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Search results for: Rabbit Anti-IFI35 Polyclonal Antibody

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#38420990   2024/02/29 To Up

Association of the combined parameters including the frequency of primary cilia, PD-L1, Smoothened protein, membranous β-catenin and cytoplasmic β-catenin expression with the outcome of patients with clear cell renal cell carcinoma.

The objective of this study was to investigate the association and combined prognostic significance of the PD-L1, Smoothened protein and β-catenin expressions in patients with clear cell renal cell carcinoma (ccRCC).
Aneta Rozsypalova, Blanka Rosova, Alzbeta Filipova, Dimitar Hadzi Nikolov, Renata Chloupkova, Igor Richter, Roman Zachoval, Radoslav Matej, Bohuslav Melichar, Tomas Buchler, Josef Dvorak

1583 related Products with: Association of the combined parameters including the frequency of primary cilia, PD-L1, Smoothened protein, membranous β-catenin and cytoplasmic β-catenin expression with the outcome of patients with clear cell renal cell carcinoma.

24 reactions 100 U

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#38420701   2024/02/29 To Up

Evaluation of species-specific polyclonal antibodies to detect and differentiate between and .

Neosporosis and toxoplasmosis are major causes of abortion in livestock worldwide, leading to substantial economic losses. Detection tools are fundamental to the diagnosis and management of those diseases. Current immunohistochemistry (IHC) tests, using sera raised against whole parasite lysates, have not been able to distinguish between and We used and recombinant proteins, expressed in and purified using insoluble conditions, to produce specific polyclonal rabbit antisera. We aimed to develop species-specific sera that could be used in IHC on formalin-fixed, paraffin-embedded (FFPE) tissue sections to improve the diagnosis of ruminant abortions caused by protozoa. Two polyclonal rabbit sera, raised against recombinant proteins, anti--rNcSRS2 and anti--rTgSRS2, had specificity for the parasite they were raised against. We tested the specificity for each polyclonal serum using FFPE tissue sections known to be infected with and . The anti--rNcSRS2 serum labeled specifically only infected tissue blocks, and the anti--rTgSRS2 serum was specific to only infected tissues. Moreover, tissues from 52 cattle and 19 sheep previously diagnosed by lesion profiles were tested using IHC with our polyclonal sera and PCR. The overall agreement between IHC and PCR was 90.1% for both polyclonal anti-rNcSRS2 and anti-rTgSRS2 sera. The polyclonal antisera were specific and allowed visual confirmation of protozoan parasites by IHC, but they were not as sensitive as PCR testing.
Tanja Lepore, Alastair I Macrae, Germán J Cantón, Carlo Cantile, Henny M Martineau, Javier Palarea-Albaladejo, Stephen Cahalan, Clare Underwood, Frank Katzer, Francesca Chianini

1816 related Products with: Evaluation of species-specific polyclonal antibodies to detect and differentiate between and .

50 ug 50 ug 50 ug 0.1 mg96T1 ml0.1 ml200ul1000 TESTS/0.65ml50 ug 50 ug 50 ug

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#38385694   2024/02/22 To Up

Discovery of Two Novel Immunoepitopes and Development of Peptide-based Sarcoidosis Immunoassay.

Sarcoidosis is a systemic granulomatous disorder associated with hypergammaglobulinemia and the presence of autoantibodies. The specific antigens initiating granulomatous inflammation in sarcoidosis are unknown and there is no specific test available to diagnose sarcoidosis. To discover novel sarcoidosis antigens, we developed a high-throughput T7 phage display library derived from the sarcoidosis cDNA and identified numerous clones differentiating sarcoidosis from other respiratory diseases. After clone sequencing and homology search, we identified two epitopes (Cofilinμ and Chain A) that specifically bind to serum IgGs of sarcoidosis patients.
Changya Peng, Jaya Talreja, Brennen Steinbauer, Kazuhiko Shinki, Laura L Koth, Lobelia Samavati

1819 related Products with: Discovery of Two Novel Immunoepitopes and Development of Peptide-based Sarcoidosis Immunoassay.

5 G50 ug50 ug100ug Lyophilized200ul50 ug50 ug50 ug50 ug50

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#38366109   2024/02/16 To Up

Development of Polyclonal Antibodies-Based Serological Method for the Detection of Calanthe Mild Mosaic Virus and Application in Virus Certification Programme.

Calanthe mild mosaic virus (CalMMV) infecting orchids is an important potyvirus which is known to cause mild leaf mosaic and flower colour-breaking symptoms in Calanthe and other orchid plants. The present study reports the production of polyclonal antibodies against CalMMV using bacterially expressed recombinant coat protein as immunogen, which in turn would be useful in routine indexing and screening of orchid germplasm. The coat protein (CP) gene (~ 807 bp) of CalMMV isolated from infected orchid sample was cloned in expression vector, pET-28a ( +) that yielded ~ 31 kDa fusion protein with Histidine tag (HisBP). The expression of fusion CP was confirmed through SDS-PAGE and Western blotting. The HisBP-CalMMV-CP obtained in soluble state after purification was used to immunize New Zealand white rabbit for the production of polyclonal antibodies (PAb). The PAb produced against the purified fusion protein successfully detected CAlMMV in the orchid samples at a dilution of 1:2000 in direct antigen-coated enzyme-linked immunosorbent assay (DAC-ELISA). This study presents the first report of Histidine tag (HisBP) fusion CalMMV-CP-based antibody production and its successful application in the identification of the virus in orchid plants. Outcome of this study will be helpful in routine certification programmes, screening of orchid germplasm and production of CalMMV-free planting materials of orchids.
Nishant Srivastava, Rakesh Kumar, Reetika Kapoor, Ashwini Kumar, Susheel K Sharma, Nitika Gupta, Pooja Bhardwaj, Gopi Kishan, Rajendra P Pant, Virendra K Baranwal

