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           Search results for: Antibodies, Mouse: Monoclonal antibody to human prorenin, clone 6E2-B7   

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High frequency of natural autoantibodies in normal newborn mice.

Spleen cells from 6-day-old nonimmunized BALB/c and BALB.B10 mice were fused with the nonsecreting hybridoma cell line Sp2/0. Three hundred and eighty-four immunoglobulin-secreting hybrids were screened for antibody activity against mouse actin, tubulin, and myosin, and against TNP, peroxidase, renin, DNA, and neurofilaments. At least 24 hybridomas in the collection (6.25%) exhibited antibody activity against this panel of antigens. Ten of these hybrids were cloned, were propagated, and the corresponding monoclonal IgM protein was isolated from ascitic fluids and was further characterized. At least four groups of antibody specificities were identified: 1) one clone reacting with TNP only; 2) one clone reacting with both actin and tubulin; 3) two clones which bound to both TNP and actin; and 4) a fourth group, comprising the six other clones, which all exhibited widespread reactivity and bound to actin, tubulin, myosin, and TNP. These results indicate: 1) B cell clones directed against self antigens are activated in the internal environment and are recovered consequently by somatic cell hybridization; 2) the widespread antibody specificities found for these newborn mouse antibodies are very similar to those previously characterized with human natural antibodies and human monoclonal Ig; and 3) the frequency of B cells binding to cytoskeletal proteins and TNP is very high (at least 6.25%).

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A monoclonal antibody for immunopurification of human renin.


2810 related Products with: A monoclonal antibody for immunopurification of human renin.

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Monoclonal antibodies binding renal renin.

Somatic-cell fusion of normal antibody-producing spleen cells with cells from a plasmacytoma culture results in a culture of hybrid cells from which a monoclonal line may be selected. These lines are immortal and may be amplified as tumors in syngeneic animals to produce large quantities of antibodies characterized by molecular homogeneity. We report the application of this technique to the production of antibodies binding canine renin. Balb/c mice were immunized with pure canine renal renin and their spleen cells fused with the NS-1 myeloma line. In two separate fusions, nine clones of cells were isolated that bound canine renal renin but did not cross-react with a number of protein antigens tested. One of these antibodies cross-reacted with renins of several different species, including human renin. Binding inhibition studies carried out with one of these monoclonal antibodies demonstrated a dissociation constant for renin of 10(-7) M. These monoclonal antibodies have great potential in answering significant questions concerning the structure, biosynthesis, tissue localization, and physiologic actions of renin.

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Monoclonal antibody against human renin.

By spleen cell fusion with NS1 myeloma, a mouse hybridoma was obtained which secretes an antibody directed against human renin. This monoclonal antibody recognizes human and monkey renin, but neither hog nor mouse. Preliminary experiments demonstrate the potential of this antibody for renin immunopurification and characterization.

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