or Δ Mcl1 (MU) M. anisopliae cells treated with collagenase (Coll), <t>proteinase</t> K (Pro K), lyticase (Lyt), DTT, poly( l -lysine)
    Proteinase K, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 20358 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher proteinase k
    Treatment of needle proteins with proteinase K, lipoprotein lipase, and polymyxin B retains NF-κB/AP-1 activation. Needle proteins (1 μg/ml) (A, B, and C) and LcrG (1 μg/ml) (B and C), PBS, flagellin (1 μg/ml) (A), Pam3
    Proteinase K, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 16903 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Merck KGaA proteinase k
    Retardation assay of pELF1 DNAs excised from PFGE or SDS-PFGE gels. DNA bands of pELF1 were excised from PFGE gel (proteinase K treatment +) or SDS-PFGE gel (proteinase K treatment –), and digested  with  Sac I (lanes 3 and 4), and  Sma I (lanes 5 and 6). After digestion, the samples were subjected to PFGE. MM, Low Range PFG Marker; 1, pELF1 excised from PFGE gel; 2, pELF1 excised from SDS-PFGE gel; 3,  Sac I-treated pELF1 excised from PFGE gel; 4,  Sac I-treated pELF1 excised from SDS-PFGE gel; 5,  Sma I-treated pELF1 excised from PFGE gel; 6,  Sma I-treated pELF1 excised from SDS-PFGE gel. N. D.; not digested.
    Proteinase K, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 97/100, based on 717 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Merck KGaA recombinant proteinase k
    Retardation assay of pELF1 DNAs excised from PFGE or SDS-PFGE gels. DNA bands of pELF1 were excised from PFGE gel (proteinase K treatment +) or SDS-PFGE gel (proteinase K treatment –), and digested  with  Sac I (lanes 3 and 4), and  Sma I (lanes 5 and 6). After digestion, the samples were subjected to PFGE. MM, Low Range PFG Marker; 1, pELF1 excised from PFGE gel; 2, pELF1 excised from SDS-PFGE gel; 3,  Sac I-treated pELF1 excised from PFGE gel; 4,  Sac I-treated pELF1 excised from SDS-PFGE gel; 5,  Sma I-treated pELF1 excised from PFGE gel; 6,  Sma I-treated pELF1 excised from SDS-PFGE gel. N. D.; not digested.
    Recombinant Proteinase K, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Millipore nuclease free proteinase k
    Retardation assay of pELF1 DNAs excised from PFGE or SDS-PFGE gels. DNA bands of pELF1 were excised from PFGE gel (proteinase K treatment +) or SDS-PFGE gel (proteinase K treatment –), and digested  with  Sac I (lanes 3 and 4), and  Sma I (lanes 5 and 6). After digestion, the samples were subjected to PFGE. MM, Low Range PFG Marker; 1, pELF1 excised from PFGE gel; 2, pELF1 excised from SDS-PFGE gel; 3,  Sac I-treated pELF1 excised from PFGE gel; 4,  Sac I-treated pELF1 excised from SDS-PFGE gel; 5,  Sma I-treated pELF1 excised from PFGE gel; 6,  Sma I-treated pELF1 excised from SDS-PFGE gel. N. D.; not digested.
    Nuclease Free Proteinase K, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore proteinase k agarose
    <t>Proteinase</t> K treatment reduces the effect of conditioned medium. Growth curves of B. subtilis 168 infected by phi3T at MOI=0.1, in control and conditioned media, with and without pre-treatment with proteinase K. Data represent average of 3 technical replicates, and error bars represent standard error.
    Proteinase K Agarose, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore dnase free proteinase k
    <t>Proteinase</t> K treatment reduces the effect of conditioned medium. Growth curves of B. subtilis 168 infected by phi3T at MOI=0.1, in control and conditioned media, with and without pre-treatment with proteinase K. Data represent average of 3 technical replicates, and error bars represent standard error.
    Dnase Free Proteinase K, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rnase free proteinase k
    <t>Proteinase</t> K treatment reduces the effect of conditioned medium. Growth curves of B. subtilis 168 infected by phi3T at MOI=0.1, in control and conditioned media, with and without pre-treatment with proteinase K. Data represent average of 3 technical replicates, and error bars represent standard error.
    Rnase Free Proteinase K, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore proteinase k agarose beads
    Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with <t>proteinase</t> K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.
    Proteinase K Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore protease k treatment
    Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with <t>proteinase</t> K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.
    Protease K Treatment, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore proteinase k inhibitor
    Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with <t>proteinase</t> K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.
    Proteinase K Inhibitor, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher proteinase k solution
    Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with <t>proteinase</t> K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.
    Proteinase K Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1330 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Millipore proteinase k acrylic beads
    Effects of glial signals on the presence of autaptic activity in single RGCs Columns indicate the fraction of single RGCs that showed spontaneous, evoked or asynchronous EACs when cultured under different conditions. RGCs were grown in the absence of glial cells ( n = 47; RGC), in direct contact with glial cells from optic nerve ( n = 26; +OPN), in the presence of GCM ( n = 36; +GCM), in the presence of GCM that had been digested before with bead-coupled <t>proteinase</t> K ( n = 15; +GCM+ProtK) and in the presence of GCM and TTX ( n = 18; +GCM+TTX). Whole-cell EACs were recorded with the perforated-patch technique at a holding potential of −70 mV and analysed in a blinded fashion. Asterisks denote significant changes compared to glia-free conditions ( P
    Proteinase K Acrylic Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Millipore protease k 2
