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           Search results for: BSA | bovine serum albumin, biotinylated Antibody   

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#28976746   2017/10/04 Save this To Up

Tailored Multivalent Neo-glycoproteins: Synthesis, Evaluation and Application of a Library of Galectin-3-binding Glycan Ligands.

Galectin-3 (Gal-3), a member of the β-galactoside binding lectin family, is a tumor biomarker and involved in tumor angiogenesis and metastasis. Gal-3 is therefore considered as promising target for early cancer diagnosis and anti-cancer therapy. We here present the synthesis of a library of tailored multivalent neo-glycoproteins and evaluate their Gal-3 binding properties. By the combinatorial use of glycosyltransferases and chemo-enzymatic reactions, we first synthesized a set of N-acetyllactosamine (Galβ1,4GlcNAc, LacNAc type 2) based oligosaccharides featuring five different terminating glycosylation epitopes, respectively. Neo-glycosylation of bovine serum albumin (BSA) was accomplished by dialkyl squarate coupling to lysine residues resulting in a library of defined multivalent neo-glycoproteins. Solid-phase binding assays with immobilized neo-glycoproteins revealed distinct affinity and specificity of the multivalent glycan epitopes for Gal-3 binding. In particular, neo-glycoproteins decorated with N',N''-diacetyllactosamine (GalNAcβ1,4GlcNAc, LacdiNAc) epitopes showed high selectivity and were demonstrated to capture Gal-3 from human serum with high affinity. Furthermore, neo-glycoproteins with terminal biotinylated LacNAc glycan motif could be utilized as Gal-3 detection agents in a sandwich ELISA format. We conclude that, in contrast to antibody-based capture steps, the presented neo-glycoproteins are highly useful to detect functionally intact Gal-3 with high selectivity and avidity. We further gain novel insights into the binding affinity of Gal-3 using tailored multivalent neo-glycoproteins, which have the potential for an application in the context of cancer related biomedical research.

1311 related Products with: Tailored Multivalent Neo-glycoproteins: Synthesis, Evaluation and Application of a Library of Galectin-3-binding Glycan Ligands.

ribosome binding protein ribosome binding protein calcium binding protein P Cortisol Binding Globulin SH3 domain-binding protei Guanylate-binding protein amyloid beta precursor pr zona pellucida binding pr RNA binding motif protein SH3KBP1 binding protein 1 Anti Galectin(Gal 3) Huma Rabbit Anti-Rat Androgen

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#28870829   2017/09/05 Save this To Up

Chemiluminescence immunoassays for estradiol and ethinylestradiol based on new biotinylated estrogen derivatives.

New chemiluminescence-based immunoassays for sensitive detection of 17-β estradiol (E2) and ethinylestradiol (EE2) are described on the basis of the use of biotinylated estrogen derivatives. Estrogen derivatives bearing a carboxylic group (E2-COOH and EE2-COOH) on C-3 position were synthesized, covalently bound to aminated biotin and subsequently immobilized on avidin-coated microtiter plates. The assay principle was based on competition between free and immobilized estrogens for their binding to primary antibodies, with subsequent revelation using horseradish peroxidase (HRP)-labeled secondary antibodies. Under optimized conditions, the chemiluminescence immunoassays showed a highly sensitive response to E2 and EE2, with respective detection limits of 0.5 and 1.2 ng L(-1). The LOD achieved using biotinylated E2 was in the same order of magnitude as those obtained using commercially available E2-bovine serum albumin conjugate (E2-BSA). The developed devices were successfully applied to analysis wastewater treatment plants effluents (WWTP) with negligible matrix effect.

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MarkerGeneTM Fluorescent Cellufine Formyl , 50 ml Cellufine Formyl Media Cellufine Formyl , 500 ml Cellufine Formyl Media Cellufine Formyl Media Bcl-2 Oncoprotein; Clone Bcl-2 Oncoprotein; Clone Estrogen Receptor; Clone Estrogen Receptor; Clone c-erbB-2 Oncoprotein c-erbB-2 Oncoprotein

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#28626461   2017/06/19 Save this To Up

Neoglycoconjugate of Tetrasaccharide Representing One Repeating Unit of the Streptococcus pneumoniae Type 14 Capsular Polysaccharide Induces the Production of Opsonizing IgG1 Antibodies and Possesses the Highest Protective Activity As Compared to Hexa- and Octasaccharide Conjugates.

