aprotinin a  (Millipore)


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  • 99
    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 aprotinin a
    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/aprotinin a/product/Millipore
    Average 99 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    aprotinin a - by Bioz Stars, 2020-07
    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.

    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 ( ).

    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.

    Article Title: Common and specific effects of TIE2 mutations causing venous malformations
    Article Snippet: .. In serine protease inhibition assays both the gel and media were supplemented with 25 µg/ml aprotinin (Sigma-Aldrich). .. After 16 h cells were fixed with 4% paraformaldehyde and imaged for quantification using a phase-contrast microscope.

    Activity Assay:

    Article Title: German Cockroach Proteases and Protease-Activated Receptor-2 Regulate Chemokine Production and Dendritic Cell Recruitment
    Article Snippet: .. To inhibit protease activity, frass was pretreated with aprotinin (Sigma-Aldrich; 10 μg/ml for 30 min at 37°C) prior to use. .. The same concentration of aprotinin was added to PBS and used as a control.

    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 ( ).

    other:

    Article Title: Temporal and Pharmacological Characterization of Angiostatin Release and Generation by Human Platelets: Implications for Endothelial Cell Migration
    Article Snippet: Prostacyclin-sodium salt, S-nitroso-glutathione, acetylsalicyclic acid, MRS2395, RGDS peptide, and aprotinin were obtained from Sigma (Mississauga, ONT, Canada).

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  • 99
    Millipore aprotinin
    a , The presence of the three forms of neurocan is not an artifact of storage, concentration, or chondroitinase treatment. The same three bands are seen whether conditioned medium is analyzed before or after storing, concentrating, or chondroitinase treatment. b , Protease inhibitors do not affect neurocan processing. Astrocytes were grown in the presence of <t>aprotinin</t> (1.0 μg/ml), anti-thrombin III (0.1 inhibitor U/ml), or TIMP-2 (0.2 μg/ml) for 4 d. Each inhibitor was added fresh each day. Conditioned medium was concentrated and treated with chondroitinase ABC, and an equal amount of total protein (150 μg) was applied to each lane. The blot was labeled with the 1G2 mAb ( left ) and then relabeled with the 1F6 mAb ( right ). Neither serine protease (aprotinin and anti-thrombin III) nor metalloproteinase (TIMP-2) inhibitors prevented the processing of neurocan.
    Aprotinin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3422 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aprotinin/product/Millipore
    Average 99 stars, based on 3422 article reviews
    Price from $9.99 to $1999.99
    aprotinin - by Bioz Stars, 2020-07
    99/100 stars
      Buy from Supplier

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    a , The presence of the three forms of neurocan is not an artifact of storage, concentration, or chondroitinase treatment. The same three bands are seen whether conditioned medium is analyzed before or after storing, concentrating, or chondroitinase treatment. b , Protease inhibitors do not affect neurocan processing. Astrocytes were grown in the presence of aprotinin (1.0 μg/ml), anti-thrombin III (0.1 inhibitor U/ml), or TIMP-2 (0.2 μg/ml) for 4 d. Each inhibitor was added fresh each day. Conditioned medium was concentrated and treated with chondroitinase ABC, and an equal amount of total protein (150 μg) was applied to each lane. The blot was labeled with the 1G2 mAb ( left ) and then relabeled with the 1F6 mAb ( right ). Neither serine protease (aprotinin and anti-thrombin III) nor metalloproteinase (TIMP-2) inhibitors prevented the processing of neurocan.