    Effects of glial signals on the presence of autaptic activity in single RGCs Columns indicate the fraction of single RGCs that showed spontaneous, evoked or asynchronous EACs when cultured under different conditions. RGCs were grown in the absence of glial cells ( n = 47; RGC), in direct contact with glial cells from optic nerve ( n = 26; +OPN), in the presence of GCM ( n = 36; +GCM), in the presence of GCM that had been digested before with bead-coupled <t>proteinase</t> K ( n = 15; +GCM+ProtK) and in the presence of GCM and TTX ( n = 18; +GCM+TTX). Whole-cell EACs were recorded with the perforated-patch technique at a holding potential of −70 mV and analysed in a blinded fashion. Asterisks denote significant changes compared to glia-free conditions ( P
    Protease K 2, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Millipore no 24627 188 proteinase k
    Effects of glial signals on the presence of autaptic activity in single RGCs Columns indicate the fraction of single RGCs that showed spontaneous, evoked or asynchronous EACs when cultured under different conditions. RGCs were grown in the absence of glial cells ( n = 47; RGC), in direct contact with glial cells from optic nerve ( n = 26; +OPN), in the presence of GCM ( n = 36; +GCM), in the presence of GCM that had been digested before with bead-coupled <t>proteinase</t> K ( n = 15; +GCM+ProtK) and in the presence of GCM and TTX ( n = 18; +GCM+TTX). Whole-cell EACs were recorded with the perforated-patch technique at a holding potential of −70 mV and analysed in a blinded fashion. Asterisks denote significant changes compared to glia-free conditions ( P
    No 24627 188 Proteinase K, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Millipore proteinase k conjugated to agarose beads
    FacX is resistant to boiling, but sensitive to Proteinase K. (A) Conditioned media was boiled for 15 min and utilized in the sporulation assay ( Fig 2A ) with strain MF1913 (P hy-spank - kinA ). (B) Conditioned media was treated with <t>proteinase</t> K and utilized in the sporulation assay with strain MF1913 (P hy-spank - kinA ). When indicated, KinA was induced with IPTG (20 μM). Cells were grown for 2 hrs at 37°C before image capture. Membranes were stained with TMA.
    Proteinase K Conjugated To Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore proteinase k lactic acid
    FacX is resistant to boiling, but sensitive to Proteinase K. (A) Conditioned media was boiled for 15 min and utilized in the sporulation assay ( Fig 2A ) with strain MF1913 (P hy-spank - kinA ). (B) Conditioned media was treated with <t>proteinase</t> K and utilized in the sporulation assay with strain MF1913 (P hy-spank - kinA ). When indicated, KinA was induced with IPTG (20 μM). Cells were grown for 2 hrs at 37°C before image capture. Membranes were stained with TMA.
    Proteinase K Lactic Acid, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Millipore hpse proteinase k agarose beads
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    Hpse Proteinase K Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 76/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Millipore f4 80 staining required proteinase k
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    F4 80 Staining Required Proteinase K, supplied by Millipore, used in various techniques. Bioz Stars score: 82/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore proteinase k treated torula yeast rna
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    Proteinase K Treated Torula Yeast Rna, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore proteinase k 500 unit benzonase endonuclease
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    Proteinase K 500 Unit Benzonase Endonuclease, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore protease k calbiochem treated bacterial lysates
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    Protease K Calbiochem Treated Bacterial Lysates, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore sodium dodecyl sulfate sds protease k
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    Sodium Dodecyl Sulfate Sds Protease K, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore proteinase k protease inhibitor cocktail
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    Proteinase K Protease Inhibitor Cocktail, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore pasteur pipettes novagen pellet paint coprecipitant phenol proteinase k transcription stop buffer
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    Pasteur Pipettes Novagen Pellet Paint Coprecipitant Phenol Proteinase K Transcription Stop Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore p4504 proteinase k
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    P4504 Proteinase K, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore genelute mammalian genomic dna miniprep kit
    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
    Genelute Mammalian Genomic Dna Miniprep Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1955 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    <t>Proteinase-K</t> treated <t>HPSE</t> results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =
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    Millipore protk
    Measurement of the degree of sialylation by SNA lectin inhibition ELISA. % SNA lectin binding after pre-incubation A ) with <t>IVIg,</t> IVIg-SA (+) or IVIg-SA (−) B ) with Fab and Fc fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−) C ) with Fab or <t>protK</t> digested Fab fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−) D ) with Fc or protK digested Fc fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−). Data represents mean ± SEM, n = 3.
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    Spermiograms and in vitro fertilization assays. Spermiograms from PCI +/+ ( a ) and from PCI +/– ( b ) were normal, whereas in spermiograms from PCI –/– mice ( c ) immature and malformed cells were prevalent. ( d ) In in vitro fertilization assays, sperm obtained from PCI +/– mice were able to bind and subsequently fertilize PCI +/+ oocytes. Sperm obtained from PCI –/– males failed to fertilize zona <t>pellucida–containing</t> ( e ) or zona pellucida–free ( f ) oocytes.
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    Image Search Results


