Search results for: Mouse Anti-GAPDH(3E12)-Loading Control Monoclonal Antibody, PE-Cy5.5 conjugated Isotype: IgG
#29724483 2018/04/30 To Up
Immune suppression of food allergy by maternal IgG in murine models.Most of the patients develop food allergy early in life. The factors related to parental immune condition might be one of the conceivable causes.
Hirotaka Yamashita, Tadamasa Hayashi, Kenichi Saneyasu, Hiroki Matsuhara, Teruaki Matsui, Hiroyuki Tanaka, Naoki Inagaki100 ul0.1ml100 µg100 ul0.1ml (1mg/ml)100 ug0.1ml1 mg0.1ml0.1ml96 wells0.1ml
#26661181 2015/10/06 To Up
Internalization of targeted quantum dots by brain capillary endothelial cells in vivo.Receptors located on brain capillary endothelial cells forming the blood-brain barrier are the target of most brain drug delivery approaches. Yet, direct subcellular evidence of vectorized transport of nanoformulations into the brain is lacking. To resolve this question, quantum dots were conjugated to monoclonal antibodies (Ri7) targeting the murine transferrin receptor. Specific transferrin receptor-mediated endocytosis of Ri7-quantum dots was first confirmed in N2A and bEnd5 cells. After intravenous injection in mice, Ri7-quantum dots exhibited a fourfold higher volume of distribution in brain tissues, compared to controls. Immunofluorescence analysis showed that Ri7-quantum dots were sequestered throughout the cerebral vasculature 30 min, 1 h, and 4 h post injection, with a decline of signal intensity after 24 h. Transmission electron microscopic studies confirmed that Ri7-quantum dots were massively internalized by brain capillary endothelial cells, averaging 37 ± 4 Ri7-quantum dots/cell 1 h after injection. Most quantum dots within brain capillary endothelial cells were observed in small vesicles (58%), with a smaller proportion detected in tubular structures or in multivesicular bodies. Parenchymal penetration of Ri7-quantum dots was extremely low and comparable to control IgG. Our results show that systemically administered Ri7-quantum dots complexes undergo extensive endocytosis by brain capillary endothelial cells and open the door for novel therapeutic approaches based on brain endothelial cell drug delivery.
Sarah Paris-Robidas, Danny Brouard, Vincent Emond, Martin Parent, Frédéric Calon
2528 related Products with: Internalization of targeted quantum dots by brain capillary endothelial cells in vivo.1.00 flask1.00 flask1.00 flask1.00 flask1.00 flask1.00 flask1.00 flask1.00 flask1.00 flask1x10e7 cells48 samples
#25908833 2015/04/23 To Up
Small-Animal PET Imaging of Pancreatic Cancer Xenografts Using a 64Cu-Labeled Monoclonal Antibody, MAb159.Overexpression of the GRP78 receptor on cell surfaces has been linked with tumor growth, metastasis, and resistance to therapy. We developed a (64)Cu-labeled probe for PET imaging of tumor GRP78 expression based on a novel anti-GRP78 monoclonal antibody, MAb159.
Hui Wang, Dan Li, Shuanglong Liu, Ren Liu, Hong Yuan, Valery Krasnoperov, Hong Shan, Peter S Conti, Parkash S Gill, Zibo Li
1378 related Products with: Small-Animal PET Imaging of Pancreatic Cancer Xenografts Using a 64Cu-Labeled Monoclonal Antibody, MAb159.100100100100ul0.1mg1001mg0.1mg1mg100ul100ug100ul
#24054660 2013/06/28 To Up
Real-time and sensitive detection of Salmonella Typhimurium using an automated quartz crystal microbalance (QCM) instrument with nanoparticles amplification.The accidental contamination of Salmonella in raw and processed foods is a major problem for the food industry worldwide. At present many of the currently used methods for Salmonella detection are time and labour intensive. Therefore, rapid detection is a key to the prevention and identification of problems related to health and safety. This paper describes the application of a new quartz crystal microbalance (QCM) instrument with a microfluidic system for the rapid and real time detection of Salmonella Typhimurim. The QCMA-1 bare gold sensor chip which contain two sensing array was modified by covalently immobilising the monoclonal capture antibody on the active spot and a mouse IgG antibody on the control spot using a conventional amine coupling chemistry (EDC-NHS). The binding of the Salmonella cells onto the immobilised anti-Salmonella antibody alters the sensor frequency which was correlated to cells concentration in the buffer samples. Salmonella cells were detected using direct, sandwich, and sandwich assay with antibody conjugated gold-nanoparticles. The performance of the QCM immunosensor developed with gold-nanoparticles gave the highest sensitivity with a limit of detection (LOD) ~10-20 colony forming unit (CFU) ml(-1) compared to direct and sandwich assay (1.83 × 10(2) CFU ml(-1) and 1.01 × 10(2) CFU ml(-1), respectively). The sensor showed good sensitivity and selectivity for Salmonella in the presence of other bacteria in real food samples and helped in reducing the pre-enrichment step, hence, demonstrating the potential of this technology for the rapid and sensitive microbial analysis.
