Search results for: Mouse Anti-Insulin(1D4:) Monoclonal Antibody, Biotin conjugated, Isotype: IgG
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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.
1956 related Products with: On-bead antibody-small molecule conjugation using high-capacity magnetic beads.Protein A G L Magnetic Be NanoLink™ 4FB Magnetic Protein G Magnetic Beads MagnaLink™ Streptavidin NanoLink™ Streptavidin Protein L Magnetic Beads NanoLink™ Amino Magneti MagnaLink™ Amino Magnet Protein A Magnetic Beads NanoLink™ Streptavidin NanoLink™ Streptavidin Protein A G Magnetic Bead
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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.
1143 related Products with: Delivery of a peptide radiopharmaceutical to brain with an IgG-avidin fusion protein.Mouse Anti-RSV Fusion Pro Polyclonal Antibody Excha Brain Natriuretic Peptide Mouse Anti-RSV Fusion Pro Anti-human brain natriure FIV Core Ag, recombinant TOM1-like protein 2 antib Mouse Anti-Parainfluenza Anti-Bsx(Brain-specific h Brain Natriuretic Peptide Mouse Anti-RSV Fusion Pro Polyclonal Antibody Viral
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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.
2719 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.FDA Standard Frozen Tissu Rabbit Anti-Insulin Recep Multiple organ tumor tiss Rabbit Anti-Insulin Recep FDA Standard Frozen Tissu Thermal Shaker with cooli FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Rabbit Anti-Insulin Recep FDA Standard Frozen Tissu Rabbit Anti-Insulin Recep
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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.
1761 related Products with: Platelet-endothelial cell adhesion molecule-1-directed immunotargeting to cardiopulmonary vasculature.Human soluble vascular ce Human vascular cell adhes Human Tonsil Microvascula Human Cardiac Microvascul RFP Expressing Human Umbi Nycodenz, non ionic, non Human Dermal Microvascula RFP Expressing Human Reti Human Small Intestine Mic GFP Expressing Human Saph CELLKINES PLATELET DERIVE Mouse Brain Microvascular
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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.
1631 related Products with: Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domains.Proteins and Antibodies H Rabbit Anti-HBV Receptor Rabbit Anti-Human Lambda Mouse Anti-HCV NS-4 (Reco Goat Anti-Human Cdc42-bin Goat Anti-Human IgG, heav Viral antibodies, anti-H Mouse Anti-Insulin, penta Rabbit Anti-C. botulinum Recombinant Anti-HBV HBsA Mouse Anti-Human Retinol Goat Anti-Human Kinesin H
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Synthesis of N,N'-bis(acrylamido)acetic acid-based T-antigen glycodendrimers and their mouse monoclonal IgG antibody binding properties.Novel glycodendrimers based on N,N'-bis(acrylamido)acetic acid core with valencies between two and six were synthesized. The breast cancer-associated T-antigen carbohydrate marker, (beta-Gal-(1-3)-alpha-GalNAc-OR), was then conjugated by (i) 1,4-conjugate addition of thiolated T-antigen to the N-acrylamido dendritic cores and by (ii) amide bond formation between an acid derivative of the T-antigen and the polyamino dendrimers. The protein-binding ability of these new glycodendrimers was fully demonstrated by turbidimetric analysis and by enzyme-linked immunosorbent assay (ELISA) using peanut lectin from Arachis hypogaea and a mouse monoclonal antibody (MAb) FAA-J11 (IgG3). When tested as inhibitors of binding between MAb and a polymeric form of the T-antigen (T-antigen-co-polyacrylamide) used as a coating antigen, di- (17), tetra- (20), hexa- (21), and tetravalent (22) dendrimers showed IC(50) values of 174, 19, 48, and 18 nM, respectively. Two tetramers showed 120- to approximately 128-fold increased inhibitory properties over the monovalent antigen 6 used as a standard (IC(50) 2.3 mM). Heterobifunctional glycodendrimer bearing a biotin probe was also prepared for cancer cell labeling.
1474 related Products with: Synthesis of N,N'-bis(acrylamido)acetic acid-based T-antigen glycodendrimers and their mouse monoclonal IgG antibody binding properties.Folic Acid antibody, Mono HBsAg antibody, Monoclona Shiga Toxin 1 antibody, M Amphetamine antibody, Mon hCG beta antibody, Monocl HBsAg antibody, Monoclona Bacillus anthracis (Anthr CRP antibody, Monoclonal EBV antibody, Monoclonal HBeAg antibody, Monoclona HIV1 p24 antibody, Monocl Mouse (monoclonal) AntiLa
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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.