    Recognition of blastospores, conidia, and beads by Manduca hemocytes in vitro . Monolayers were exposed to wild-type (WT) or Δ Mcl1 (MU) M. anisopliae cells treated with collagenase (Coll), proteinase K (Pro K), lyticase (Lyt), DTT, poly( l -lysine)

    Journal:

    Article Title: A collagenous protective coat enables Metarhizium anisopliae to evade insect immune responses

    doi: 10.1073/pnas.0601951103

    Figure Lengend Snippet: Recognition of blastospores, conidia, and beads by Manduca hemocytes in vitro . Monolayers were exposed to wild-type (WT) or Δ Mcl1 (MU) M. anisopliae cells treated with collagenase (Coll), proteinase K (Pro K), lyticase (Lyt), DTT, poly( l -lysine)

    Article Snippet: In some experiments, fungal cells were fixed in 4% formaldehyde or pretreated for 1 h in PBS containing either DTT, poly( l -lysine), lyticase, proteinase K, or collagenase (Sigma) (the enzymes at 200 μg/ml) before assaying.

    Techniques: In Vitro

    SAMMSON  expression increases rRNA processing thus promoting protein synthesis. ( a ) Heatmap representation of pre-rRNA analysis in Mel-ST cells overexpressing  SAMMSON  ( SAM  O/E) relative to cells transfected with an empty (Ctrl). Each pre-RNA intermediates detected was quantified with a PhosphorImager; n=3. ( b ) Quantification of relative protein synthesis (%) after a 10-minute pulse with puromycin and subsequent cytosol(Cyto)-mitochondria(Mito)-mitoplast(Mitopl) fractionation in Mel-ST cells described in  a . Error bars represent mean ± s.e.m. Total and Cyto, n=4; Mito and Mitopl, n=3. ( c ) Quantification of relative protein synthesis (%) after a 10-minute pulse with puromycin and subsequent cytosol(Cyto)-mitochondria(Mito)-mitoplast(Mitopl) fractionation in LCL cells as described in  Figure 1a ; n=5. ( d )  p32  relative expression measured by RT-qPCR in LCL cells as described in  c ; n=6. ( e ) Quantification of p32 protein levels relative to the control fraction in LCL cells described in  c  after cytosol(Cyto)-mitochondria(Mito)-mitoplast(Mitopl) fractionation; n=6. ( f ) Quantification of p32 protein levels relative to the control fraction after cytosol(Cyto)-mitochondria(Mito)-proteinase K-treated mitochondria(Mito+PK) fractionation in LCL cells as described in  Figure 1a ; n=4. ( g ) Puromycin quantification (each point represents the average of the quantification of three different fields) of tumors as described in  Figure 1e-g ; n=8. Box boundaries represent 25th and 75th percentiles; center line represents the median; whiskers, last data point within ±1.5 interquartile range.  P  values were calculated by paired two-tailed Student’s t-test. *  P

    Journal: Nature structural & molecular biology

    Article Title: SAMMSON fosters cancer cell fitness by enhancing concertedly mitochondrial and cytosolic translation

    doi: 10.1038/s41594-018-0143-4

    Figure Lengend Snippet: SAMMSON expression increases rRNA processing thus promoting protein synthesis. ( a ) Heatmap representation of pre-rRNA analysis in Mel-ST cells overexpressing SAMMSON ( SAM O/E) relative to cells transfected with an empty (Ctrl). Each pre-RNA intermediates detected was quantified with a PhosphorImager; n=3. ( b ) Quantification of relative protein synthesis (%) after a 10-minute pulse with puromycin and subsequent cytosol(Cyto)-mitochondria(Mito)-mitoplast(Mitopl) fractionation in Mel-ST cells described in a . Error bars represent mean ± s.e.m. Total and Cyto, n=4; Mito and Mitopl, n=3. ( c ) Quantification of relative protein synthesis (%) after a 10-minute pulse with puromycin and subsequent cytosol(Cyto)-mitochondria(Mito)-mitoplast(Mitopl) fractionation in LCL cells as described in Figure 1a ; n=5. ( d ) p32 relative expression measured by RT-qPCR in LCL cells as described in c ; n=6. ( e ) Quantification of p32 protein levels relative to the control fraction in LCL cells described in c after cytosol(Cyto)-mitochondria(Mito)-mitoplast(Mitopl) fractionation; n=6. ( f ) Quantification of p32 protein levels relative to the control fraction after cytosol(Cyto)-mitochondria(Mito)-proteinase K-treated mitochondria(Mito+PK) fractionation in LCL cells as described in Figure 1a ; n=4. ( g ) Puromycin quantification (each point represents the average of the quantification of three different fields) of tumors as described in Figure 1e-g ; n=8. Box boundaries represent 25th and 75th percentiles; center line represents the median; whiskers, last data point within ±1.5 interquartile range. P values were calculated by paired two-tailed Student’s t-test. * P

    Article Snippet: For proteinase K experiments, purified mitochondria were resuspended in 1× sucrose buffer (SB: HEPES 10 mM, sucrose 280 mM, EGTA 1 mM pH 7,4) supplemented with 100 µg mL-1 proteinase K (Sigma-Aldrich) and with 60 U mL−1 Superase-In (Ambion) for 30 min at 4 °C rotating.

    Techniques: Expressing, Transfection, Fractionation, Quantitative RT-PCR, Two Tailed Test

    Percent detachment of preformed biofilms obtained with 18 ocular S. haemolyticus isolates after treatment with NaIO 4 , proteinase K or DNase I.

    Journal: Frontiers in Microbiology

    Article Title: Biofilm Formation by ica-Negative Ocular Isolates of Staphylococcus haemolyticus

    doi: 10.3389/fmicb.2018.02687

    Figure Lengend Snippet: Percent detachment of preformed biofilms obtained with 18 ocular S. haemolyticus isolates after treatment with NaIO 4 , proteinase K or DNase I.

    Article Snippet: Detachment Assay of Biofilm We performed detachment assays to determine the components of biofilm matrix by the method of using reagent and enzymes (i) 40 mM NaIO4 (Sigma; S1878), (ii) 0.1 mg/ml proteinase K (Sigma; P2308), and (iii) 0.5 mg/ml DNase I (Sigma; DN25).

