a protinin  (Millipore)


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    Name:
    Aprotinin
    Description:
    Trypsin inhibitor pancreas type from bovine lung It is known as Pancreatic trypsin inhibitor BPTI Aprotinin also known as pancreatic trypsin inhibitor and trypsin kallikrein inhibitor is found to be expressed in lungs spleen liver and pancreas It is also found to be present in the free form in calf serum
    Catalog Number:
    roapro
    Price:
    None
    Applications:
    Aprotinin is used for the protection of proteins and enzymes during isolation/purification. The inhibition of protease activity increases the lifetime of cells in cell and tissue culture studies.. Further applications: Purification of urokinase, trypsin, and chymotrypsin on immobilized aprotinin. Quantification of kallikrein activity in mixtures of esterases and proteases. Controlled degradation of substrates by avoiding nonspecific proteolysis in clinical chemical tests. Aprotinin as a model protein in protein-folding studies. Molecular weight marker in SDS-polyacrylamide gel electrophoresis
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    Structured Review

    Millipore a protinin
    Trypsin inhibitor pancreas type from bovine lung It is known as Pancreatic trypsin inhibitor BPTI Aprotinin also known as pancreatic trypsin inhibitor and trypsin kallikrein inhibitor is found to be expressed in lungs spleen liver and pancreas It is also found to be present in the free form in calf serum
    https://www.bioz.com/result/a protinin/product/Millipore
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    a protinin - by Bioz Stars, 2020-09
    99/100 stars

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    Related Articles

    Protease Inhibitor:

    Article Title: Proangiogenic microtemplated fibrin scaffolds containing aprotinin promote improved wound healing responses
    Article Snippet: .. Inhibition of scaffold degradation by proteases was tested by adding the serine protease inhibitor aprotinin (3000U/mL, Sigma-Aldrich, St. Louis, MO) to the fibrinogen solution. .. These scaffold modifications were tested alone and in combination with each other to determine their effects on in vivo degradation and tissue responses to the fibrin scaffolds.

    Article Title: Virulence Associated Gene 8 of Bordetella pertussis Enhances Contact System Activity by Inhibiting the Regulatory Function of Complement Regulator C1 Inhibitor
    Article Snippet: .. For assessment of HK cleavage upon incubation of plasma with B. pertussis , several bacterial strains (2 × 109 CFU) were incubated with 50% plasma either alone or in the presence of the contact protease inhibitors aprotinin ( ) (100 units/mL, Sigma), which inhibits PK and d -phenylalanyl-prolyl-arginyl chloromethyl ketone ( ) (PPACK; 200 µM, Hematologic Technologies, Essex Junction, VT, USA), a multi-target serine protease inhibitor which restricts auto activation and self-digestion of FXIIa, and sampled after 30 min at 37°C shaking at 300 rpm. .. Plasma samples incubated with βFXIIa (16.7 nM corresponding to 0.5 µg/mL) or only buffer A were taken along as positive and negative controls, respectively.

    Construct:

    Article Title: New Insights into the Lpt Machinery for Lipopolysaccharide Transport to the Cell Surface: LptA-LptC Interaction and LptA Stability as Sensors of a Properly Assembled Transenvelope Complex ▿
    Article Snippet: .. The calibration curve was constructed by using the following standards (0.5 mg/ml): transferrin (81,000 Da), chicken ovalbumin (43,000 Da), chymotrypsin (21,500 Da), bovine cytochrome c (12,200 Da), and aprotinin (6,500 Da) (Sigma Aldrich, St. Louis, MO). .. LptC was injected at a concentration of 1 mg/ml.

    Article Title: Compaction Properties of an Intrinsically Disordered Protein: Sic1 and Its Kinase-Inhibitor Domain
    Article Snippet: .. A calibration curve was constructed using the following standards (0.75 mg/mL): bovine aprotinin (6,500 Da), horse cytochrome c (12,400 Da), horse myoglobin (17,600 Da), chicken ovalbumin (45,000 Da), equine apoferritin (80,000 Da) (Sigma Aldrich, St. Louis, MO), and recombinant green fluorescent protein (29,800 Da). .. A second calibration curve was constructed to calculate the Rh values of Sic1FL and Sic1Δ214 , by plotting the Rh values of the standards (ovalbumin, myoglobin, cytochrome c , and aprotinin) against their relatve elution volume ( ).

