Search results for: Rabbit Anti-Desmuslin Polyclonal Antibody
#33671430 
2021/02/17
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Developing a Vaccine to Block West Nile Virus Transmission: In Silico Studies, Molecular Characterization, Expression, and Blocking Activity of mosGCTL-1.
Mosquito galactose-specific C-type lectins (mosGCTLs), such as mosGCTL-1, act as ligands to facilitate the invasion of flaviviruses like West Nile virus (WNV). WNV interacts with the of (Culicidae) and facilitates the invasion of this virus. Nevertheless, there is no data about the role of mosGCTL-1 as a transmission-blocking vaccine candidate in , the most abundant Culicinae mosquito in temperate regions.Hasan Bakhshi, Mehdi Fazlalipour, Javad Dadgar-Pakdel, Sedigheh Zakeri, Abbasali Raz, Anna-Bella Failloux, Navid Dinparast Djadid
1873 related Products with: Developing a Vaccine to Block West Nile Virus Transmission: In Silico Studies, Molecular Characterization, Expression, and Blocking Activity of mosGCTL-1.
100 µg1 kit50 ug1 kit100 100 ug/vial50 ug50 ug50 ug50 ug50 ug
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#33670728 2021/02/18
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Surface Exposed GroEL Is a Multifunctional Protein.
The spirochete, , has a large number of membrane proteins involved in a complex life cycle, that includes a tick vector and a vertebrate host. Some of these proteins also serve different roles in infection and dissemination of the spirochete in the mammalian host. In this spirochete, a number of proteins have been associated with binding to plasminogen or components of the extracellular matrix, which is important for tissue colonization and dissemination. GroEL is a cytoplasmic chaperone protein that has previously been associated with the outer membrane of A His-tag purified GroEL was used to generate a polyclonal rabbit antibody showing that GroEL also localizes in the outer membrane and is surface exposed. GroEL binds plasminogen in a lysine dependent manner. GroEL may be part of the protein repertoire that successfully uses to establish infection and disseminate in the host. Importantly, this chaperone is readily recognized by sera from experimentally infected mice and rabbits. In summary, GroEL is an immunogenic protein that in addition to its chaperon role it may contribute to pathogenesis of the spirochete by binding to plasminogen and components of the extra cellular matrix.Thomas Cafiero, Alvaro Toledo
1530 related Products with: Surface Exposed GroEL Is a Multifunctional Protein.
100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized
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#33636533 2021/02/20
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Adulteration of cow's milk with buffalo's milk detected by an on-site carbon nanoparticles-based lateral flow immunoassay.
A competitive lateral flow immunoassay using amorphous carbon nanoparticles (CNPs) and non-immunoglobulin antigen has been developed for the rapid detection of adulteration of cow's milk with buffalo's milk. Purified polyclonal antibodies against a specific buffalo's milk protein fraction were conjugated to CNPs and sprayed on a conjugate pad. The test line consisted of buffalo's skimmed milk proteins (1.6 μg/cm), while the control line contained anti-rabbit antibodies raised in goat (0.5 μg/cm). In the test procedure milk sample is mixed with 100 mM borate buffer (pH 8.8 containing 1% BSA and 0.05% Tween 20) and pipetted onto the sample-cum-conjugate pad. A black/grey test line can be observed if the sample is free from buffalo's milk. The sensitivity of the test i.e. no visible test line is 5% adulteration of cow's milk with buffalo's milk. The test has applicability at the milk receiving stations and can be applied to heated milk samples.Rajan Sharma, Archana Verma, Nitin Shinde, Bimlesh Mann, Kamal Gandhi, Jan H Wichers, Aart van Amerongen
1299 related Products with: Adulteration of cow's milk with buffalo's milk detected by an on-site carbon nanoparticles-based lateral flow immunoassay.
100ug Lyophilized100μg100ug Lyophilized1 kit(96 Wells)100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug100ug Lyophilized100ug Lyophilized
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#33629311 //
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The detection of SAS1B in serum provides clues for early diagnosis of thyroid cancer.