Identifying protective synthetic oligosaccharide (OS) epitopes of Streptococcus pneumoniae capsular polysaccharides (CPs) is an indispensable step in the development of third-generation carbohydrate pneumococcal vaccines. Synthetic tetra-, hexa-, and octasaccharide structurally related to CP of S. pneumoniae type 14 were coupled to bovine serum albumin (BSA), adjuvanted with aluminum hydroxide, and tested for their immunogenicity in mice upon intraperitoneal prime-boost immunizations. Injections of the conjugates induced production of opsonizing anti-OS IgG1 antibodies (Abs). Immunization with the tetra- and octasaccharide conjugates stimulated the highest titers of the specific Abs. Further, the tetrasaccharide ligand demonstrated the highest ability to bind OS and CP Abs. Murine immune sera developed against tetra- and octasaccharide conjugates promoted pathogen opsonization to a higher degree than antisera against conjugated hexasaccharide. For the first time, the protective activities of these glycoconjugates were demonstrated in mouse model of generalized pneumococcal infections. The tetrasaccharide conjugate possessed the highest protective activities. Conversely, the octasaccharide conjugate had lower protective activities and the lowest one showed the hexasaccharide conjugate. Sera against all of the glycoconjugates passively protected naive mice from pneumococcal infections. Given that the BSA-tetrasaccharide induced the most abundant yield of specific Abs and the best protective activity, this OS may be regarded as the most promising candidate for the development of conjugated vaccines against S. pneumoniae type 14 infections.

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Single Strand DNA Ligase, Single Strand DNA Ligase, Thermostable TDG Enzyme & Thermostable TDG Kit Thermostable TDG Kit (DIS Thermostable TDG Kit *DIS Bovine Androstenedione,AS Rat Anti-CCT theta Antibo Rabbit Anti-Theophylline Sheep Anti-Theophylline 3 FDA Standard Frozen Tissu FDA Standard Frozen Tissu

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#27600788   2016/09/21 Save this To Up

Immunoassay for determination of trilobolide.

Trilobolide (Tb) is a pharmacologically interesting sesquiterpene lactone isolated from Laser trilobum (L.) Borkh. Structural relation to a sarco/endoplasmic reticulum Ca(2+)-ATPase inhibitor thapsigargin bring promising prospects for Tb to be used in the development of new anti-cancer drugs. As long as there are still unanswered questions regarding its investigation, a need for novel analytical tools emerge. Since immunoassays serve as one of powerful tools within the investigation of natural products, the development of indirect competitive enzyme-linked immunosorbent assay (ELISA) utilizing coating based on avidin-biotin technology is described. In our set-up of ELISA, newly synthesized biotinylated Tb served as immobilized competitor. Tb-carboxymethyloxime-bovine serum albumin (BSA) and Tb-succinoyl-BSA conjugates were used separately for immunization of rabbits. Two sets of polyclonal antibodies (RAbs) were obtained. Antibodies against Tb-succinoyl-BSA conjugate (RAb No. 206) were chosen as the best. Under optimized conditions, limit of detection and 50% intercept of our ELISA were 849pg/mL and 8.89ng/mL, respectively. The cross-reactivity (CR) was tested on 10 structurally related compounds and CR did not exceed 6.1%. The reproducibility of the system is expressed as intra- and inter-assay coefficients of variation (9.7% and 11.4%, respectively). Based on conducted experiments, we proposed the use of ELISA for quantification of Tb in complex biological matrices such as plant extracts. A method was applied to analyze three extracts obtained from different parts of L. trilobum. Data obtained were compared to those acquired by UHPLC-MS/MS. The concordance between the methods (103-87%) showed the ability of ELISA to quantify Tb.

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QuantiChrom™ Formaldehy Cellufine Formyl , 50 ml Cellufine Formyl Media Cellufine Formyl , 500 ml Cellufine Formyl Media Cellufine Formyl Media Formalin Solution (20%) Formalin Solution (20%) Formalin Solution (20%) Formalin (10% Neutral Bu Formalin (10% Neutral Bu Zinc Formalin Solution

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#27399806   2016/07/11 Save this To Up

AMA0428, A Potent Rock Inhibitor, Attenuates Early and Late Experimental Diabetic Retinopathy.

Diabetic retinopathy (DR) is characterized by an early stage of inflammation and vessel leakage, and an advanced vasoproliferative stage. Also, neurodegeneration might play an important role in disease pathogenesis. The aim of this study was to investigate the effect of the Rho kinase (ROCK) inhibitor, AMA0428, on these processes.

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ELISA kit CLGI,Collagenas Caspase-3 Inhibitor Z-DEV Caspase-3 Inhibitor Z-DEV Caspase-Family Inhibitor Caspase-Family Inhibitor Caspase-6 Inhibitor Z-VEI Caspase-6 Inhibitor Z-VEI Caspase-1 Inhibitor Z-YVA Caspase-1 Inhibitor Z-YVA Caspase-8 Inhibitor Z-IET Caspase-8 Inhibitor Z-IET Caspase-2 Inhibitor Z-VDV

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#26092332   2015/06/20 Save this To Up

A new colorimetric platform for ultrasensitive detection of protein and cancer cells based on the assembly of nucleic acids and proteins.

