Search results for: Mouse Anti-Insulin(1G11) Monoclonal Antibody, Biotin conjugated, Isotype: IgG
#26316179 2015/08/24 To Up
On-bead antibody-small molecule conjugation using high-capacity magnetic beads.
Antibodies labeled with small molecules such as fluorophore, biotin or drugs play an important role in various areas of biological research, drug discovery and diagnostics. However, the majority of current methods for labeling antibodies is solution-based and has several limitations including the need for purified antibodies at high concentrations and multiple buffer exchange steps. In this study, a method (on-bead conjugation) is described that addresses these limitations by combining antibody purification and conjugation in a single workflow. This method uses high capacity-magnetic Protein A or Protein G beads to capture antibodies directly from cell media followed by conjugation with small molecules and elution of conjugated antibodies from the beads. High-capacity magnetic antibody capture beads are key to this method and were developed by combining porous and hydrophilic cellulose beads with oriented immobilization of Protein A and Protein G using HaloTag technology. With a variety of fluorophores it is shown that the on-bead conjugation method is compatible with both thiol- and amine-based chemistry. This method enables simple and rapid processing of multiple samples in parallel with high-efficiency antibody recovery. It is further shown that recovered antibodies are functional and compatible with downstream applications.Nidhi Nath, Becky Godat, Hélène Benink, Marjeta Urh
1074 related Products with: On-bead antibody-small molecule conjugation using high-capacity magnetic beads.
10 mL at 10 mg/mL1 ml5 mL at 10 mg/mL1 ml2 mL at 10 mg/mL1 ml1 mL at 10 mg/mL1 mL at 10 mg/mL1 mL at 10 mg/mL1ml1 mL at 10 mg/mL1 mL at 10 mg/mLRelated Pathways
#21707084 2011/07/06 To Up
Delivery of a peptide radiopharmaceutical to brain with an IgG-avidin fusion protein.
The genetic engineering, host cell expression, purity, identity, and in vivo brain drug targeting properties are described for a new IgG-fusion protein, designated the cTfRMAb-AV fusion protein. Avidin (AV) is fused to the carboxyl terminus of the heavy chain of the genetically engineered chimeric monoclonal antibody (mAb) against the mouse transferrin receptor (TfR). The TfRMAb binds the endogenous TfR on the blood-brain barrier (BBB), which triggers transport into brain from blood. The cTfRMAb-AV fusion protein is produced in stably transfected Chinese hamster ovary cells, which are grown in serum free medium under conditions of biotin starvation. Following affinity purification, the purity and identity of the cTfRMAb-AV fusion protein were verified by electrophoresis and Western blotting. The affinity of the cTfRMAb for the murine TfR is high, K(I) = 4.6 ± 0.5 nM, despite fusion of avidin to the antibody heavy chain. The model peptide radiopharmaceutical used in this study is the Aβ(1-40) amyloid peptide of Alzheimer's disease (AD), which in a brain-penetrating form could be used to image the amyloid plaque in brain in AD. The BBB transport and brain uptake of the [(125)I]-Aβ(1-40) peptide was measured in mice injected intravenously (IV) with the peptide either free or conjugated to the cTfRMAb-AV fusion protein. The brain uptake of the free Aβ(1-40) peptide was very low, 0.1% of injected dose (ID)/gram brain following i.v. injection, and is comparable to the brain uptake of a brain blood volume marker. However, the brain uptake of the Aβ(1-40) peptide was high, 2.1 ± 0.2% ID/gram brain, following attachment of the biotinylated peptide to the cTfRMAb-AV fusion protein. Capillary depletion analysis showed the peptide penetrated the brain parenchyma from blood. The cTfRMAb-AV fusion protein is a new drug delivery system that can target to mouse brain monobiotinylated peptide or antisense radiopharmaceuticals.Qing-Hui Zhou, Jeff Zhiqiang Lu, Eric Ka-Wai Hui, Ruben J Boado, William M Pardridge
1199 related Products with: Delivery of a peptide radiopharmaceutical to brain with an IgG-avidin fusion protein.
