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#12506074   // To Up

Molecular analysis of Pseudomonas aeruginosa protease IV expressed in Pseudomonas putida.

In this study, the protease IV gene of Pseudomonas aeruginosa was expressed in the nonocular pathogenic host, Pseudomonas putida, to elucidate the molecular properties and virulence contribution of the enzyme. Recent determination of the protease IV gene sequence suggests that the protein of 463 amino acids contains a signal sequence, a propeptide domain, and a mature protease. The only form of this protein that has been detected previously is the extracellular mature protease.
Mullika Traidej, Armando R Caballero, Mary E Marquart, Brett A Thibodeaux, Richard J O'Callaghan

1823 related Products with: Molecular analysis of Pseudomonas aeruginosa protease IV expressed in Pseudomonas putida.

0.1ml0.1ml0.1ml1100μg10 mg1 set (5 x 1 ml)5mg50 ug1 set20 ug

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Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts.

Membrane type (MT) 1 matrix metalloproteinase (MMP) activates progelatinase A (pro-MMP-2), a type IV collagenase, on the cell surface of tumors; however, its function in breast cancer progression and metastasis is not fully understood. To examine the expression of MT1-MMP in breast cancer cells and fibroblasts, a specific rabbit antibody (Ab) directed against a unique synthetic peptide derived from the human MT1-MMP catalytic domain was produced, purified, and characterized. This Ab is not likely to cross-react with MT2-, MT3-, or MT4-MMP or any other MMPs. MT1-MMP expression and pro-MMP-2 activation were stimulated by concanavalin A in two human breast carcinoma cell lines (BT549 and MDA-MB-231) and in normal human fetal-lung fibroblasts (HFL-1) and were slightly upregulated by breast cancer cell-fibroblast interactions. Both pro-MT1-MMP in plasma membrane (63.4 kDa) and the soluble forms of the enzyme in culture medium (57.6 and 25-30 kDa) were detected by immunoblot analysis, suggesting that cell-surface MT1-MMP exhibits an active conformation without the removal of its propeptide domain and that the mature enzyme is shed into the medium. In breast cancer cells, MT1-MMP and a recombinant catalytic domain of MT1-MMP were unable to activate pro-matrilysin, indicating that MT1-MMP is not a universal activator of all MMPs. MT1-MMP may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier. Furthermore, use of the specific Ab may aid in the investigation of the role of MT1-MMP in human tumors.
H Li, D E Bauzon, X Xu, H Tschesche, J Cao, Q A Sang

1948 related Products with: Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts.

100ug Lyophilized 100ul100ug Lyophilized

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Immunisation of Chickens with the Aminoterminal Propeptide of Bovine Procollagen Type III (Specificity of egg yolk antibodies and comparison with immunoassays using rabbit and mouse antibodies.

Two chickens were immunised with the aminoterminal propeptide of bovine procollagen type III (PIIINP) purified from bovine fetal skin. Both animals developed antibodies binding to either unmodified or iodinated bovine PIIINP, but only one chicken developed antibodies which recognise PIIINP variants in serum. These antibodies were used to establish RIAs to analyze the specificity of these particular antibodies and to compare their specificity with that of published assays, as well as laboratory assay variants utilizing different rabbit and mouse antibodies. In comparison to most anti-PIIINP polyclonal antisera from rabbits the chicken antibodies do not bind to the Col-1 domain of PIIINP, a characteristic which they share with a monoclonal antibody (MAB 238) produced from a mouse immunized with the same antigen. Like the monoclonal antibody, the chicken antibodies exhibit reactivity against intact serum PIIINP and its high molecular weight variants, most probably pN procollagen type III and procollagen type III. While the monoclonal antibody can only be applied to analyze PIIINP in human sera, the avian antibodies show reactivity to the antigen in both, human and rat sera. The chicken anti PIIINP antibodies described in this study may become a powerful tool to quantitative PIIINP in serum of patients with liver fibrosis and in serum from experimental rat models of fibrogenesis. The fact that both can be analyzed with the same assay, gives, for the first time, the opportunity for a direct comparison of the results from human and rat studies designed to evaluate the action of antifibrotic agents.
Martin Gerl, Cornelia Steinert, Manfred Quint, Rüdiger Schade, Volkmar Günzler

2385 related Products with: Immunisation of Chickens with the Aminoterminal Propeptide of Bovine Procollagen Type III (Specificity of egg yolk antibodies and comparison with immunoassays using rabbit and mouse antibodies.

1000 TESTS/0.65ml1 ml0.2 mg200 0.1 mg100.00 ug100 μg0.25 mg0.1 ml100 ug1mg100 μg

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