    Techniques:

    The figure shows the orthogonal views of CLSM images. (A) Biofilms formed by ATCC 35984 and SHN65 in the presence of proteinase K and DNase I, and (B) Detachment of preformed biofilms by adding NaIO 4 , proteinase K, and DNase I. Acquired the z-stacks of each chamber by CLSM with a Leica TCS SP5 confocal scanning system (Leica Microsystem, Mannheim, Germany) 63× oil objective lens.

    Journal: Frontiers in Microbiology

    Article Title: Biofilm Formation by ica-Negative Ocular Isolates of Staphylococcus haemolyticus

    doi: 10.3389/fmicb.2018.02687

    Figure Lengend Snippet: The figure shows the orthogonal views of CLSM images. (A) Biofilms formed by ATCC 35984 and SHN65 in the presence of proteinase K and DNase I, and (B) Detachment of preformed biofilms by adding NaIO 4 , proteinase K, and DNase I. Acquired the z-stacks of each chamber by CLSM with a Leica TCS SP5 confocal scanning system (Leica Microsystem, Mannheim, Germany) 63× oil objective lens.

    Article Snippet: Detachment Assay of Biofilm We performed detachment assays to determine the components of biofilm matrix by the method of using reagent and enzymes (i) 40 mM NaIO4 (Sigma; S1878), (ii) 0.1 mg/ml proteinase K (Sigma; P2308), and (iii) 0.5 mg/ml DNase I (Sigma; DN25).

    Techniques: Confocal Laser Scanning Microscopy

    Treatment of needle proteins with proteinase K, lipoprotein lipase, and polymyxin B retains NF-κB/AP-1 activation. Needle proteins (1 μg/ml) (A, B, and C) and LcrG (1 μg/ml) (B and C), PBS, flagellin (1 μg/ml) (A), Pam3

    Journal: Infection and Immunity

    Article Title: Type III Secretion Needle Proteins Induce Cell Signaling and Cytokine Secretion via Toll-Like Receptors

    doi: 10.1128/IAI.01705-14

    Figure Lengend Snippet: Treatment of needle proteins with proteinase K, lipoprotein lipase, and polymyxin B retains NF-κB/AP-1 activation. Needle proteins (1 μg/ml) (A, B, and C) and LcrG (1 μg/ml) (B and C), PBS, flagellin (1 μg/ml) (A), Pam3

    Article Snippet: Needle proteins and flagellin (standard flagellin from Salmonella Typhimurium; Invivogen) were incubated with 40 μg/ml proteinase K (Thermo-Fisher) at 37°C for 16 h. Proteinase K was then inactivated with 1.6 mg/ml phenylmethylsulfonyl fluoride (PMSF; Sigma-Aldrich, St. Louis, MO).

    Techniques: Activation Assay

    Retardation assay of pELF1 DNAs excised from PFGE or SDS-PFGE gels. DNA bands of pELF1 were excised from PFGE gel (proteinase K treatment +) or SDS-PFGE gel (proteinase K treatment –), and digested  with  Sac I (lanes 3 and 4), and  Sma I (lanes 5 and 6). After digestion, the samples were subjected to PFGE. MM, Low Range PFG Marker; 1, pELF1 excised from PFGE gel; 2, pELF1 excised from SDS-PFGE gel; 3,  Sac I-treated pELF1 excised from PFGE gel; 4,  Sac I-treated pELF1 excised from SDS-PFGE gel; 5,  Sma I-treated pELF1 excised from PFGE gel; 6,  Sma I-treated pELF1 excised from SDS-PFGE gel. N. D.; not digested.

    Journal: Frontiers in Microbiology

    Article Title: Novel Multidrug-Resistant Enterococcal Mobile Linear Plasmid pELF1 Encoding vanA and vanM Gene Clusters From a Japanese Vancomycin-Resistant Enterococci Isolate

    doi: 10.3389/fmicb.2019.02568

    Figure Lengend Snippet: Retardation assay of pELF1 DNAs excised from PFGE or SDS-PFGE gels. DNA bands of pELF1 were excised from PFGE gel (proteinase K treatment +) or SDS-PFGE gel (proteinase K treatment –), and digested with Sac I (lanes 3 and 4), and Sma I (lanes 5 and 6). After digestion, the samples were subjected to PFGE. MM, Low Range PFG Marker; 1, pELF1 excised from PFGE gel; 2, pELF1 excised from SDS-PFGE gel; 3, Sac I-treated pELF1 excised from PFGE gel; 4, Sac I-treated pELF1 excised from SDS-PFGE gel; 5, Sma I-treated pELF1 excised from PFGE gel; 6, Sma I-treated pELF1 excised from SDS-PFGE gel. N. D.; not digested.

    Article Snippet: Agarose plugs (1%) containing embedded enterococci were treated with lysozyme (Roche Diagnostics K.K, Minneapolis, MN, United States) solution (10 mg/ml) at 37°C for 6 h, followed by treatment with proteinase K (Merck Millipore, Darmstadt, Germany) solution (60 mAnson U/ml) at 50°C for 48 h. After washing the plugs with wash buffer (20 mM Tris-HCl, pH 8.0; 50 mM EDTA), proteinase K was inhibited using phenylmethylsulfonyl fluoride (PMSF) solution (20 mM Tris-HCl, pH 8.0, 50 mM EDTA, and 1 mM PMSF).

    Techniques: Marker

    PFGE of the restriction fragments of pELF1 with proteinase K treatment. Lanes: Low Range PFG Marker; proteinase K-treatment only; proteinase K-treated Sal I digests; proteinase K-treated Sma I digests; proteinase K-treated Eag I digests. N. D., not digested.

