aprotinin Search Results


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  • 99
    Millipore aprotinin
    Insulin (10nM) induced EGFR phosphorylation was not inhibited by the plasmin inhibitors (ε-aminocaproic acid -EACA- and <t>aprotinin).</t> Pre-incubation with the matrix metalloprotease inhibitor GM6001 and the ADAM inhibitors TAPI-0 and TAPI-1 blocked Insulin induced EGFR phosphorylation. Values are the mean±SEM of the ratio of the phosphorylation of the respective protein relative to the total unphosphosylated protein (n=6, *p
    Aprotinin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 9126 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aprotinin/product/Millipore
    Average 99 stars, based on 9126 article reviews
    Price from $9.99 to $1999.99
    aprotinin - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    93
    Tocris aprotinin
    Insulin (10nM) induced EGFR phosphorylation was not inhibited by the plasmin inhibitors (ε-aminocaproic acid -EACA- and <t>aprotinin).</t> Pre-incubation with the matrix metalloprotease inhibitor GM6001 and the ADAM inhibitors TAPI-0 and TAPI-1 blocked Insulin induced EGFR phosphorylation. Values are the mean±SEM of the ratio of the phosphorylation of the respective protein relative to the total unphosphosylated protein (n=6, *p
    Aprotinin, supplied by Tocris, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aprotinin/product/Tocris
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    aprotinin - by Bioz Stars, 2020-08
    93/100 stars
      Buy from Supplier

    91
    Selleck Chemicals aprotinin
    Insulin (10nM) induced EGFR phosphorylation was not inhibited by the plasmin inhibitors (ε-aminocaproic acid -EACA- and <t>aprotinin).</t> Pre-incubation with the matrix metalloprotease inhibitor GM6001 and the ADAM inhibitors TAPI-0 and TAPI-1 blocked Insulin induced EGFR phosphorylation. Values are the mean±SEM of the ratio of the phosphorylation of the respective protein relative to the total unphosphosylated protein (n=6, *p
    Aprotinin, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aprotinin/product/Selleck Chemicals
    Average 91 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    aprotinin - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    97
    Millipore bovine aprotinin
    Molecular size estimation under nondenaturing and denaturing conditions. ( A ) Representative elution profiles from analytical gel permeation chromatography of either the wild-type (dotted line, peak elution volumes are indicated in italics) or the Ile-314 → Gly mutant (solid line, peak elution volumes are indicated in bold) αX I domains. The samples were spiked with blue dextran (BD) eluting at the excluded volume of the column (8.34 ml) and bovine <t>aprotinin</t> (BAp), which eluted at 16.38 ml (the peak elution volumes of both internal markers are indicated with long arrows). The bed volume of the column was 18 ml. The column was calibrated with bovine serum albumin (BSA; 67.0 kDa, R S = 35.5 Å), ovalbumin (Ova; 43.0 kDa, R S = 30.5 Å), chymotrypsinogen A (Chy; 25.0 kDa, R S = 20.9 Å), and ribonuclease A (Rib; 13.7 kDa, R S = 16.4 Å). The peak elution volumes of the size markers are indicated with short arrows. ( B ) Nonreducing SDS/PAGE of the wild-type (wt) and Ile-314 → Gly mutant αX I domain.
    Bovine Aprotinin, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine aprotinin/product/Millipore
    Average 97 stars, based on 68 article reviews
    Price from $9.99 to $1999.99
    bovine aprotinin - by Bioz Stars, 2020-08
    97/100 stars
      Buy from Supplier

    Image Search Results


    Insulin (10nM) induced EGFR phosphorylation was not inhibited by the plasmin inhibitors (ε-aminocaproic acid -EACA- and aprotinin). Pre-incubation with the matrix metalloprotease inhibitor GM6001 and the ADAM inhibitors TAPI-0 and TAPI-1 blocked Insulin induced EGFR phosphorylation. Values are the mean±SEM of the ratio of the phosphorylation of the respective protein relative to the total unphosphosylated protein (n=6, *p

    Journal: Surgery

    Article Title: INSULIN INDUCED EPIDERMAL GROWTH FACTOR ACTIVATION IN VASCULAR SMOOTH MUSCLE CELLS IS ADAM-DEPENDENT

    doi: 10.1016/j.surg.2008.03.023

    Figure Lengend Snippet: Insulin (10nM) induced EGFR phosphorylation was not inhibited by the plasmin inhibitors (ε-aminocaproic acid -EACA- and aprotinin). Pre-incubation with the matrix metalloprotease inhibitor GM6001 and the ADAM inhibitors TAPI-0 and TAPI-1 blocked Insulin induced EGFR phosphorylation. Values are the mean±SEM of the ratio of the phosphorylation of the respective protein relative to the total unphosphosylated protein (n=6, *p

    Article Snippet: Insulin, EGF, EACA, and aprotinin were purchased from Sigma Chemical Co (St. Louis, MO).

    Techniques: Incubation

    Molecular size estimation under nondenaturing and denaturing conditions. ( A ) Representative elution profiles from analytical gel permeation chromatography of either the wild-type (dotted line, peak elution volumes are indicated in italics) or the Ile-314 → Gly mutant (solid line, peak elution volumes are indicated in bold) αX I domains. The samples were spiked with blue dextran (BD) eluting at the excluded volume of the column (8.34 ml) and bovine aprotinin (BAp), which eluted at 16.38 ml (the peak elution volumes of both internal markers are indicated with long arrows). The bed volume of the column was 18 ml. The column was calibrated with bovine serum albumin (BSA; 67.0 kDa, R S = 35.5 Å), ovalbumin (Ova; 43.0 kDa, R S = 30.5 Å), chymotrypsinogen A (Chy; 25.0 kDa, R S = 20.9 Å), and ribonuclease A (Rib; 13.7 kDa, R S = 16.4 Å). The peak elution volumes of the size markers are indicated with short arrows. ( B ) Nonreducing SDS/PAGE of the wild-type (wt) and Ile-314 → Gly mutant αX I domain.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Structure and allosteric regulation of the ?X?2 integrin I domain

    doi: 10.1073/pnas.0237387100

    Figure Lengend Snippet: Molecular size estimation under nondenaturing and denaturing conditions. ( A ) Representative elution profiles from analytical gel permeation chromatography of either the wild-type (dotted line, peak elution volumes are indicated in italics) or the Ile-314 → Gly mutant (solid line, peak elution volumes are indicated in bold) αX I domains. The samples were spiked with blue dextran (BD) eluting at the excluded volume of the column (8.34 ml) and bovine aprotinin (BAp), which eluted at 16.38 ml (the peak elution volumes of both internal markers are indicated with long arrows). The bed volume of the column was 18 ml. The column was calibrated with bovine serum albumin (BSA; 67.0 kDa, R S = 35.5 Å), ovalbumin (Ova; 43.0 kDa, R S = 30.5 Å), chymotrypsinogen A (Chy; 25.0 kDa, R S = 20.9 Å), and ribonuclease A (Rib; 13.7 kDa, R S = 16.4 Å). The peak elution volumes of the size markers are indicated with short arrows. ( B ) Nonreducing SDS/PAGE of the wild-type (wt) and Ile-314 → Gly mutant αX I domain.

    Article Snippet: Before gel permeation chromatography, the samples of recombinant I domains were mixed with blue dextran 2000 and bovine aprotinin (catalog no. A-6279, Sigma) and adjusted to a total sample volume of 100 μl with HBS/Tw.

    Techniques: GPC Assay, Mutagenesis, SDS Page