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Search results for: Rabbit Anti-Iumbrokinase Polyclonal Antibody, Biotin Conjugated

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#35518307   2020/05/18 To Up

A signal-enhanced and sensitive lateral flow aptasensor for the rapid detection of PDGF-BB.

Platelet-derived growth factor BB (PDGF-BB) is a potential biomarker of tumor angiogenesis. For the first time, we developed a highly sensitive aptasensor for PDGF-BB with an enhanced test line signal by using two different gold nanoparticles (AuNPs). Herein, we describe a highly sensitive biosensor for PDGF-BB detection that combines biotinylated aptamer on a sample pad and poly thymine-Cy3-AuNP-monoclonal antibody complexes against PDGF-BB immobilized on conjugate pad A. Streptavidin (SA) and rabbit anti-mouse polyclonal antibody were also immobilized in the nitrocellulose membrane at the test and control zones, respectively. When the target PDGF-BB protein was added, it first bound the aptamer, and later the monoclonal antibody to form a biotinylated complex that was captured by SA, resulting in a visual red line on the test zone. In addition, to enhance the sensitivity, another monoclonal antibody against Cy3 was conjugated on AuNP B and immobilized on conjugate pad B to form a AuNPs (A&B)-antibody-(PDGF-BB-Cy3)-aptamer-biotin-SA complex on the test line when a loading buffer was subsequently added. This approach showed a linear response to PDGF-BB from 3 ng mL to 300 ng mL with a limit of detection as low as 1 ng mL obtained in 10 minutes. Our biosensor displayed results through red lines readable by the naked eye. Interestingly, our approach has been successfully applied for real sample verification, proving its applicability for cancer monitoring and diagnosis.
Na Cheng, Yujie Liu, Omar Mukama, Xiaobo Han, Hualin Huang, Shuai Li, Peng Zhou, Xuewen Lu, Zhiyuan Li

1713 related Products with: A signal-enhanced and sensitive lateral flow aptasensor for the rapid detection of PDGF-BB.

100ug Lyophilized100ug Lyophilized50 assays100tests96 tests1 kit100ug Lyophilized100 ul 100ul100ug Lyophilized

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#30800246   // To Up

Characterization of Monoclonal and Polyclonal Antibodies Recognizing Prostate Specific Antigen: Implication for Design of a Sandwich ELISA.

Prostate cancer is the second most common cancer in men. Prostate-Specific Antigen (PSA) is a tumor-associated glycoprotein with enzymatic activity which is secreted by the prostate gland. Following entry to the blood, 70-90% of PSA forms complexes with protease inhibitors and its enzymatic activity is inhibited. The serum level of PSA is increased and the rate of free PSA (fPSA) to total PSA is decreased in prostate cancer patients. Therefore, measurement of PSA and fPSA in serum is very valuable for diagnosis and prognosis of prostate cancer.
Sahar Raoofi Mohseni, Forough Golsaz-Shirazi, Mostafa Hosseini, Jalal Khoshnoodi, Tannaz Bahadori, Mohammad Ali Judaki, Mahmood Jeddi-Tehrani, Fazel Shokri

2425 related Products with: Characterization of Monoclonal and Polyclonal Antibodies Recognizing Prostate Specific Antigen: Implication for Design of a Sandwich ELISA.

0.2 mg1 kit(96 Wells) 6 ml Ready-to-use 100 0.1 ml 2 ml Ready-to-use 25 µg0.2 mg100 ug/vial100.00 ug0.25 mg1 mg

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#27600788   2016/09/04 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-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.
Lukáš Huml, Michal Jurášek, Petra Mikšátková, Tomáš Zimmermann, Pavla Tomanová, Miloš Buděšínský, Zdeňka Rottnerová, Markéta Šimková, Juraj Harmatha, Eva Kmoníčková, Oldřich Lapčík, Pavel B Drašar

2522 related Products with: Immunoassay for determination of trilobolide.

100Tests1 x 961 mg250 mg1x96 well plate100tests 1 G1 ml20 ug10 ml 125 ml

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#26248424   // To Up

[Establishment and evaluation of methods for determinating cystic fibrosis transmembrane conductance regulator quantitatively].

To establish and evaluate a BA-ELISA method for the quantitative detection of cystic fibrosis transmembrane conductance regulator (CFTR) protein.
Feng Qiu, Jie Zeng, Kun Li, Ai-jun Chen, Wan-xiang Xu, Ya Ni

2817 related Products with: [Establishment and evaluation of methods for determinating cystic fibrosis transmembrane conductance regulator quantitatively].

100ul25 mg0.1 mg5 mg100ug100ug Lyophilized96T100ul5 Modulators10 mg0.12 mL

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#24931549   2014/06/12 To Up

A heterogeneous biotin-streptavidin-amplified enzyme-linked immunosorbent assay for detecting tris(2,3-dibromopropyl) isocyanurate in natural samples.