100 100 0.1 mg100ug200ul100ul 100ul100 100ug0.1 mg1mg200ulRelated Pathways
#19894757 // To Up
Molecularly defined antibody conjugation through a selenocysteine interface.
Antibody conjugates have broad utility in basic, preclinical, and clinical applications. Conventional antibody conjugation through the amine group of lysine or the thiol group of cysteine residues yields heterogeneous products of undefined stoichiometry and considerable batch-to-batch variability. To preserve the two hallmarks of the antibody molecule, precision and predictability, methods that enable site-specific antibody conjugation are in high demand. On the basis of a mammalian cell expression system, we describe the utilization of the 21st natural amino acid selenocysteine for the generation of IgG and Fab molecules with unique nucleophilic reactivity that affords site-specific conjugation to electrophilic derivatives of biotin, fluorescein, and poly(ethylene glycol). The resulting antibody conjugates were found to fully retain their antigen binding capability and, in the case of IgG, the ability to mediate effector functions. Gain of function was demonstrated in vitro and in vivo. While these antibody conjugates are relevant for a variety of proteomic, diagnostic, and therapeutic applications, they also constitute a proof of principle for the generation of molecularly defined antibody-drug conjugates and radioimmunoconjugates. Compared to other site-specific antibody conjugation methods, selenocysteine interface technology (i) only involves a minor modification at the C-terminus that does not interfere with disulfide bridges, (ii) does not require activation, and (iii) generates unique 1:1 stoichiometries of biological and chemical components. Collectively, our method affords the generation of highly defined antibody conjugates with broad utility from proteomic applications to therapeutic intervention.Thomas Hofer, Lauren R Skeffington, Colby M Chapman, Christoph Rader
1850 related Products with: Molecularly defined antibody conjugation through a selenocysteine interface.
100ul100ug100ug100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized1 Set100μgRelated Pathways
#19362845 2009/03/24 To Up
Design and synthesis of a photocleavable biotin-linker for the photoisolation of ligand-receptor complexes based on the photolysis of 8-quinolinyl sulfonates in aqueous solution.
The ability of avidin (Avn) to form strong complex with biotin (Btn) is frequently used in the detection and isolation of biomolecules in biochemical, analytical, and medicinal research. The fact that the binding is nealy irreversible, however, constitutes a drawback in term of the isolation and purification of intact biomolecules. We recently found that 8-quinolinyl esters of aromatic or aliphatic sulfonic acids undergo photolysis when irradiated at 300-330 nm in aqueous solution at neutral pH. In this work, a biotin-dopamine (BD) conjugate containing a photocleavable 8-quinolinyl benzenesulfonate (QB) linker, BDQB, was designed and synthesized for use in the efficient recovery of dopamine-protein (e.g., antibody) complexes from an Avn-Btn system. The complexation of BDQB with a primary anti-dopamine antibody (anti-dopamine IgG(1) from mouse) on an Avn-coated plate was confirmed by an enzyme-linked immunosorbent assay (ELISA) utilizing a secondary antibody (anti-IgG(1) antibody) conjugated with horseradish peroxidase (HRP). Upon the photoirradiation (at 313 nm) of the BDQB-IgG(1) complex, the release of dopamine-IgG(1) complex was confirmed by ELISA. Characterization of the resulting photoreleased dopamine-anti-dopamine IgG(1) complex was performed by SDS-PAGE and Western blot.Shin Aoki, Nanako Matsuo, Kengo Hanaya, Yasuyuki Yamada, Yoshiyuki Kageyama
2270 related Products with: Design and synthesis of a photocleavable biotin-linker for the photoisolation of ligand-receptor complexes based on the photolysis of 8-quinolinyl sulfonates in aqueous solution.
100ug1100ug100ugRelated Pathways
#11861781 // To Up
Platelet-endothelial cell adhesion molecule-1-directed immunotargeting to cardiopulmonary vasculature.