Faridah Salam, Yildiz Uludag, Ibtisam E Tothill
2616 related Products with: Real-time and sensitive detection of Salmonella Typhimurium using an automated quartz crystal microbalance (QCM) instrument with nanoparticles amplification.100ug Lyophilized25100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized1 mg100ug Lyophilized100ug Lyophilized96 tests100ug Lyophilized2 mL
#23298904 2013/01/08 To Up
Identification of the optimal therapeutic antibody for fluorescent imaging of cutaneous squamous cell carcinoma.Intraoperative, real-time fluorescence imaging may significantly improve tumor visualization and resection and postoperatively, in pathological assessment. To this end, we sought to determine the optimal FDA approved therapeutic monoclonal antibody for optical imaging of human cutaneous squamous cell carcinoma (cSCC). A near-infrared (NIR) fluorescent probe (IRDye800) was covalently linked to bevacizumab, panitumumab or tocilizumab and injected systemically into immunodeficient mice bearing either cutaneous tumor cell lines (SCC13) or cutaneous human tumor explants. Tumors were then imaged and resected under fluorescent guidance with the SPY, an FDA-approved intraoperative imaging system, and the Pearl Impulse small animal imaging system. All fluorescently labeled antibodies delineated normal tissue from tumor in SCC13 xenografts based on tumor-to-background (TBR) ratios. The conjugated antibodies produced TBRs of 1.2-2 using SPY and 1.6-3.6 using Pearl; in comparison, isotype control antibody IgG-IRDye produced TBRs of 1.0 (SPY) and 0.98 (Pearl). Comparison between antibodies revealed them to be roughly equivalent for imaging purposes with both the SPY and Pearl (p = 0.89 SPY, p = 0.99 Pearl; one way ANOVA). Human tumor explants were also imaged and tumor detection was highest with panitumumab-IRDye800 when using the SPY (TBR 3.0) and Pearl (TBR 4.0). These data suggest that FDA approved antibodies may be clinically used for intraoperative detection of cSCC.
Kristine E Day, Lauren N Beck, C Hope Heath, Conway C Huang, Kurt R Zinn, Eben L Rosenthal
1632 related Products with: Identification of the optimal therapeutic antibody for fluorescent imaging of cutaneous squamous cell carcinoma.96tests
#22988081 2012/09/17 To Up
Synthesis of site-specific antibody-drug conjugates using unnatural amino acids.Antibody-drug conjugates (ADCs) allow selective targeting of cytotoxic drugs to cancer cells presenting tumor-associated surface markers, thereby minimizing systemic toxicity. Traditionally, the drug is conjugated nonselectively to cysteine or lysine residues in the antibody. However, these strategies often lead to heterogeneous products, which make optimization of the biological, physical, and pharmacological properties of an ADC challenging. Here we demonstrate the use of genetically encoded unnatural amino acids with orthogonal chemical reactivity to synthesize homogeneous ADCs with precise control of conjugation site and stoichiometry. p-Acetylphenylalanine was site-specifically incorporated into an anti-Her2 antibody Fab fragment and full-length IgG in Escherichia coli and mammalian cells, respectively. The mutant protein was selectively and efficiently conjugated to an auristatin derivative through a stable oxime linkage. The resulting conjugates demonstrated excellent pharmacokinetics, potent in vitro cytotoxic activity against Her2(+) cancer cells, and complete tumor regression in rodent xenograft treatment models. The synthesis and characterization of homogeneous ADCs with medicinal chemistry-like control over macromolecular structure should facilitate the optimization of ADCs for a host of therapeutic uses.
