Search results for: Rabbit Anti-Phospho-SIRT1(Ser47) Polyclonal Antibody, HRP Conjugated
#37167766 2023/05/08 To Up
Quantitation of total antibody (tAb) from antibody drug conjugate (ADC) PYX-201 in rat and monkey plasma using an enzyme-linked immunosorbent assay (ELISA) and its application in preclinical studies.
PYX-201 is an investigative ADC oncology drug composed of a monoclonal human immunoglobulin G (IgG) antibody targeting the extra domain B splice variant of fibronectin (EDB + FN) conjugated to an auristatin payload through a cleavable linker. Effective measurement of PYX-201 tAb is the key to ADC drug PYX-201 preclinical pharmacokinetics (PK) assessment. PYX-201 monoclonal antibody (mAb) was used as the reference standard, goat anti-human IgG polyclonal antibody (pAb) or rabbit anti-human Kappa light chain mAb was employed as the capture antibody, and mouse mAb or goat pAb anti-human IgG the crystallizable fragment (Fc) (horseradish peroxidase (HRP)) was utilized as the detection antibody in this ELISA. This assay was validated with a dynamic range 250 - 10,000 ng/mL and 250 - 6000 ng/mL in rat and monkey KEDTA plasma, respectively. PYX-201 tAb bioanalytical ELISA assay was reported for the first time in any biological matrix. This is the first time for a bioanalytical method to be validated for a tAb from an ADC drug targeting EDB + FN in any biological matrix.Feng Yin, Chris DeCiantis, Jan Pinkas, Biplab Das, Frank Wang, Nancy Zheng, David Hahn, Aniruddha Amrite, Jianwen Feng, Diana Adhikari, Cheikh Kane, Jack Sikora, Justin Pittman, Rebecca Wates, Elizabeth Shaheen, Shawn Harriman
2933 related Products with: Quantitation of total antibody (tAb) from antibody drug conjugate (ADC) PYX-201 in rat and monkey plasma using an enzyme-linked immunosorbent assay (ELISA) and its application in preclinical studies.
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#35142129 // To Up
[Development of a double-antibody sandwich ELISA targeting the receptor binding domain of TcdB toxin of ST11 type of porcine origin].
is an important zoonotic intestinal pathogen, which is widely present in humans and a variety of animals. The ST11 type is one of the most widespread and harmful subtypes in the world. As a large country in pig farming, China lacks efficient methods for detecting of porcine origin, leaving hidden dangers for the prevention and control of . The aim of this study was to develop a specific and sensitive double-antibody sandwich ELISA for the epidemiological investigation of ST11 type of porcine origin. Firstly, a 97 kDa receptor binding domain (RBD) was expressed in a prokaryotic host and purified. A hybridoma cell line AE2D3 capable of stably secreting monoclonal antibody targeting the RBD was screened, and the antibody subtype was determined to be IgG2b (κ). Secondly, a double antibody sandwich ELISA method was developed, where the monoclonal antibody targeting the RBD was used as a detection antibody, and the rabbit polyclonal antibody was used as a capture antibody. The chessboard method was used to determine the matching concentration of the capture antibody and the detection antibody, the antigen coating conditions, the blocking conditions, the incubation conditions for detection antibody and samples to be tested, as well as the reaction conditions of HRP-conjugated and reaction conditions of TMB chromogenic solution. The negative cutoff was 0.152, and no cross-reaction with 13 strains of non-ST11 type was found. The minimum detection concentration of RBD was 8.83 ng/mL. This specific and sensitive double-antibody sandwich ELISA provides a reliable serological detection method for epidemiological investigation of the ST11 type in pig industry.Wei Liang, Keji Quan, Qin Zhao, Yaomin Wu, Yu Mu, Sanjie Cao
2864 related Products with: [Development of a double-antibody sandwich ELISA targeting the receptor binding domain of TcdB toxin of ST11 type of porcine origin].
50μl96tests96T 5 G100ug Lyophilized100ulRelated Pathways
#33968077 2021/04/23 To Up
A Double-Antibody Sandwich ELISA for Sensitive and Specific Detection of Swine Fibrinogen-Like Protein 1.