    Journal: Frontiers in Microbiology

    Article Title: Novel Multidrug-Resistant Enterococcal Mobile Linear Plasmid pELF1 Encoding vanA and vanM Gene Clusters From a Japanese Vancomycin-Resistant Enterococci Isolate

    doi: 10.3389/fmicb.2019.02568

    Figure Lengend Snippet: PFGE of the restriction fragments of pELF1 with proteinase K treatment. Lanes: Low Range PFG Marker; proteinase K-treatment only; proteinase K-treated Sal I digests; proteinase K-treated Sma I digests; proteinase K-treated Eag I digests. N. D., not digested.

    Article Snippet: Agarose plugs (1%) containing embedded enterococci were treated with lysozyme (Roche Diagnostics K.K, Minneapolis, MN, United States) solution (10 mg/ml) at 37°C for 6 h, followed by treatment with proteinase K (Merck Millipore, Darmstadt, Germany) solution (60 mAnson U/ml) at 50°C for 48 h. After washing the plugs with wash buffer (20 mM Tris-HCl, pH 8.0; 50 mM EDTA), proteinase K was inhibited using phenylmethylsulfonyl fluoride (PMSF) solution (20 mM Tris-HCl, pH 8.0, 50 mM EDTA, and 1 mM PMSF).

    Techniques: Marker

    PFGE of the AA708 strain. Lanes: Low Range PFG Marker; AA708 without proteinase K treatment; AA708 with proteinase K treatment; AA708 with both proteinase K and S1 nuclease treatment.

    Journal: Frontiers in Microbiology

    Article Title: Novel Multidrug-Resistant Enterococcal Mobile Linear Plasmid pELF1 Encoding vanA and vanM Gene Clusters From a Japanese Vancomycin-Resistant Enterococci Isolate

    doi: 10.3389/fmicb.2019.02568

    Figure Lengend Snippet: PFGE of the AA708 strain. Lanes: Low Range PFG Marker; AA708 without proteinase K treatment; AA708 with proteinase K treatment; AA708 with both proteinase K and S1 nuclease treatment.

    Article Snippet: Agarose plugs (1%) containing embedded enterococci were treated with lysozyme (Roche Diagnostics K.K, Minneapolis, MN, United States) solution (10 mg/ml) at 37°C for 6 h, followed by treatment with proteinase K (Merck Millipore, Darmstadt, Germany) solution (60 mAnson U/ml) at 50°C for 48 h. After washing the plugs with wash buffer (20 mM Tris-HCl, pH 8.0; 50 mM EDTA), proteinase K was inhibited using phenylmethylsulfonyl fluoride (PMSF) solution (20 mM Tris-HCl, pH 8.0, 50 mM EDTA, and 1 mM PMSF).

    Techniques: Marker

    SDS-PFGE of the AA708 strain. Lanes: Low Range PFG Marker; AA708 with proteinase K treatment; AA708 without proteinase K treatment; AA708 with proteinase K and S1 nuclease treatment.

    Journal: Frontiers in Microbiology

    Article Title: Novel Multidrug-Resistant Enterococcal Mobile Linear Plasmid pELF1 Encoding vanA and vanM Gene Clusters From a Japanese Vancomycin-Resistant Enterococci Isolate

    doi: 10.3389/fmicb.2019.02568

    Figure Lengend Snippet: SDS-PFGE of the AA708 strain. Lanes: Low Range PFG Marker; AA708 with proteinase K treatment; AA708 without proteinase K treatment; AA708 with proteinase K and S1 nuclease treatment.

    Article Snippet: Agarose plugs (1%) containing embedded enterococci were treated with lysozyme (Roche Diagnostics K.K, Minneapolis, MN, United States) solution (10 mg/ml) at 37°C for 6 h, followed by treatment with proteinase K (Merck Millipore, Darmstadt, Germany) solution (60 mAnson U/ml) at 50°C for 48 h. After washing the plugs with wash buffer (20 mM Tris-HCl, pH 8.0; 50 mM EDTA), proteinase K was inhibited using phenylmethylsulfonyl fluoride (PMSF) solution (20 mM Tris-HCl, pH 8.0, 50 mM EDTA, and 1 mM PMSF).

    Techniques: Marker

    Proteinase K treatment reduces the effect of conditioned medium. Growth curves of B. subtilis 168 infected by phi3T at MOI=0.1, in control and conditioned media, with and without pre-treatment with proteinase K. Data represent average of 3 technical replicates, and error bars represent standard error.

    Journal: Nature

    Article Title: Communication between viruses guides lysis-lysogeny decisions

    doi: 10.1038/nature21049

    Figure Lengend Snippet: Proteinase K treatment reduces the effect of conditioned medium. Growth curves of B. subtilis 168 infected by phi3T at MOI=0.1, in control and conditioned media, with and without pre-treatment with proteinase K. Data represent average of 3 technical replicates, and error bars represent standard error.

    Article Snippet: For the Proteinase K assay 7.5 mg (per reaction) of Proteinase K–Agarose from Tritirachium album (Sigma, CAT# P9290) were washed twice with 750 µl of sterile water and then resuspended with 750 µl of LB supplemented with 0.1 mM MnCl2 and 5 mM MgCl2 .

    Techniques: Infection

    Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with proteinase K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.

    Journal: Journal of Virology

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids

    doi: 10.1128/JVI.01218-12

    Figure Lengend Snippet: Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with proteinase K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.

    Article Snippet: HepG2 HBV capsids in sucrose fractions were digested for 1.5 h with proteinase K-agarose beads (Sigma) at 37°C with gentle agitation.