1864 related Products with: Enzyme-labelled antibody-avidin conjugates: new flexible and sensitive immunochemical reagents.Leptin ELISA Kit, Human A Anti-Avidin peroxidase co Anti-ACE-1 (Angiotension Androgen Receptor (Phosph Anti-ADAM-17 (A Disintegr Avidin -RHODAMINE Antibod Anti-Ace2(Angiotensin-con Anti-Avidin produced in r Anti-ACE-1 (Angiotension Angiotensin-Converting En Anti-Adenovirus Fluoresce Angiotensin Converting En
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Rapid immunoassays for the measurement of immunoglobulin G subclass concentration in immunoglobulin preparations and human serum.Enzyme immunoassays (EIA) capable of determining total IgG1, IgG2, IgG3 and IgG4 subclass concentrations in human serum preparations have been developed. Subclass-specific monoclonal antibodies (mAbs) are bound to polyacrylamide bead-conjugated anti-mouse immunoglobulin antibodies. Bound immunoglobulins are detected with a peroxidase-conjugated anti-IgG antibody or a biotin-conjugated anti-IgG antibody followed by peroxidase streptavidin. The standard curves were found to be linear in the regions 16.0-2.0 micrograms/ml for IgG1, 4.0-0.5 micrograms/ml for IgG2, 0.4-0.06 micrograms/ml for IgG3 and 0.25-0.05 micrograms/ml for IgG4. Coefficient of variation (CV) values range from 0.32-7.32% for IgG1, 0.66-4.85% for IgG2, 1.62-6.85% for IgG3 and 0.05-6.47% for IgG4 standard curves. The inter-assay variability for the control human serum samples was 9.6% for IgG1, 6.7% for IgG2, 9.5% for IgG3 and 6.8% for IgG4.
2638 related Products with: Rapid immunoassays for the measurement of immunoglobulin G subclass concentration in immunoglobulin preparations and human serum.Goat Anti-Human FRA1 FOSL Goat Anti-Human Urocortin Goat Anti-Human MRP8 ABCC Goat Anti-Human NPFFR1, ( Goat Anti-Human Synaptogy Goat Anti-Human, Mouse VA Goat Anti-Human Aminopept Goat Anti-Human BNIP1, (i Goat Anti-Human EPB41L2 4 Goat Anti-Human SERPINB6, Goat Anti-Human GALNS, (i Goat Anti-Human, Mouse TA
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Tumor-reactive human immunoglobulin G monoclonal antibody from a melanoma patient.To study tumor-associated antigens that are immunogenic to humans, we have generated human monoclonal antibodies by fusing lymph node lymphocytes of a melanoma patient with a mouse myeloma cell line. We examined in detail the reactivity of one IgG antibody, termed 2-139-1. Immunostaining was performed with purified antibody conjugated to biotin. Binding was visualized by the avidin-biotin-peroxidase complex. With cultured cells, 2-139-1 stained 12 of 12 melanomas and 12 of 16 carcinomas. Reactivity was not detectable in seven neural crest tumors, six sarcomas, and 45 lymphomas and leukemias. This spectrum of reactivity was confirmed with sections of human tissues. The human monoclonal antibody 2-139-1 reacted against melanomas and not banal nevi. While the antibody reacted strongly to adenocarcinomas of the colon, prostate, rectum, and pancreas, it did not stain all the carcinomas tested. Furthermore, reactivity was not seen against sarcomas. Interestingly, 2-139-1 did not bind to the majority of the cells in normal tissues, including fetal tissues. The reactivity of 2-139-1 may be representative of the humoral immune response found in the regional lymph nodes of cancer patients. The distribution of this epitope in various tumors was fairly limited and appeared to be associated with malignant transformation.
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An improved method for the detection of IgE antibody of defined specificity by ELISA using rat monoclonal anti-IgE antibody.An improved method for the detection of IgE antibody of defined specificity by ELISA using rat monoclonal anti-IgE antibodies is described. The innovation consists of coating the plates first by a monoclonal rat anti-murine IgE antibody, adding the sera to this antibody-coated plates and then adding the biotin-conjugated antigen after the sera. The plates are then reacted with streptavidin-peroxidase and developed. This procedure eliminates possible competitions with other isotypes of the same specificity. The method is useful especially to quantitate IgE with defined specificity in the presence of high amounts of isotypes of the same specificity.
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