Fibrinogen-like protein 1 (FGL1), a member of the fibrinogen family, is a specific hepatocyte mitogen. Recently, it has been reported that FGL1 is the main inhibitory ligand of lymphocyte activating gene 3 (LAG3). Furthermore, the FGL1-LAG3 pathway has a synergistic effect with programmed death 1 (PD-1)/programmed death ligand 1 (PD-L1) pathway and is regarded as a promising immunotherapeutic target. However, swine FGL1 (sFGL1) has not been characterized and its detection method is lacking. In the study, the sFGL1 gene was amplified from the liver tissue of swine and then inserted into a prokaryotic expression vector, pQE-30. The recombinant plasmid pQE30-sFGL1 was transformed into JM109 competent cells. The recombinant sFGL1 was induced expression by isopropyl-β-d-thiogalactoside (IPTG) and the purified sFGL1 was used as an antigen to produce mouse monoclonal antibody (mAb) and rabbit polyclonal antibody (pAb). After identification, a double-antibody sandwich enzyme-linked immunosorbent assay (DAS-ELISA) for sensitive and specific detection of sFGL1 was developed. Swine FGL1 in samples was captured by anti-sFGL1 mAb followed by detection with anti-sFGL1 rabbit pAb and HRP-conjugated goat anti-rabbit IgG. The limit of detection of the developed sFLG1-DAS-ELISA is 35 pg/ml with recombinant sFLG1. Besides, it does not show cross-reactivity with the control protein. Then serum samples of PRRSV-negative and -positive pigs were tested with the established DAS-ELISA and calculated according to the equation of y=0.0735x+0.0737. The results showed that PRRSV infection enhanced the serum FGL1 levels significantly. Our research provides a platform for the research on the functional roles of swine FGL1.Xin Zhang, Haipeng Zhu, Xu Zheng, Yunjie Jiao, Lulu Ning, En-Min Zhou, Yang Mu
2556 related Products with: A Double-Antibody Sandwich ELISA for Sensitive and Specific Detection of Swine Fibrinogen-Like Protein 1.
1 kit0.1 mg25 µg100ug Lyophilized100 ml100 TESTS100ug100μg100ug Lyophilized0.1 ml0.1 mg96 testsRelated Pathways
#32822033 // To Up
Immunohistochemical Detection of 5-Hydroxymethylcytosine and 5-Carboxylcytosine in Sections of Zebrafish Embryos.
5-methylcytosine (5mC) is an epigenetic modification to DNA which modulates transcription. 5mC can be sequentially oxidized to 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Collectively, these marks are referred to as the oxidized derivatives of 5mC (i.e., oxi-mCs). Their formation is catalyzed by the ten-eleven translocation methylcytosine dioxygenases (TETs 1, 2 and 3). Various techniques have been developed for the detection of oxi-mCs. The following chapter describes an immunochemical protocol for the simultaneous detection of 5hmC and 5caC in embryonic zebrafish tissue sections. The embryos are fixed, permeabilized and embedded in paraffin blocks. The blocks are cut into sections that are mounted onto slides. Depurination of the DNA is performed to allow immunodetection of the oxi-mCs. The 5hmC is detected with the help of a mouse anti-5hmC monoclonal primary antibody and a goat anti-mouse Alexa Fluor 633-conjugated secondary antibody. The weak 5caC signal requires enzymatic amplification. Its detection involves a rabbit anti-5caC polyclonal primary antibody and a goat anti-rabbit secondary antibody that is conjugated to horseradish peroxidase (HRP). HRP amplifies the 5caC signal by catalyzing the deposition of large quantities of fluorescein-labeled tyramide. Sections immunostained for 5hmC and 5caC are analyzed by fluorescent light or confocal laser scanning microscopy. This immunochemical method allows for highly sensitive detection of 5hmC and 5caC in zebrafish tissues.Peter Jessop, Martin Gering
1618 related Products with: Immunohistochemical Detection of 5-Hydroxymethylcytosine and 5-Carboxylcytosine in Sections of Zebrafish Embryos.