    Journal: The Journal of Neuroscience

    Article Title: Neurocan Is Upregulated in Injured Brain and in Cytokine-Treated Astrocytes

    doi: 10.1523/JNEUROSCI.20-07-02427.2000

    Figure Lengend Snippet: a , The presence of the three forms of neurocan is not an artifact of storage, concentration, or chondroitinase treatment. The same three bands are seen whether conditioned medium is analyzed before or after storing, concentrating, or chondroitinase treatment. b , Protease inhibitors do not affect neurocan processing. Astrocytes were grown in the presence of aprotinin (1.0 μg/ml), anti-thrombin III (0.1 inhibitor U/ml), or TIMP-2 (0.2 μg/ml) for 4 d. Each inhibitor was added fresh each day. Conditioned medium was concentrated and treated with chondroitinase ABC, and an equal amount of total protein (150 μg) was applied to each lane. The blot was labeled with the 1G2 mAb ( left ) and then relabeled with the 1F6 mAb ( right ). Neither serine protease (aprotinin and anti-thrombin III) nor metalloproteinase (TIMP-2) inhibitors prevented the processing of neurocan.

    Article Snippet: To investigate neurocan processing, astrocytes were maintained for 4 d in serum-free DMEM containing one of the following protease inhibitors: anti-thrombin III (0.1 U/ml), aprotinin (1.0 μg/ml), tissue inhibitor of metalloproteinase-2 (TIMP-2, 0.2 μg/ml), leupeptin (1.0 μg/ml), E-64 (1.0 μg/ml; Calbiochem, Nottingham, Notts, UK), cathepsin B inhibitor II (1.0 μg/ml; Calbiochem), or α2 -macroglobulin (10 μg/ml).

    Techniques: Concentration Assay, Labeling

    Endogenous tissue-type plasminogen activator (tPA) induces hypoxic tolerance. Mean cell survival determined by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay in wild-type (Wt; A ) and tPA-deficient (tPA −/− ; B ) neurons exposed to 5 minutes of oxygen–glucose deprivation (OGD) conditions (hypoxic preconditioning, HP), followed 5 minutes later by 55 minutes of OGD. A subgroup of neurons was incubated during the preconditioning phase with either α 2 -antiplasmin 100 nmol/L (AP) or aprotinin 1.4 μ mol/L (Apro), or tPA 5 nmol/L or plasmin 10 nmol/L. HP denotes the moment when cells were exposed to sublethal hypoxia; n =12 for each observation. Data represent mean cell survival±s.d. ( A ) * P

    Journal: Journal of Cerebral Blood Flow & Metabolism

    Article Title: Tissue-type plasminogen activator has a neuroprotective effect in the ischemic brain mediated by neuronal TNF-α

    doi: 10.1038/jcbfm.2011.106

    Figure Lengend Snippet: Endogenous tissue-type plasminogen activator (tPA) induces hypoxic tolerance. Mean cell survival determined by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay in wild-type (Wt; A ) and tPA-deficient (tPA −/− ; B ) neurons exposed to 5 minutes of oxygen–glucose deprivation (OGD) conditions (hypoxic preconditioning, HP), followed 5 minutes later by 55 minutes of OGD. A subgroup of neurons was incubated during the preconditioning phase with either α 2 -antiplasmin 100 nmol/L (AP) or aprotinin 1.4 μ mol/L (Apro), or tPA 5 nmol/L or plasmin 10 nmol/L. HP denotes the moment when cells were exposed to sublethal hypoxia; n =12 for each observation. Data represent mean cell survival±s.d. ( A ) * P

    Article Snippet: Other reagents were human recombinant tPA (Genentech, San Francisco, CA, USA), aprotinin (1.4 μ mol/L; Calbiochem, Gibbstown, NJ, USA), kainic acid (KA; 250 μ mol/L) and the NMDAR antagonist MK-801 (10 μmol/L; Tocris Bioscience, Ellisville, MO, USA), murine anti-TNF- α neutralizing antibodies (40 ng/mL) and recombinant TNF- α (1.2 nmol/L; R & D Systems; Minneapolis, MN, USA), 4′,6-diamidino-2-phenylindole and triphenyltetrazolium chloride (Sigma-Aldrich, St Louis, MO, USA), and p21 short hairpin RNA (shRNA) and shRNA lentiviral particles (Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: MTT Assay, Incubation