Search results for: Biotin Labeled Anti mouse factor X Antibody
#31432158 2019/08/12 To Up
Construction and characterization of a truncated tissue factor‑coagulation‑based composite system for selective thrombosis in tumor blood vessels.
The selective induction of tumor vascular thrombosis using truncated tissue factor (tTF) delivered via a target ligand is a promising novel antitumor strategy. In the present study, an anti‑neuropilin‑1 (NRP‑1) monoclonal antibody (mAb)‑streptavidin (SA):tTF‑biotin (B) composite system was established. In this system, anti‑NRP‑1‑mAb located tTF to the tumor vascular endothelial cell surface and induced vascular embolization. Due to their high binding affinity, SA and B were used to enhance thrombogenic activity. mAb was conjugated with SA using a coupling method with water‑soluble 1‑ethyl‑3‑(3‑dimethylaminopropyl) carbodiimide and N‑hydroxysulfosuccinimide. Biotinylated tTF (tTF‑B) was prepared using a B‑labeling kit subsequent to the generation and purification of fusion protein tTF. Confocal microscopy and flow cytometry indicated that the anti‑NRP‑1‑mAb‑SA conjugate retained mAb targeting activity. The preservation of B‑conjugate binding capacity was confirmed using a competitive ELISA, and factor X‑activation analysis revealed that tTF‑B retained the procoagulant activity exhibited by tTF. Live imaging was performed to assess mAb‑SA distribution and tumor‑targeting capability, and this yielded promising results. The results of in vivo studies in mice with subcutaneous xenografts demonstrated that this composite system significantly induced tumor vascular thrombosis and inhibited tumor growth, whereas these histological changes were not observed in normal organs.Peilan Xu, Mingyuan Zou, Shengyu Wang, Tingting Li, Cong Liu, Li Wang, Lanlan Wang, Fanghong Luo, Ting Wu, Jianghua Yan
1682 related Products with: Construction and characterization of a truncated tissue factor‑coagulation‑based composite system for selective thrombosis in tumor blood vessels.
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#8126163 // To Up
Enzyme-linked immunosorbent assay and enzyme-linked coagulation assay for detection of Clostridium botulinum neurotoxins A, B, and E and solution-phase complexes with dual-label antibodies.
The measurement of toxins A, B, and E from Clostridium botulinum was accomplished by use of a modified sandwich enzyme-linked immunosorbent assay (ELISA) employing labeled horse antibody and either chicken antibody or biotinylated horse antibody. The complexes formed in solution phase were captured onto solid phases coated with rabbit anti-chicken immunoglobulin G (chicken antibody) or avidin (biotinylated antibody). The assay was brought to the sensitivity of the mouse bioassay (5 to 10 pg/ml, or 0.03 to 0.07 pM) by employing as labeling enzyme the factor X activator of Russell's viper venom (RVV-XA) and a sensitive coagulation-based assay amplification system known as enzyme-linked coagulation assay. Complex formation was found to be a slower reaction than binding to the capture plate, and so the assay used a preincubation step to produce the solution-phase complexes before they were bound to the solid phase. Keeping the concentrations of Russell's viper venom factor X activator antibody and capture antibody constant for diluted samples and diluting complexes into buffer without keeping labeled antibody concentrations constant were equivalent in allowing the detection of low neurotoxin concentrations. This ELISA-enzyme-linked coagulation assay procedure is a convenient alternative to the mouse bioassay, which shows complete resolution of the neurotoxins in addition to the requisite sensitivity.G J Doellgast, G A Beard, J D Bottoms, T Cheng, B H Roh, M G Roman, P A Hall, M X Triscott
1365 related Products with: Enzyme-linked immunosorbent assay and enzyme-linked coagulation assay for detection of Clostridium botulinum neurotoxins A, B, and E and solution-phase complexes with dual-label antibodies.
900 tests1000 TESTS/0.65ml0.1 mg100 μg100tests100testsRelated Pathways
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