    Activation Assay:

    Article Title: Virulence Associated Gene 8 of Bordetella pertussis Enhances Contact System Activity by Inhibiting the Regulatory Function of Complement Regulator C1 Inhibitor
    Article Snippet: .. For assessment of HK cleavage upon incubation of plasma with B. pertussis , several bacterial strains (2 × 109 CFU) were incubated with 50% plasma either alone or in the presence of the contact protease inhibitors aprotinin ( ) (100 units/mL, Sigma), which inhibits PK and d -phenylalanyl-prolyl-arginyl chloromethyl ketone ( ) (PPACK; 200 µM, Hematologic Technologies, Essex Junction, VT, USA), a multi-target serine protease inhibitor which restricts auto activation and self-digestion of FXIIa, and sampled after 30 min at 37°C shaking at 300 rpm. .. Plasma samples incubated with βFXIIa (16.7 nM corresponding to 0.5 µg/mL) or only buffer A were taken along as positive and negative controls, respectively.

    Incubation:

    Article Title: Virulence Associated Gene 8 of Bordetella pertussis Enhances Contact System Activity by Inhibiting the Regulatory Function of Complement Regulator C1 Inhibitor
    Article Snippet: .. For assessment of HK cleavage upon incubation of plasma with B. pertussis , several bacterial strains (2 × 109 CFU) were incubated with 50% plasma either alone or in the presence of the contact protease inhibitors aprotinin ( ) (100 units/mL, Sigma), which inhibits PK and d -phenylalanyl-prolyl-arginyl chloromethyl ketone ( ) (PPACK; 200 µM, Hematologic Technologies, Essex Junction, VT, USA), a multi-target serine protease inhibitor which restricts auto activation and self-digestion of FXIIa, and sampled after 30 min at 37°C shaking at 300 rpm. .. Plasma samples incubated with βFXIIa (16.7 nM corresponding to 0.5 µg/mL) or only buffer A were taken along as positive and negative controls, respectively.

    Inhibition:

    Article Title: Proangiogenic microtemplated fibrin scaffolds containing aprotinin promote improved wound healing responses
    Article Snippet: .. Inhibition of scaffold degradation by proteases was tested by adding the serine protease inhibitor aprotinin (3000U/mL, Sigma-Aldrich, St. Louis, MO) to the fibrinogen solution. .. These scaffold modifications were tested alone and in combination with each other to determine their effects on in vivo degradation and tissue responses to the fibrin scaffolds.

    Injection:

    Article Title: A Novel Signaling Pathway of Tissue Kallikrein in Promoting Keratinocyte Migration: Activation of Proteinase-Activated Receptor 1 and Epidermal Growth Factor Receptor
    Article Snippet: .. Active TK (3 μg) with or without AG1478 (2 μg) (Calbiochem) and icatibant (12 μg) (Sigma), as well as aprotinin (3 μg) (Sigma), neutralizing antibody to rat TK, control IgG (50 μg), or saline in 100 μl final volume was injected intradermally at 6 different sites around the wound edge once a day for 8 days. .. Effects of TK on the migration of cultured HaCaT keratinocytes were determined by both scratch wound method and modified Boyden chambers.

    Recombinant:

    Article Title: Compaction Properties of an Intrinsically Disordered Protein: Sic1 and Its Kinase-Inhibitor Domain
    Article Snippet: .. A calibration curve was constructed using the following standards (0.75 mg/mL): bovine aprotinin (6,500 Da), horse cytochrome c (12,400 Da), horse myoglobin (17,600 Da), chicken ovalbumin (45,000 Da), equine apoferritin (80,000 Da) (Sigma Aldrich, St. Louis, MO), and recombinant green fluorescent protein (29,800 Da). .. A second calibration curve was constructed to calculate the Rh values of Sic1FL and Sic1Δ214 , by plotting the Rh values of the standards (ovalbumin, myoglobin, cytochrome c , and aprotinin) against their relatve elution volume ( ).