Therapeutic molecules conjugated with antibodies to the platelet-endothelial cell adhesion molecule-1 (PECAM-1) accumulate in the pulmonary endothelium after i.v. injection in mice. In this study, we characterized PECAM-directed targeting to the lung and heart after local versus systemic intravascular administration in a large animal model, pigs. Radiolabel tracing showed that 1 h post-i.v. injection, 35% of anti-PECAM versus 2.5% of control IgG had accumulated in the lungs. Infusion of anti-PECAM via a catheter placed in the right pulmonary artery (RPA) resulted in a 3-fold elevation of the uptake in the right lower lobe and 2-fold reduction of uptake in the left lobes in the lung. Cardiac uptake of anti-PECAM was negligible after i.v. and RPA infusion. In contrast, delivery with a catheter placed in the right coronary artery (RCA) resulted in a 4-fold elevation of cardiac uptake of anti-PECAM, but not IgG, compared with i.v. injection. To estimate the targeting of an active reporter enzyme, streptavidin-conjugated beta-galactosidase (beta-Gal) was coupled to anti-PECAM or IgG (anti-PECAM/beta-Gal and IgG/beta-Gal) and injected into the RCA. Beta-Gal activity was markedly elevated in the heart and lungs (5- and 25-fold increased, respectively) after injection of anti-PECAM/beta-Gal, but not IgG/beta-Gal. Image analysis confirmed endothelial targeting of anti-PECAM/beta-Gal in the heart and lung. In summary, anti-PECAM antibody conjugates deliver agents to the pulmonary endothelium regardless of injection route, whereas local arterial infusion permits targeting to the cardiac vasculature. This paradigm may be useful for drug targeting to endothelium in lungs, heart, and possibly other organs.Arnaud Scherpereel, Jonathan J Rome, Rainer Wiewrodt, Simon C Watkins, David Winslow Harshaw, Sean Alder, Melpo Christofidou-Solomidou, Elliott Haut, Juan-Carlos Murciano, Marian Nakada, Steven M Albelda, Vladimir R Muzykantov
1814 related Products with: Platelet-endothelial cell adhesion molecule-1-directed immunotargeting to cardiopulmonary vasculature.
96tests96tests1.00 flask1.00 flask1.00 flask11.00 flask1.00 flask 6 ml Ready-to-use 1.00 flask1.00 flask100.00 ugRelated Pathways
#11756693 2001/12/26 To Up
Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domains.
To study the molecular structure and function of gene products in situ, we developed a molecular immunolabeling technology. Starting with cDNA from hybridomas producing monoclonal antibodies against biotin, catalase, and superoxide dismutase, we bioengineered recombinant single-chain variable fragment antibodies (scFv) and their derivatives containing metal-binding domains (scFv:MBD). As tested with surface plasmon resonance and enzyme-linked immunosorbent assay, affinity binding constants of the scFv (5.21 x 10(6) M(-1)) and scFv:MBD (4.17 x 10(6) M(-1)) were close to those of Fab proteolytic fragments (9.78 x 10(6) M(-1)) derived from the parental IgG antibodies. After saturation of MBD with nickel or cobalt, scFv:MBD was imaged with electron spectroscopic imaging at each element's specific energy loss, thus generating the element's map. Immunolabeling with scFv:MBD resulted in a significant improvement of the labeling fidelity over that obtained with Fab or IgG derivatives, as it produced a much heavier specific labeling and label-free background. As determined with radioimmunoassay, labeling effectiveness with scFv:MBD was nearly the same as with scFv, but much higher than with scFv conjugated to colloidal gold, Nanogold, or horseradish peroxidase. This technology opens possibilities for simultaneous imaging of multiple molecules labeled with scFv:MBD at the molecular resolution within the same sample with electron spectroscopic imaging. Moreover, the same scFv:MBD can also be imaged with fluorescence resonance energy transfer and lifetime imaging as well as positron emission tomography and magnetic resonance imaging. Therefore, this technology may serve as an integrative factor in life science endeavors.Marek Malecki, Annie Hsu, Lynn Truong, Sylvia Sanchez
2567 related Products with: Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domains.
1 ml1mg1 mg100.00 ug1 mg0.1 ml1mg1000 TESTS/0.65ml1 mL1 ml100 2Related Pathways
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#10973889 // To Up
Streptavidin-polyvinylamine conjugates labeled with a europium chelate: applications in immunoassay, immunohistochemistry, and microarrays.