    Techniques: Purification, Western Blot, SDS Page, Staining

    Endogenous kinase reactions with virion-derived HBV capsids. HBV capsids were released from virions purified from the medium of HBV-transfected HepG2 cells by NP-40 treatment. One control aliquot was removed, and the remaining virion-derived capsids were digested by proteinase K. The untreated (lane 1) or proteinase K-treated (lanes 2 to 5), virion-derived capsids (ca. 6 ng per reaction) were phosphorylated by the encapsidated kinase in endogenous kinase reactions in the presence of the indicated kinase inhibitors (lanes 3 to 5) or DMSO control (lane 2). Kinase inhibitors used included CDK2 inhibitor III (lane 3, 250 μM, 500× IC 50 for CDK2), roscovitine (lane 4, 250 μM, 350× IC 50 for CDK2), and Bisindo (lane 3, 5 μM, 500× IC 50 for PKC). An equal amount of proteinase K alone was also loaded as an additional control (lane 6). In parallel, 6 ng (lane 7) or 12 ng (lane 8) of cytoplasmic HBV capsids from HepG2 cells (also treated with proteinase K; see Materials and Methods) were subjected to the endogenous kinase reaction. Half of each reaction product was resolved by agarose gel electrophoresis to visualize capsid particles (top), and proteinase K inhibitor was added to the other half to terminate the digestion before boiling in SDS sample buffer and resolving by SDS-PAGE to visualize the total core protein (bottom). The gels were dried, and labeled capsids or core proteins were detected by autoradiography. *, unknown labeled species. CA, capsids; C, core protein; PK, proteinase K; IC, intracellular.

    Journal: Journal of Virology

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids

    doi: 10.1128/JVI.01218-12

    Figure Lengend Snippet: Endogenous kinase reactions with virion-derived HBV capsids. HBV capsids were released from virions purified from the medium of HBV-transfected HepG2 cells by NP-40 treatment. One control aliquot was removed, and the remaining virion-derived capsids were digested by proteinase K. The untreated (lane 1) or proteinase K-treated (lanes 2 to 5), virion-derived capsids (ca. 6 ng per reaction) were phosphorylated by the encapsidated kinase in endogenous kinase reactions in the presence of the indicated kinase inhibitors (lanes 3 to 5) or DMSO control (lane 2). Kinase inhibitors used included CDK2 inhibitor III (lane 3, 250 μM, 500× IC 50 for CDK2), roscovitine (lane 4, 250 μM, 350× IC 50 for CDK2), and Bisindo (lane 3, 5 μM, 500× IC 50 for PKC). An equal amount of proteinase K alone was also loaded as an additional control (lane 6). In parallel, 6 ng (lane 7) or 12 ng (lane 8) of cytoplasmic HBV capsids from HepG2 cells (also treated with proteinase K; see Materials and Methods) were subjected to the endogenous kinase reaction. Half of each reaction product was resolved by agarose gel electrophoresis to visualize capsid particles (top), and proteinase K inhibitor was added to the other half to terminate the digestion before boiling in SDS sample buffer and resolving by SDS-PAGE to visualize the total core protein (bottom). The gels were dried, and labeled capsids or core proteins were detected by autoradiography. *, unknown labeled species. CA, capsids; C, core protein; PK, proteinase K; IC, intracellular.

    Article Snippet: HepG2 HBV capsids in sucrose fractions were digested for 1.5 h with proteinase K-agarose beads (Sigma) at 37°C with gentle agitation.

    Techniques: Derivative Assay, Purification, Transfection, Agarose Gel Electrophoresis, SDS Page, Labeling, Autoradiography

    Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with proteinase K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.

    Journal: Journal of Virology

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids

    doi: 10.1128/JVI.01218-12

    Figure Lengend Snippet: Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with proteinase K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.

    Article Snippet: When proteinase K-treated capsids were resolved by SDS-PAGE, the proteinase K digestion was stopped by adding proteinase K inhibitor (Calbiochem) to 1 mM (final concentration) and incubating the sample at room temperature for 10 min ( ).

    Techniques: Purification, Western Blot, SDS Page, Staining

    Endogenous kinase reactions with virion-derived HBV capsids. HBV capsids were released from virions purified from the medium of HBV-transfected HepG2 cells by NP-40 treatment. One control aliquot was removed, and the remaining virion-derived capsids were digested by proteinase K. The untreated (lane 1) or proteinase K-treated (lanes 2 to 5), virion-derived capsids (ca. 6 ng per reaction) were phosphorylated by the encapsidated kinase in endogenous kinase reactions in the presence of the indicated kinase inhibitors (lanes 3 to 5) or DMSO control (lane 2). Kinase inhibitors used included CDK2 inhibitor III (lane 3, 250 μM, 500× IC 50 for CDK2), roscovitine (lane 4, 250 μM, 350× IC 50 for CDK2), and Bisindo (lane 3, 5 μM, 500× IC 50 for PKC). An equal amount of proteinase K alone was also loaded as an additional control (lane 6). In parallel, 6 ng (lane 7) or 12 ng (lane 8) of cytoplasmic HBV capsids from HepG2 cells (also treated with proteinase K; see Materials and Methods) were subjected to the endogenous kinase reaction. Half of each reaction product was resolved by agarose gel electrophoresis to visualize capsid particles (top), and proteinase K inhibitor was added to the other half to terminate the digestion before boiling in SDS sample buffer and resolving by SDS-PAGE to visualize the total core protein (bottom). The gels were dried, and labeled capsids or core proteins were detected by autoradiography. *, unknown labeled species. CA, capsids; C, core protein; PK, proteinase K; IC, intracellular.

