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Search results for: Mouse Anti-Human C4b Antibodies

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Deciphering complement interference in anti-human leukocyte antigen antibody detection with flow beads assays.

Anti-human leukocyte antigen (HLA) antibody detection in solid-phase flow beads assays can be quenched by complement activation, but the precise mechanism of this interference is not fully elucidated yet.
Jonathan Visentin, Margaux Vigata, Sophie Daburon, Cécile Contin-Bordes, Véronique Fremeaux-Bacchi, Claire Dromer, Marc-Alain Billes, Martine Neau-Cransac, Gwendaline Guidicelli, Jean-Luc Taupin

1697 related Products with: Deciphering complement interference in anti-human leukocyte antigen antibody detection with flow beads assays.

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Isolation and characterization of complement receptor type 1 from rat glomerular epithelial cells.

Complement receptor type 1 (C3b/C4b receptor, CR1) is known to be present in human glomerular epithelial cells (GEC) in vivo. The presence of CR1 has not been documented in rat glomeruli, although cultured rat GEC appear to express CR1 based upon their ability to rosette with complement-coated erythrocytes. In this study, we establish that CR1 is present in cultured rat GEC: (1) by isolating a 200 kDa protein from detergent-solubilized cultured rat GEC through the use of C3b affinity chromatography; (2) by Western blotting studies demonstrating reactivity of anti-human CR1 antibodies with this protein from cultured GEC; and (3) by demonstrating that C3b binding to GEC monolayers exhibits low affinity and that an estimate of the number of binding sites is 6700 per cell, both of which are comparable to that seen for CR1 in human blood cells. Furthermore, we show that CR1 is also present in rat glomeruli by Western blotting studies with anti-human CR1. Anti-human CR1 also identifies a 70 kDa protein from cultured GEC and isolated glomeruli. This 70 kDa protein is likely to be the CR1-like protein, designated Crry, which was initially identified in the mouse and has significant homology to human CR1. Crry may be present in rat GEC instead of decay accelerating factor, which is present in human GEC.
R J Quigg, M L Galishoff, A E Sneed, D Kim

2522 related Products with: Isolation and characterization of complement receptor type 1 from rat glomerular epithelial cells.

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Monoclonal anti-human C4b antibodies: stabilization and inhibition of the classical-pathway C3 convertase.

Two IgG mouse monoclonal antibodies (MAbs), Abs 242 and 463, were prepared by fusion of spleen cells from mice immunized with human C4b with a myeloma cell line, P3/ X 63-Ag 8.653. They were assessed for their effect on the activation and stability of the cell-bound classical-pathway C3 convertase, EAC14b2a and on the binding of C2 and C4bp to EC4b. Ab 242 recognized a conformational neoantigen which appeared upon activation of C4 with C-1s and disappeared after chain separation of C4b, while Ab 463 recognized a linear epitope in the beta-chain of C4b. Ab 242 was found to be a C4bp-like MAb: it accelerates the decay-dissociation of C3 convertase and interferes with the binding of C2 to C4b. It also interfered with the binding of C4bp to C4b. These results suggest that Ab 242 recognizes an epitope which is closely related to the C2- and C4bp-binding sites in C4b. Ab 463, on the other hand, was found to be a nephritic factor like MAb: it prolongs the half-life of C3 convertase from 8 to 30 min at 37 degrees C.
C Ichihara, T Nakamura, S Nagasawa, J Koyama

1657 related Products with: Monoclonal anti-human C4b antibodies: stabilization and inhibition of the classical-pathway C3 convertase.

1 ml100.00 ug0.1 mg100ul50ul1 ml50ul100.00 ug100 μg100 μg0.1 mg50

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