100 μg100 μg100 μgRelated Pathways
#32762697 2020/08/06 To Up
Evaluation of an in-house indirect enzyme-linked immunosorbent assay of feline panleukopenia VP2 subunit antigen in comparison to hemagglutination inhibition assay to monitor tiger antibody levels by Bayesian approach.
Feline panleukopenia virus (FPV) is an etiologic pathogen of feline panleukopenia that infects all members of Felidae including tigers (Panthera tigris). Vaccinations against FPV among wild felid species have long been practiced in zoos worldwide. However, few studies have assessed the tiger immune response post-vaccination due to the absence of a serological diagnostic tool. To address these limitations, this study aimed to develop an in-house indirect enzyme-linked immunosorbent assay (ELISA) for the monitoring of tiger antibody levels against the feline panleukopenia vaccine by employing the synthesized subunit capsid protein VP2. An in-house horseradish peroxidase (HRP) conjugated rabbit anti-tiger immunoglobulin G (IgG) polyclonal antibody (HRP-anti-tiger IgG) was produced in this study and employed in the assay. It was then compared to a commercial HRP-conjugated goat anti-cat IgG (HRP-anti-cat IgG). Sensitivity and specificity were evaluated using the Bayesian model with preferential conditional dependence between HRP-conjugated antibody-based ELISAs and hemagglutination-inhibition (HI) tests.Chanakan Areewong, Amarin Rittipornlertrak, Boondarika Nambooppha, Itsarapan Fhaikrue, Tawatchai Singhla, Chollada Sodarat, Worapat Prachasilchai, Preeyanat Vongchan, Nattawooti Sthitmatee
2871 related Products with: Evaluation of an in-house indirect enzyme-linked immunosorbent assay of feline panleukopenia VP2 subunit antigen in comparison to hemagglutination inhibition assay to monitor tiger antibody levels by Bayesian approach.
1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)1 kit(96 Wells)Related Pathways
#31737229 2019/09/15 To Up
Development and characterization of polyclonal antibody against human kappa light chain in rabbit.
Polyclonal antibodies against kappa light chain are used to diagnose diseases producing free light chain. The kappa and lambda light chains are products of immunoglobulin synthesis and released into the circulation in minor amounts such as serum, cerebrospinal fluid, urine and synovial fluid in normal condition. The purpose of this study was the production and purification of polyclonal immunoglobulin G (IgG) against human kappa light chains. In this study, early human IgG was purified by ion-exchange chromatography, reduced with Dithiothreitol and heavy and light chains were separated with size-exclusion chromatography. Afterward, affinity chromatography with protein L Sepharose at pH 2.00 was displayed to be a dominant condition for the separation and purification of the kappa light chain of immunoglobulins from human serum. Eventually, the rabbit was immunized by human kappa light chains. The rabbit IgG was purified and labeled with horseradish peroxidase (HRP). Direct enzyme-linked immunosorbent assay was planned to determine the titer of HRP conjugated rabbit IgG against the human kappa light chain. The optimum titer of anti-kappa IgG was 1:16000. At the result, purified polyclonal anti-kappa is useful tool in biomedical and biochemical researches and diagnostic kits.Mojgan Esparvarinha, Hamid Nickho, Leili Aghebati-Maleki, Jalal Abdolalizadeh, Hadi Nasiri, Zahra Valedkarimi, Jafar Majidi
2874 related Products with: Development and characterization of polyclonal antibody against human kappa light chain in rabbit.
0.05 mg100 ug 100ug1 ml100ug Lyophilized100ug Lyophilized50 ug 100ug Lyophilized6 ml100ug Lyophilized100ug Lyophilized100ug LyophilizedRelated Pathways
#31621104 2019/11/14 To Up
Development of a double-antibody sandwich ELISA for sensitive detection of Yersinia pestis.
We developed a biotin-streptavidin-based sandwich ELISA for the sensitive and specific detection of Yersinia pestis. In this assay, the F1 capsular protein and Y. pestis were captured by anti-F1 mouse monoclonal antibody followed by detection with biotinylated-anti-F1 rabbit polyclonal antibody and HRP-conjugated streptavidin. The developed F1 ELISA could detect not only the F1 protein up to 29 and 17 pg/ml but also Y. pestis up to 177.8 and 129.2 CFU/ml in PBS buffer and human serum, respectively. In addition, the F1 ELISA did not show any cross-reactivity with various proteins and bacterial strains.Sang-Yoon Choi, Gi-Eun Rhie, Jun Ho Jeon
1570 related Products with: Development of a double-antibody sandwich ELISA for sensitive detection of Yersinia pestis.