    Journal: Journal of Virology

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids

    doi: 10.1128/JVI.01218-12

    Figure Lengend Snippet: Endogenous kinase reactions with virion-derived HBV capsids. HBV capsids were released from virions purified from the medium of HBV-transfected HepG2 cells by NP-40 treatment. One control aliquot was removed, and the remaining virion-derived capsids were digested by proteinase K. The untreated (lane 1) or proteinase K-treated (lanes 2 to 5), virion-derived capsids (ca. 6 ng per reaction) were phosphorylated by the encapsidated kinase in endogenous kinase reactions in the presence of the indicated kinase inhibitors (lanes 3 to 5) or DMSO control (lane 2). Kinase inhibitors used included CDK2 inhibitor III (lane 3, 250 μM, 500× IC 50 for CDK2), roscovitine (lane 4, 250 μM, 350× IC 50 for CDK2), and Bisindo (lane 3, 5 μM, 500× IC 50 for PKC). An equal amount of proteinase K alone was also loaded as an additional control (lane 6). In parallel, 6 ng (lane 7) or 12 ng (lane 8) of cytoplasmic HBV capsids from HepG2 cells (also treated with proteinase K; see Materials and Methods) were subjected to the endogenous kinase reaction. Half of each reaction product was resolved by agarose gel electrophoresis to visualize capsid particles (top), and proteinase K inhibitor was added to the other half to terminate the digestion before boiling in SDS sample buffer and resolving by SDS-PAGE to visualize the total core protein (bottom). The gels were dried, and labeled capsids or core proteins were detected by autoradiography. *, unknown labeled species. CA, capsids; C, core protein; PK, proteinase K; IC, intracellular.

    Article Snippet: When proteinase K-treated capsids were resolved by SDS-PAGE, the proteinase K digestion was stopped by adding proteinase K inhibitor (Calbiochem) to 1 mM (final concentration) and incubating the sample at room temperature for 10 min ( ).

    Techniques: Derivative Assay, Purification, Transfection, Agarose Gel Electrophoresis, SDS Page, Labeling, Autoradiography

    Effects of glial signals on the presence of autaptic activity in single RGCs Columns indicate the fraction of single RGCs that showed spontaneous, evoked or asynchronous EACs when cultured under different conditions. RGCs were grown in the absence of glial cells ( n = 47; RGC), in direct contact with glial cells from optic nerve ( n = 26; +OPN), in the presence of GCM ( n = 36; +GCM), in the presence of GCM that had been digested before with bead-coupled proteinase K ( n = 15; +GCM+ProtK) and in the presence of GCM and TTX ( n = 18; +GCM+TTX). Whole-cell EACs were recorded with the perforated-patch technique at a holding potential of −70 mV and analysed in a blinded fashion. Asterisks denote significant changes compared to glia-free conditions ( P

    Journal: The Journal of Physiology

    Article Title: Glia-derived signals induce synapse formation in neurones of the rat central nervous system

    doi: 10.1111/j.1469-7793.2001.00665.x

    Figure Lengend Snippet: Effects of glial signals on the presence of autaptic activity in single RGCs Columns indicate the fraction of single RGCs that showed spontaneous, evoked or asynchronous EACs when cultured under different conditions. RGCs were grown in the absence of glial cells ( n = 47; RGC), in direct contact with glial cells from optic nerve ( n = 26; +OPN), in the presence of GCM ( n = 36; +GCM), in the presence of GCM that had been digested before with bead-coupled proteinase K ( n = 15; +GCM+ProtK) and in the presence of GCM and TTX ( n = 18; +GCM+TTX). Whole-cell EACs were recorded with the perforated-patch technique at a holding potential of −70 mV and analysed in a blinded fashion. Asterisks denote significant changes compared to glia-free conditions ( P

    Article Snippet: Briefly, GCM (2.2 ml) was incubated with proteinase K-acrylic beads (0.5 ml suspension, washed 10 times with PBS; Sigma) for 30 min at 37°C on a horizontal shaker.

    Techniques: Activity Assay, Cell Culture

    FacX is resistant to boiling, but sensitive to Proteinase K. (A) Conditioned media was boiled for 15 min and utilized in the sporulation assay ( Fig 2A ) with strain MF1913 (P hy-spank - kinA ). (B) Conditioned media was treated with proteinase K and utilized in the sporulation assay with strain MF1913 (P hy-spank - kinA ). When indicated, KinA was induced with IPTG (20 μM). Cells were grown for 2 hrs at 37°C before image capture. Membranes were stained with TMA.

    Journal: PLoS ONE

    Article Title: A Secreted Factor Coordinates Environmental Quality with Bacillus Development

    doi: 10.1371/journal.pone.0144168

    Figure Lengend Snippet: FacX is resistant to boiling, but sensitive to Proteinase K. (A) Conditioned media was boiled for 15 min and utilized in the sporulation assay ( Fig 2A ) with strain MF1913 (P hy-spank - kinA ). (B) Conditioned media was treated with proteinase K and utilized in the sporulation assay with strain MF1913 (P hy-spank - kinA ). When indicated, KinA was induced with IPTG (20 μM). Cells were grown for 2 hrs at 37°C before image capture. Membranes were stained with TMA.

    Article Snippet: To treat the conditioned CH media with protease, 30 mg of proteinase K conjugated to agarose beads (Sigma) was hydrated in 3 ml ddH2 0 for 20 min at room temperature, and then centrifuged at 1,292 x g for 2 min. After removing the supernatant, the beads were washed in 3 ml ddH2 0, and pelleted by centrifuging at 1,292 x g for 2 min.

    Techniques: Staining

    Flotation of BKV in the presence of human erythrocyte (RBC) membranes. (A) BKV was incubated with BSA, RBC membranes, or RBC membranes treated with proteinase K (PK), centrifuged on a sucrose gradient, fractionated, blotted, and probed for the presence of VP1. (B) Protein gel showing complete digestion by PK. Indicated amounts of RBC samples were separated by SDS-polyacrylamide gel electrophoresis and stained with Colloidal Blue. (C) BKV was incubated with neuraminidase-treated or untreated RBC membranes and analyzed as in panel A.