Tris(2,3-dibromopropyl) isocyanurate (TBC) is a novel brominated flame retardant (BFR) that is widely used to substitute the prohibited BFRs throughout the world. With the development of research, the potential environmental and ecological harms of TBC have been revealed. For sensitive and selective detecting TBC, an indirect competitive biotin-streptavidin-amplified enzyme-linked immunosorbent assay (BA-ELISA) has been established in this study. The small molecular TBC-hapten was synthesized first; it mimicked the chemical structure of TBC and possessed a secondary amine group. The as-obtained hapten was then conjugated with carrier proteins to prepare artificial antigen. After immunization, the anti-TBC polyclonal antibody was obtained from separating rabbit serum. The procedures of this BA-ELISA were optimized. Under the optimal conditions, the limit of detection (IC10) was 0.0067 ng/ml and the median inhibitory concentration (IC50) was 0.66 ng/ml. Cross-reactivity values of the BA-ELISA with the tested TBC analogues were ⩽5%. This immunoassay was successfully applied to determine the TBC residue in river water samples that were collected near a BFR manufacturing plant. Satisfactory recoveries (92.1-109.2%) were obtained. The results indicated that this proposed BA-ELISA is suitable for the rapid and sensitive determining of TBC in environmental monitoring.
Dan Bu, Huisheng Zhuang, Xinchu Zhou, Guangxin Yang

1932 related Products with: A heterogeneous biotin-streptavidin-amplified enzyme-linked immunosorbent assay for detecting tris(2,3-dibromopropyl) isocyanurate in natural samples.

96 samples96 samples96 samples900 tests48 samples96 samples100ug100 assays16 Arrays/Slide100ug LyophilizedFor 2 miRNA probes, each

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#23000004   2012/09/19 To Up

Cysteine-terminated B-domain of Staphylococcus aureus protein A as a scaffold for targeting GABA(A) receptors.

This study reports the preparation and characterization of cysteine-terminated B-domain (Bd-cys) of Staphylococcus aureus protein A, in combination with immunoglobulin G (IgG) antibodies directed against the ρ1 and α1 subunits of GABA(A) receptors, for localizing reagents of interest to the target receptor. A cysteine residue was inserted at the C terminus of the cysteine-lacking B-domain (Bd) and used for conjugating maleimide-containing compounds. As determined by enzyme-linked immunosorbent assay (ELISA), binding of a Bd-cys-S-fluorescein conjugate to polyclonal guinea pig anti-GABA(A)-ρ1 and rabbit anti-GABA(A)-α1 IgG was similar to that exhibited by full-length protein A. Surface plasmon resonance analysis of the interaction of Bd-cys-S-PEG3400-biotin conjugate (where PEG is polyethylene glycol) with anti-GABA(A)-ρ1 and anti-GABA(A)-α1 yielded K(D) values of 6.4 ± 1.9 and 0.4 ± 0.1 nM, respectively. Fluorescence anisotropy analysis of the binding of Bd-cys-S-fluorescein to the two antibodies yielded EC50 values of 65 and 18 nM, respectively. As determined with biotin-reactive fluorescent reagents, Bd-cys-S-PEG3400-biotin specifically bound to the plasma membrane of Xenopus laevis oocytes that expressed α1β2γ2 or homomeric ρ1 GABA(A) receptors and were pretreated with the corresponding anti-GABA(A) IgG. The IgG-binding specificity and high affinity of Bd-cys conjugates illustrate the potential of these conjugates, in combination with a selected IgG, to localize compounds of interest at specific cell surface proteins.
Nasser M Qtaishat, Hélène A Gussin, David R Pepperberg

2168 related Products with: Cysteine-terminated B-domain of Staphylococcus aureus protein A as a scaffold for targeting GABA(A) receptors.

1000 assays100ug200 100μg50 ug 100 ml100μg96 Tests50 Test100ug

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#21406139   2011/03/16 To Up

Participation of the 39-kDa glycoprotein (gp39) of the vitelline envelope of Bufo arenarum eggs in sperm-egg interaction.

The acquisition of egg fertilizability in Bufo arenarum takes place during the oviductal transit and during this process the extracellular coelomic envelope (CE) of the eggs is converted into the vitelline envelope (VE). It has been stated that one of the necessary events leading to a fertilizable state is the proteolytic cleavage of CE glycoproteins in the oviductal pars recta by oviductin, a serine protease. Consequently, there is a marked increase in the relative quantity of glycoproteins with 39 (gp39) and 42 kDa (gp42) in the VE. In the present study, sperm-VE binding assays using heat-solubilized biotin-conjugated VE glycoproteins revealed that both gp39 and gp42 have sperm binding capacity. According to this result, our study was focused on gp39, a glycoprotein that we have previously reported as a homologue of mammalian ZPC. For this purpose, rabbit polyclonal antibodies against gp39 were generated at our laboratory. The specificity of the antibodies was confirmed with western blot of VE glycoproteins separated on SDS-PAGE. Immunohistochemical and immunoelectron studies showed gp39 distributed throughout the width of the VE. In addition, immunofluorescence assays probed that gp39 bound to the sperm head. Finally, as an approach to elucidate the possible involvement of gp39 in fertilization, inhibition assays showed that pretreatment of eggs with antibodies against gp39 generated a significant decrease in the fertilization rate. Therefore, our findings suggest that gp39, which is modified by oviductal action, participates as a VE glycoprotein ligand for sperm in Bufo arenarum fertilization.
Daniel Barrera, Ricardo J Llanos, Dora C Miceli

2901 related Products with: Participation of the 39-kDa glycoprotein (gp39) of the vitelline envelope of Bufo arenarum eggs in sperm-egg interaction.

5 G11 Set1 Set

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