The incidence of thyroid cancer is rising globally. Most patients progress slowly, but some patients develop lymph node and distant metastasis earlier, and their prognosis is poor. Therefore, early diagnosis and warning of malignancy are very meaningful for such patients. SAS1B gene is a newly discovered protein expressed on the surface of mature egg cells and has metalloendopeptidase activity. We aimed at exploring whether SAS1B is involved in the occurrence of thyroid cancer, and at providing evidence for early diagnosis and targeted therapy of thyroid cancer.H-X Yang, Y Yang, X-D Li, X-M Miao, C Yang, D-F Zhi, H Su, G Yang, J Gao, C-G Du, H-J Li, Y-L Song, G-F Cao
1051 related Products with: The detection of SAS1B in serum provides clues for early diagnosis of thyroid cancer.
Each2x96 well plate
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#33610651 2021/02/18
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Avidin-Biotin recombinant antigen capture ELISA for the detection of peste des petits ruminants virus in the clinical specimens of sheep and goats.
This study describes the development of Avidin-Biotin recombinant Antigen Capture ELISA (ABrAC ELISA) for the detection of the peste des petits ruminants virus (PPRV) antigens in the clinical specimens of sheep and goats. The assay uses the truncated recombinant PPRV N-terminal immunogenic region of nucleoprotein (rPPRV-NPN) as a reference positive antigen and its polyclonal antibodies as capture/detective antibodies and the rabbit PPRV polyclonal antibodies as coating antibodies. The cut-off value was determined as double times the mean reactivity of blank control based on the reactivity of the PPR confirmed negative and positive control panel samples. On assessing the specificity with the related differential diagnosis of the disease-causing viruses and bacteria, the assay showed specific detective reactivity to PPRV. Further, on evaluation using clinical specimens (n-274) of sheep and goats, the assay showed that the relative diagnostic sensitivity of 86.49 % (95 % confidence interval (CI): 71.23-95.46 %) and diagnostic specificity of 96.20 % (95 % CI: 92.91-98.25 %) against PPRV nucleoprotein-specific monoclonal antibody-based sandwich-ELISA (PPR s-ELISA) kit, with an accuracy of 94.89 % (95 % CI: 91.58-97.18 %) and Cohen's Kappa value of 0.791 + 0.055 SE (95 % CI: 0.68-0.90) with substantial agreements. The ABrAC-ELISA is an alternative method of an immunoassay for the rapid, sensitive, and specific detection of the PPRV antigens m the clinical specimens of sheep and goats for surveillance or diagnosis of PPR. This study also shows that the rPPRV-NPN and its specific polyclonal antibodies could be the sustainable source of safe diagnostic reagents without the need to handle the infectious virus during the eradication and post-eradication phases in endemic countries like India or PPR non-endemic countries.V Balamurugan, Bibitha Varghese, S Sowjanya Kumari, K Vinod Kumar, D Muthuchelvan, M Nagalingam, Parimal Roy
2920 related Products with: Avidin-Biotin recombinant antigen capture ELISA for the detection of peste des petits ruminants virus in the clinical specimens of sheep and goats.
1100 296 tests100 25 ml50ml100 µg2 100 µg96 tests
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#33606748 2021/02/19
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Immunohistochemical identification of complement peptide C5a receptor 1 (C5aR1) in non-neoplastic and neoplastic human tissues.
The complement component C5a and its receptor C5aR1 are involved in the development of numerous inflammatory diseases. In addition to immune cells, C5aR1 is expressed in neoplastic cells of multiple tumour entities, where C5aR1 is associated with a higher proliferation rate, advanced tumour stage, and poor patient outcomes. The aim of the present study was to obtain a broad expression profile of C5aR1 in human non-neoplastic and neoplastic tissues, especially in tumour entities not investigated in this respect so far. For this purpose, we generated a novel polyclonal rabbit antibody, {5227}, against the carboxy-terminal tail of C5aR1. The antibody was initially characterised in Western blot analyses and immunocytochemistry using transfected human embryonic kidney (HEK) 293 cells. It was then applied to a large series of formalin-fixed, paraffin-embedded non-neoplastic and neoplastic human tissue samples. C5aR1 was strongly expressed by different types of immune cells in the majority of tissue samples investigated. C5aR1 was also present in alveolar macrophages, bronchial, gut, and bile duct epithelia, Kupffer cells, occasionally in hepatocytes, proximal renal tubule cells, placental syncytiotrophoblasts, and distinct stem cell populations of bone marrow. C5aR1 was also highly expressed in the vast majority of the 32 tumour entities investigated, where a hitherto unappreciated high prevalence of the receptor was detected in thyroid carcinomas, small-cell lung cancer, gastrointestinal stromal tumours, and endometrial carcinomas. In addition to confirming published findings, we found noticeable C5aR1 expression in many tumour entities for the first time. Here, it may serve as an interesting target for future therapies.Benjamin Nürge, Alan Lennart Schulz, Daniel Kaemmerer, Jörg Sänger, Katja Evert, Stefan Schulz, Amelie Lupp
2828 related Products with: Immunohistochemical identification of complement peptide C5a receptor 1 (C5aR1) in non-neoplastic and neoplastic human tissues.