An amplified colorimetric method has been developed for the detection of protein and cancer cells based on the assembly of nucleic acids and proteins for the first time. In this process, the assembly of nucleic acids was triggered by a biotinylated DNA strand after a sandwich immunoreaction. The biotinylated DNA strand and sandwich immunocomplex were connected by streptavidin. Then, the assembly of biotinylated bovine serum albumin (Biotin-BSA) and streptavidin-horseradish peroxidase (SA-HRP) occurred at a node of the assembled products of nucleic acids through the biotin-streptavidin reaction. Under the catalysis of horseradish peroxidase, 3,3',5,5'-tetramethylbenzidine (TMB) was oxidized by H2O2 and the oxidized product was analyzed by its UV-vis absorbance signal and sensitive colorimetric detection. This colorimetric sensor could not only achieve the quantitative determination of protein by UV-vis absorbance but could also be applied for semiquantitative determination by digital visualization. Using alpha-fetoprotein (AFP) as the model target, this proposed colorimetric method showed a wide linear range from 5 pg/mL to 1 ng/mL with a detection limit of 1.95 pg/mL by the instrument, and even 5 pg/mL target protein could be distinguished simply by the naked eye. This approach was then expanded to detect cancer cells based on the recognition of folic acid receptors that were over-expressed on the cancer cells by folic acid-tethered DNA. More importantly, this strategy can be further used as a universal colorimetric method for the determination of viruses or other proteins by changing the corresponding antibodies.

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Anti AGE 3 Monoclonal Ant Recombinant Human Androge Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Human RAGE AG Recombinant Human RAGE AG Recombinant Human RAGE AG Rabbit Anti-Rat Androgen

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#25905497   2015/06/03 Save this To Up

A novel electrochemical aptamer-antibody sandwich assay for lysozyme detection.

In this paper, we have reported a novel electrochemical aptamer-antibody based sandwich biosensor for the detection of lysozyme. In the sensing strategy, an anti-lysozyme aptamer was immobilized onto the carbon electrode surface by covalent binding via diazonium salt chemistry. After incubating with a target protein (lysozyme), a biotinylated antibody was used to complete the sandwich format. The subsequent additions of avidin-alkaline phosphatase as an enzyme label, and a 1-naphthyl phosphate substrate (1-NPP) allowed us to determine the concentration of lysozyme (Lys) via Differential Pulse Voltammetry (DPV) of the generated enzyme reaction product, 1-naphthol. Using this strategy, a wide detection range from 5 fM to 5 nM was obtained for a target lysozyme, with a detection limit of 4.3 fM. The control experiments were carried out by using bovine serum albumin (BSA), cytochrome c and casein. The results showed that the proposed biosensor had good specificity, stability and reproducibility for lysozyme analysis. In addition, the biosensor was applied for detecting lysozyme in spiked wine samples, and very good recovery rates were obtained in the range from 95.2 to 102.0% for lysozyme detection. This implies that the proposed sandwich biosensor is a promising analytical tool for the analysis of lysozyme in real samples.

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MarkerGeneTM Fluorescent MOUSE ANTI BOVINE ROTAVIR Detection Buffer A&B Anti Detection Buffer C&D Anti Mouse anti-chick type I c Mouse anti-chick type I c Mouse anti-bovine type I Mouse anti-bovine type I Mouse anti-porcine type I Mouse anti-porcine type I Mouse anti-human type I c Mouse anti-mouse type I c

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#24277607   2013/11/26 Save this To Up

Visualization of the membrane engineering concept: evidence for the specific orientation of electroinserted antibodies and selective binding of target analytes.

Membrane engineering is a generic methodology for increasing the selectivity of a cell biosensor against a target molecule, by electroinserting target-specific receptor-like molecules on the cell surface. Previous studies have elucidated the biochemical aspects of the interaction between various analytes (including viruses) and their homologous membrane-engineered cells. In the present study, purified anti-biotin antibodies from a rabbit antiserum along with in-house prepared biotinylated bovine serum albumin (BSA) were used as a model antibody-antigen pair of molecules for facilitating membrane engineering experiments. It was proven, with the aid of fluorescence microscopy, that (i) membrane-engineered cells incorporated the specific antibodies in the correct orientation and that (ii) the inserted antibodies are selectively interacting with the homologous target molecules. This is the first time the actual working concept of membrane engineering has been visualized, thus providing a final proof of the concept behind this innovative process. In addition, the fluorescence microscopy measurements were highly correlated with bioelectric measurements done with the aid of a bioelectric recognition assay.