The favorable properties of lanthanide chelates compared with conventional fluorescent probes have attracted considerable interest. A Eu(3+) chelator, 4,7-bis(chlorosulfophenyl)-1, 10-phenanthroline-2,9-dicarboxylic acid (BCPDA), has been synthesized previously.A Scorilas, A Bjartell, H Lilja, C Moller, E P Diamandis
1504 related Products with: Streptavidin-polyvinylamine conjugates labeled with a europium chelate: applications in immunoassay, immunohistochemistry, and microarrays.
500 1 Set100 μg1 Set1 Set250 MG10100 Tests100ug100 μgRelated Pathways
#9219060 // To Up
Enzyme immunoassays for specific IgG and IgE antibodies to Pichia pastoris components in normal humans.
We developed enzyme immunoassays for human anti-Pichia pastoris components (PPC) IgG and anti-PPC IgE antibody titers. Anti-PPC IgG antibody assay were performed using antigen-coated plate and anti-human IgG peroxidase conjugate. The intra- and interassay coefficients of variation (CV) of anti-PPC IgG antibody were 1.83-2.51% and 1.97-2.76%, respectively. The anti-PPC IgE antibody assay was performed using an anti-IgE monoclonal antibody-coated plate, biotin-labeled PPC and avidin-labeled peroxidase, which was not subject to interference by the high titer of anti-PPC IgG antibody. The intra- and interassay CV were 3.83-5.34% and 3.56-5.84%, respectively. We determined and compared anti-PPC IgG antibody titers in the 40 normal individuals. We confirmed that a high titer of anti-PPC IgG antibody is contained in all normal human sera and that these antibodies are directed primarily to mannan by immunoblotting analysis. The ratio of the maximum to minimum anti-PPC IgG antibody titers in normal individuals was > 8,000. Anti-PPC IgG antibody titers did not correlate with the age. However, we did not detect anti-PPC IgE antibody in normal individuals.W Ohtani, K Kobayashi, T Ohmura
1576 related Products with: Enzyme immunoassays for specific IgG and IgE antibodies to Pichia pastoris components in normal humans.
4 Membranes/Box2 Pieces/Box4 Arrays/Slide4 Membranes/Box2 Pieces/Box2 Pieces/Box100 ug4 Membranes/BoxRelated Pathways
#8576573 // To Up
Enzyme-labelled antibody-avidin conjugates: new flexible and sensitive immunochemical reagents.
We have prepared avidin-labelled antibodies ('shuttles') with the aim of increasing the sensitivity of detecting mouse IgG and human complement factors in ELISA tests and of detecting monoclonal antibodies and digoxigenin haptens (DIG) in hybridization and immunoblot procedures. Avidin-D was conjugated to goat IgG anti-mouse IgG or to anti-digoxigenin antibodies by thiol/maleimide chemistry. Conjugates of different molecular weight were obtained by Superdex 200 gel filtration. The avidin-D-labelled antibodies were then incubated with biotinylated horseradish peroxidase or with biotinylated alkaline phosphatase. Such preformed enzyme-labelled complexes were subsequently used in the various assays. A 5-8-fold increase in sensitivity was found when the preformed enzyme-labelled antibody-avidin-D complexes were compared to directly enzyme-labelled antibodies or antibody fragments. Furthermore it was shown that ELISA procedures employing digoxigenin-labelled polyclonal antibodies detected by shuttle conjugates were approximately five times more sensitive than biotinylated antibodies detected by avidin-biotin complexes (ABC method). The greatest sensitivity was obtained using antibody-avidin complexes which consisted of two IgG molecules and 4-6 avidin-D molecules.R P van Gijlswijk, D J van Gijlswijk-Janssen, A K Raap, M R Daha, H J Tanke
1341 related Products with: Enzyme-labelled antibody-avidin conjugates: new flexible and sensitive immunochemical reagents.
100ug1 kit100ug100ul100ug1 ml100μg100μg100ug100ug1,000 testsRelated Pathways
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