1349 related Products with: Development of Polyclonal Antibodies-Based Serological Method for the Detection of Calanthe Mild Mosaic Virus and Application in Virus Certification Programme.

1 mL100 200 100 100 1 mL500 1 mg100 1 mL100 1 mg

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#38344705   2023/07/01 To Up

Cloning, Prokaryotic Expression and Functional Characterization of Gene from the Associative Nitrogen-Fixing Bacteria DX120E.

Biological nitrogen fixation (BNF) is a unique mechanism in which microorganisms utilize the nitrogenase enzyme to catalyze the conversion of atmospheric nitrogen (N) to ammonia (NH). Fe protein, encoded by the gene, is an essential component of the nitrogenase in DX120E. However, the function of this gene in regulating nitrogen fixing activity is still unclear.
Ying Qin, Yu-Yan Huang, Qaisar Khan, Kun-Kun Zhang, Dao-Jun Guo, Li-Tao Yang, Yang-Rui Li, Yong-Xiu Xing

1584 related Products with: Cloning, Prokaryotic Expression and Functional Characterization of Gene from the Associative Nitrogen-Fixing Bacteria DX120E.

5 μg4

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#38336093   2024/02/07 To Up

Eimeria tenella pyrroline -5-carboxylate reductase is a secreted protein and involved in host cell invasion.

Chicken coccidiosis, which caused by Eimeria spp, is a parasitic protozoal disease. At present, control measures of this disease depend mainly on anticoccidial drugs and live vaccines. But these control strategies have drawbacks such as drug resistance and limitations in live vaccines production. Therefore, novel control approaches are urgently need to study to control this disease effectively. In this study, the function and characteristics of the pyrroline-5-carboxylate reductase of Eimeria tenella (EtPYCR) protein were preliminary analyzed. The transcription and translation level were analyzed by using qPCR and Western blot. The results showed that the mRNA transcription and translation levels of EtPYCR were higher in unsporulated oocysts (UO) and second generation merozoites (Mrz) than that in sporulated oocysts (SO) and sporozoites. Enzyme activity showed that the enzyme activity of EtPYCR was also higher in the UO and Mrz than that in the SO and sporozoites. Immunofluorescence localization showed EtPYCR was mainly located on the top of sporozoites and the whole cytoplasm and surface of Mrz. The secretion assay indicated that EtPYCR was secretion protein, but not from micronemes. Invasion inhibition assay showed that rabbit anti-rEtPYCR polyclonal antibodies can effectively inhibit sporozoite invasion of DF-1 cells. These results showed that EtPYCR possess several important roles that separate and distinct from its conversion 1-pyrroline-5-carboxylate (P5C) into proline and maybe involved in the host cell invasion and development of parasites in host cells.
Shanshan Liang, Shunhai Zhu, Qingjie Wang, Qiping Zhao, Hui Dong, Bing Huang, Yu Yu, Hongyu Han

2032 related Products with: Eimeria tenella pyrroline -5-carboxylate reductase is a secreted protein and involved in host cell invasion.

100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized

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#38308826   // To Up

A non-toxic recombinant protein rSUMO-CPBm4 as a potential vaccine candidate against Clostridium perfringens type C beta enterotoxemia.

Beta toxin (CPB) is a lethal toxin and plays a key role in enterotoxemia of ruminants caused by Clostridium perfringens type C strain. The existing vaccines based on crude CPB need time-consuming detoxification and difficult quality control steps. In this study, we synthesized the rCPB of C. perfringens type C strain and small ubiquitin-like modifier (SUMO)-tag CPB (rSUMO-CPB) by introducing four amino acid substitutions: R212E, Y266A, L268G, and W275A. Compared with rCPB, rSUMO-CPB was expressed with higher solubility in Escherichia coli BL21 (DE3). Neither rCPB nor rSUMO-CPB was lethal to mice. Although rCPB and rSUMO-CPB were reactogenic with polyclonal antibodies against crude CPB, rabbits vaccinated with rSUMO-CPB developed significant levels of toxin-neutralizing antibody (TNA) titers that conferred protection against crude toxin challenge. These data suggest that genetically detoxified rSUMO-CPB is a promising subunit vaccine candidate for C. perfringens type C beta enterotoxemia.
Y Goa, J G Du, C Jirapattharasate, E Galon, S W Ji, Z G Ran, Y Q Xia

1214 related Products with: A non-toxic recombinant protein rSUMO-CPBm4 as a potential vaccine candidate against Clostridium perfringens type C beta enterotoxemia.

1mg96T101 kit10 200

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