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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
1267 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 2 ml Ready-to-use 100 0.1 ml25 µg0.2 mg100 ug/vial100.00 ug0.25 mg1 mgRelated Pathways
#30612650 2018/10/21 To Up
Ultrasensitive immunosensor for acrylamide based on chitosan/SnO-SiC hollow sphere nanochains/gold nanomaterial as signal amplification.
An electrochemical immunosensor for ultrasensitive detection of acrylamide (AA) in water and food samples was developed. SnO-SiC hollow sphere nanochains with high surface area and gold nanoparticles with good electroconductivity were fabricated onto the surface of a glassy carbon electrode pre-coated with chitosan. The coating antigen (AA-4-mercaptophenylacetic acid-ovalbumin conjugate, AA-4-MPA-OVA) was immobilized on the electrode. Polyclonal antibody specific for AA-4-MPA was conjugated to gold nanorod (AuNR) as primary antibody (AuNR-Ab). Horseradish peroxidase labelled anti-rabbit antibody produced in goat was conjugated to AuNR as secondary antibody (HRP-AuNR-Ab). For detection, the analyte (AA-4-MPA) in sample competed with coating antigen for binding with AuNR-Ab. After washing, HRP-AuNR-Ab was added to capture the AuNR-Ab, and the electrical signal was obtained by addition of hydroquinone and HO. After investigation of the binding ability on nanomaterials and optimization of competitive immunoassay conditions, the proposed immunosensor exhibited a sensitive response to AA with a detection limit of 45.9 ± 2.7 ng kg, and working range of 187 ± 12.3 ng kg to 104 ± 8.2 μg kg for drinking water samples. Recoveries of AA from spiked samples were ranged from 86.0% to 115.0%. The specificity, repeatability and stability of the immunosensor were also proved to be acceptable, indicating its potential application in AA monitoring.Min-Fu Wu, Yu Wang, Sha Li, Xiu-Xiu Dong, Jin-Yi Yang, Yu-Dong Shen, Hong Wang, Yuan-Ming Sun, Hong-Tao Lei, Zhen-Lin Xu
1742 related Products with: Ultrasensitive immunosensor for acrylamide based on chitosan/SnO-SiC hollow sphere nanochains/gold nanomaterial as signal amplification.
500 tests96 Tests1 Bag of 1000 Caps/Unit x100tests1,000 tests50 assays100ug Lyophilized100TestsRelated Pathways
#29719659 2018/03/15 To Up
A methodological approach for production and purification of polyclonal antibody against dog IgG.
Antibodies are a class of biomolecules that has an important role in the immune system and lots of applications in biotechnological methods and in pharmaceutics. Production and purification of antibodies in laboratory animals is one of the first ways to manufacture of these prominent tools. The obtained antibodies from these process could be used in various types of bioassay techniques such as enzyme linked immunosorbent assay (ELISA), radioimmunoassay, etc. Also, antibodies employed in diagnostics applications in humans and other animals in order to detect specific antigens. In this study, we aimed to produce and purify anti-dog IgG via immunizing rabbits with dog IgG in combination with Freund's adjuvant. Polyclonal IgG were purified by ion exchange chromatography and then the purified antibody was labeled with horse radish peroxidase (HPR). Direct ELISA was used to determine the optimum titer and cross-reactivity of HRP conjugated IgG. The purity of various IgG preparations and the optimum dilution of prepared HRP conjugated IgG, respectively, was about 95.00% and 1:8000. This study showed that efficiency ion-exchange chromatography could be an appropriate method for purification of IgG antibodies. This antibody could be a useful tool for future dog immune diagnosis tests. This product characterization shown here sets the foundations for future work on dog IgGs.Somayeh Sadeghi, Leili Aghebati-Maleki, Samira Nozari, Jafar Majidi
1786 related Products with: A methodological approach for production and purification of polyclonal antibody against dog IgG.
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