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Multiple organ cancer tis Multiple organ tumor tiss MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD NATIVE HUMAN PROLACTIN, P Nuclear Membrane Receptor Angiogenesis (Human) Anti Angiogenesis (Human) Anti Angiogenesis (Mouse) Anti Apoptosis (Human) Antibod Atherosclerosis (Human) A Atherosclerosis (Mouse) A

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#24099991   2013/11/26 Save this To Up

Hyaluronan synthase 1 (HAS1) produces a cytokine-and glucose-inducible, CD44-dependent cell surface coat.

Hyaluronan is a ubiquitous glycosaminoglycan involved in embryonic development, inflammation and cancer. In mammals, three hyaluronan synthase isoenzymes (HAS1-3) inserted in the plasma membrane produce hyaluronan directly on cell surface. The mRNA level and enzymatic activity of HAS1 are lower than those of HAS2 and HAS3 in many cells, obscuring the importance of HAS1. Here we demonstrate using immunocytochemistry and transfection of fluorescently tagged HAS1 that its enzymatic activity depends on the ER-Golgi-plasma membrane traffic, like reported for HAS2 and HAS3. When cultured in 5 mM glucose, HAS1-transfected MCF-7 cells show very little cell surface hyaluronan, detected with a fluorescent hyaluronan binding probe. However, a large hyaluronan coat was seen in cells grown in 20 mM glucose and 1 mM glucosamine, or treated with IL-1β, TNF-α, or TGF-β. The coats were mostly removed by the presence of hyaluronan hexasaccharides, or Hermes1 antibody, indicating that they depended on the CD44 receptor, which is in a contrast to the coat produced by HAS3, remaining attached to HAS3 itself. The findings suggest that HAS1-dependent coat is induced by inflammatory agents and glycemic stress, mediated by altered presentation of either CD44 or hyaluronan, and can offer a rapid cellular response to injury and inflammation.

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D (+) Glucose anhydrous c Rabbit Anti-Nitric Oxide Fontana-Masson Stain Kit HBV surface recombinant a HBV surface recombinant a Anti C Reactive Protein A anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl anti HBsAg pre surface Ig Mouse Anti-Human CD44 [+F Rat Anti-Mouse CD44 [+FIT Rabbit Anti-Human Androge

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#23849086   2013/07/15 Save this To Up

Configuration of antibodies for assay of urinary cortisol in dogs influences analytic specificity.

Whether the variation in the reported urinary corticoid-to-creatinine ratio in dogs is affected by the application of 2 commonly applied anticortisol antibodies was investigated. Free-catch morning urine samples of 50 healthy dogs were analyzed in duplicate with the use of 2 different polyclonal antibodies (antibody A and B) raised in different rabbits. Antibody A was raised against cortisol-3-carboxymethyl-oxime and antibody B against cortisol-21-hemisuccinate linked to BSA. Enzyme immunoassays were applied by using corresponding biotinylated labels. To examine possible cross-reactions with conjugated and nonconjugated cortisol metabolites, EIA measurements were performed with urine samples both before (directly assayed) and after diethyl-ether extraction, as well as after reversed-phase HPLC. Although the results correlated (P < 0.001), urinary corticoid concentrations and accordingly the urinary corticoid-to-creatinine ratios were 8 times higher when using antibody A than when using antibody B (mean ± SD corticoid concentrations, 223 ± 131 vs 29 ± 12 nmol/L; P < 0.001). Irrespective of the antibody used, extraction significantly decreased measured corticoid concentrations (antibody A, 158 ± 120 nmol/L; antibody B, 15 ± 8 nmol/L; P < 0.001), but the decrease was conspicuous when antibody A was used. Antibody A cross-reacted significantly with polar (eg, conjugated) metabolites, clearly depicted in the chromatogram by 3 additional peaks in earlier fractions well separated from cortisol. In contrast the assay that used antibody B was specific, showing only 1 major peak in the fractions eluting authentic cortisol. In summary, the study indicates that the configuration of the antibody considerably influences the analytic specificity of cortisol assays and underlines the pivotal importance of assay validation for each species and sample material.

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Multiple organ tumor tiss MOUSE ANTI BOVINE ROTAVIR HIV1 integrase antibody, Cortisol 3 antibody, Mono Cortisol antibody, Monocl Amplite™ Fluorimetric H Amplite™ Intracellular Amplite™ Fluorimetric P Amplite™ Fluorimetric A Goat Anti- TRPM8, (intern Goat Anti- TFAP2D, (inter Goat Anti- T1R3, (interna

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