Jun Y Axup, Krishna M Bajjuri, Melissa Ritland, Benjamin M Hutchins, Chan Hyuk Kim, Stephanie A Kazane, Rajkumar Halder, Jane S Forsyth, Antonio F Santidrian, Karin Stafin, Yingchun Lu, Hon Tran, Aaron J Seller, Sandra L Biroc, Aga Szydlik, Jason K Pinkstaff, Feng Tian, Subhash C Sinha, Brunhilde Felding-Habermann, Vaughn V Smider, Peter G Schultz
1947 related Products with: Synthesis of site-specific antibody-drug conjugates using unnatural amino acids.100 ug100ug Lyophilized4 Membranes/Box100μg4 Arrays/Slide4 Membranes/Box4 Membranes/Box100ug Lyophilized4 Membranes/Box100μg100ug4 Arrays/Slide
#22509912 // To Up
Model IgG monoclonal autoantibody-anti-idiotype pair for dissecting the humoral immune response to oxidized low density lipoprotein.Increasing evidence implicates IgG autoantibodies against oxidized forms of low density lipoprotein (oxLDL) in the pathophysiology of atherosclerotic arterial disease. However, insufficient knowledge of their structure and function is a key gap. Using an elderly LDL receptor-deficient atherosclerotic mouse, we isolated a novel IgG3k against oxLDL (designated MAb LO1). LO1 reacts with copper-oxidized LDL, but minimally with native LDL. Further analysis showed that MAb LO1 also reacts in vitro with malondialdehyde-conjugated LDL (MDA-LDL), a known key epitope in copper-oxidized LDL preparations. By screening a phage library expressing single chain variable region antibodies (scFv), we selected an anti-idiotype scFv (designated H3) that neutralizes MAb LO1 binding to MDA-LDL. Amino acid substitutions between H3 and an irrelevant control scFv C12 showed that residues in the H3 CDRH2, CDRH3, and CDRL2 are all critical for MAb LO1 binding, consistent with a conformational epitope on H3 involving both heavy and light chains. Comparison of amino acids in H3 CDRH2 and CDRL2 with apoB, the major LDL protein, showed homologous sequences, suggesting H3 has structural similarities to the MAb LO1 binding site on MDA-LDL. Immunocytochemical staining showed that MAb LO1 binds epitopes in mouse and human atherosclerotic lesions. The MAb LO1-H3 combination therefore provides a very promising model for analyzing the structure and function of an individual IgG autoantibody in relation to atherosclerosis.
Shang-Hung Chang, Michael Johns, Joseph J Boyle, Ellen McConnell, Paul A Kirkham, Colin Bicknell, M Zahoor-ul-Hassan Dogar, Robert J Edwards, Oliver Gale-Grant, Ramzi Khamis, Kurrun V V Ramkhelawon, Dorian O Haskard
2851 related Products with: Model IgG monoclonal autoantibody-anti-idiotype pair for dissecting the humoral immune response to oxidized low density lipoprotein.1 ml0.2 mg100 TESTS0.25 mg100 ul100 ul100 ul100 ul100 ul100 ug/vial100 ul100ug Lyophilized
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#18829494 // To Up
Therapy of advanced B-lymphoma xenografts with a combination of 90Y-anti-CD22 IgG (epratuzumab) and unlabeled anti-CD20 IgG (veltuzumab).Antibodies are effective therapeutic agents in cancer, but cures are rarely if ever obtained. Combination therapies are likely to be more effective than a single agent. In this study, the combination of a new unconjugated humanized anti-CD20 IgG, veltuzumab, with a (90)Y-conjugated humanized antibody to CD22 (epratuzumab) was evaluated for the treatment of B-cell lymphoma in a nude mouse model system.
M Jules Mattes, Robert M Sharkey, Habibe Karacay, Myron S Czuczman, David M Goldenberg
2391 related Products with: Therapy of advanced B-lymphoma xenografts with a combination of 90Y-anti-CD22 IgG (epratuzumab) and unlabeled anti-CD20 IgG (veltuzumab).0.1ml (1mg/ml)0.5 mg100 ul1 mg100 μg100 ul0.2 mg0.5 mg100 ul100 ul100 ul100 µg
#18523585 2008/06/04 To Up
Liposomal co-entrapment of CD40mAb induces enhanced IgG responses against bacterial polysaccharide and protein.Antibody against CD40 is effective in enhancing immune responses to vaccines when chemically conjugated to the vaccine antigen. Unfortunately the requirement for chemical conjugation presents some difficulties in vaccine production and quality control which are compounded when multivalent vaccines are required. We explore here an alternative to chemical conjugation, involving the co-encapsulation of CD40 antibody and antigens in liposomal vehicles.
Caterina Hatzifoti, Andrew Bacon, Helen Marriott, Peter Laing, Andrew W Heath
1200 related Products with: Liposomal co-entrapment of CD40mAb induces enhanced IgG responses against bacterial polysaccharide and protein.100 µg100 µg100 ul1 mg1000 TESTS/0.65ml100 µg100 µg0.1ml (1mg/ml)100 μg1 mg500 ml1 mg
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