1000 20 100ul 100ul 100ul200ul100ug100ug Lyophilized96 wells (1 kit) 100ul100 μg100ug
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#33592264 2021/02/13
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Epitope-based in silico peptide design yields peptide-directed antibodies that recognize the buffalo luteinizing hormone.
We present a novel peptide sequence identified through in silico epitope design and the later generation of peptide-directed antibodies recognizing the buffalo luteinizing hormone. Peptides and antibodies, specific to reproductive hormones, are valuable tools for developing point-of-care immunodiagnostic tools. The study predicted an epitope peptide in silico from buffalo luteinizing hormone and the generation of polyclonal antibodies against this peptide sequence. In this quest, we identified a novel epitope peptide sequence (luteinizing hormone peptide, LHP) through bioinformatics tools. The peptide was further synthesized and characterized. The polyclonal antibodies (anti-LHP) were raised against the peptide in the rabbit. Thereafter, we explored a strategy for detecting buffalo luteinizing hormone (LH) using the anti-peptide antibodies developed. The affinity of the peptide, bovine lutropin beta, and crude LH (prepared from buffalo pituitary) towards the raised antibodies was established by dot blot and ELISA. Specific recognition of the luteinizing hormone by the raised polyclonal antibodies highlights the ability of the identified peptide (LHP) and developed polyclonal antibodies (anti-LHP) as suitable diagnostic reagents for sensing the buffalo luteinizing hormone. Through this work, we analyzed and translated the "-omics" information in the LH gene sequence for the development of a novel peptide and antibodies as valuable immuno-reagents.Varij Nayan, Suneel Kumar Onteru, Dheer Singh
2406 related Products with: Epitope-based in silico peptide design yields peptide-directed antibodies that recognize the buffalo luteinizing hormone.
96 assays96 tests20 250 TESTS1 mg100ug50 1 ml0.2 mg200ul100 0.25 ml
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#33591729 2021/02/16
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Generation of Antibodies Targeting Cleavable Cross-Linkers.
Chemical cross-linking has become a powerful tool for the analysis of protein structures and interactions by mass spectrometry. A particular strength of this approach is the ability to investigate native states in vivo, investigating intact organelles, cells, or tissues. For such applications, the cleavable cross-linkers disuccinimidyl sulfoxide (DSSO) and disuccinimidyl dibutyric urea (DSBU) are gaining increasing popularity, as they allow for the analysis of complex mixtures. It is inherently difficult to follow the reaction of cross-linkers with proteins in intact biological structures, stalling the optimization of in vivo cross-linking experiments. We generated polyclonal antibodies targeting DSSO- and DSBU-modified proteins, by injection of cross-linked bovine serum albumin (BSA) in rabbits. We show that the cross-linker-modified BSA successfully triggered an immune response, and that DSSO- and DSBU-specific antibodies were generated by the animals. Using affinity-purified antibodies specific for the individual cross-linkers, we demonstrate their application to the detection of cross-linker-modified proteins in Western blot and immunocytochemistry experiments of intact and permeabilized cells. Furthermore, we show their ability to immunoprecipitate DSSO/DSBU-modified proteins and provide evidence for their affinity toward water-quenched dead-links. These antibodies provide a valuable tool for the investigation of proteins modified with the cross-linkers DSSO and DSBU.Jasjot Singh, Srigayatri Ponnaiyan, Volkmar Gieselmann, Dominic Winter