    Journal: Journal of Virology

    Article Title: Identification of Gangliosides GD1b and GT1b as Receptors for BK Virus

    doi: 10.1128/JVI.80.3.1361-1366.2006

    Figure Lengend Snippet: Flotation of BKV in the presence of human erythrocyte (RBC) membranes. (A) BKV was incubated with BSA, RBC membranes, or RBC membranes treated with proteinase K (PK), centrifuged on a sucrose gradient, fractionated, blotted, and probed for the presence of VP1. (B) Protein gel showing complete digestion by PK. Indicated amounts of RBC samples were separated by SDS-polyacrylamide gel electrophoresis and stained with Colloidal Blue. (C) BKV was incubated with neuraminidase-treated or untreated RBC membranes and analyzed as in panel A.

    Article Snippet: To remove proteins, 100 μl of human erythrocyte membranes was incubated with 20 μl of proteinase K-conjugated agarose beads (Sigma) for 30 min at 25°C.

    Techniques: Incubation, Polyacrylamide Gel Electrophoresis, Staining

    Proteinase-K treated HPSE results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =

    Journal: PLoS ONE

    Article Title: Soluble Heparan Sulfate Fragments Generated by Heparanase Trigger the Release of Pro-Inflammatory Cytokines through TLR-4

    doi: 10.1371/journal.pone.0109596

    Figure Lengend Snippet: Proteinase-K treated HPSE results in a reduced cytokine response in PBMCs. HPSE (1 µg) was treated with proteinase-K agarose beads (80 µg/ml) for 30 min at 37°C before removal of proteinase-K agarose beads and SDS-PAGE analysis. ( A ) Western blot analysis for HPSE confirms that proteinase-K treatment dramatically reduced intact HPSE levels in the sample. ( B ) HPSE activity assay on identically treated samples of either HPSE alone, proteinase K alone, or HPSE treated with proteinase K. Data represent the mean ±SEM (n = 3). ( C ) Expression of cytokines after stimulation with proteinase-K treated HPSE in IL-1β, IL-6, IL-10, IL-8 and TNF in PBMCs isolated from human whole blood. Data represent the mean ±SEM of triplicate samples, results are representative of three independent experiments. *p =

    Article Snippet: Proteinase-K treatment of HPSE Proteinase-K-agarose beads (Sigma Aldrich) were suspended in endotoxin free PBS (Ca2+ - and Mg2+ -free, Life Technologies, CA) to a concentration of 80 mg/ml.

    Techniques: SDS Page, Western Blot, Activity Assay, Expressing, Isolation

    Measurement of the degree of sialylation by SNA lectin inhibition ELISA. % SNA lectin binding after pre-incubation A ) with IVIg, IVIg-SA (+) or IVIg-SA (−) B ) with Fab and Fc fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−) C ) with Fab or protK digested Fab fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−) D ) with Fc or protK digested Fc fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−). Data represents mean ± SEM, n = 3.

    Journal: PLoS ONE

    Article Title: Enrichment of Sialylated IgG by Lectin Fractionation Does Not Enhance the Efficacy of Immunoglobulin G in a Murine Model of Immune Thrombocytopenia

    doi: 10.1371/journal.pone.0021246

    Figure Lengend Snippet: Measurement of the degree of sialylation by SNA lectin inhibition ELISA. % SNA lectin binding after pre-incubation A ) with IVIg, IVIg-SA (+) or IVIg-SA (−) B ) with Fab and Fc fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−) C ) with Fab or protK digested Fab fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−) D ) with Fc or protK digested Fc fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−). Data represents mean ± SEM, n = 3.

    Article Snippet: Proteinase K digestion of Fc fragments To determine the degree of Fc sialylation, Fc fragments derived from IVIg, IVIg-SA (+) or IVIg-SA (−) were digested with protK (proteinase K, Sigma-Aldrich, St. Louis, MO, USA).

    Techniques: Inhibition, Enzyme-linked Immunosorbent Assay, Binding Assay, Incubation, Derivative Assay

    Spermiograms and in vitro fertilization assays. Spermiograms from PCI +/+ ( a ) and from PCI +/– ( b ) were normal, whereas in spermiograms from PCI –/– mice ( c ) immature and malformed cells were prevalent. ( d ) In in vitro fertilization assays, sperm obtained from PCI +/– mice were able to bind and subsequently fertilize PCI +/+ oocytes. Sperm obtained from PCI –/– males failed to fertilize zona pellucida–containing ( e ) or zona pellucida–free ( f ) oocytes.

    Journal: The Journal of Clinical Investigation

    Article Title: Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility

    doi:

    Figure Lengend Snippet: Spermiograms and in vitro fertilization assays. Spermiograms from PCI +/+ ( a ) and from PCI +/– ( b ) were normal, whereas in spermiograms from PCI –/– mice ( c ) immature and malformed cells were prevalent. ( d ) In in vitro fertilization assays, sperm obtained from PCI +/– mice were able to bind and subsequently fertilize PCI +/+ oocytes. Sperm obtained from PCI –/– males failed to fertilize zona pellucida–containing ( e ) or zona pellucida–free ( f ) oocytes.

    Article Snippet: These oocytes were either surrounded by cumulus cells, cumulus cell–free (removed by treatment with 0.1% hyaluronidase), or zona pellucida–free (removed by treatment with 0.1% proteinase K; Sigma-Aldrich).

    Techniques: In Vitro, Mouse Assay