Search results for: Rabbit Anti-14-3-3 Antibodies
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A modular synthetic route to size-defined immunogenic b antigens is key to the identification of an octasaccharide lead vaccine candidate.The first glycoconjugate vaccine using isolated glycans was licensed to protect children from serotype b (Hib) infections. Subsequently, the first semisynthetic glycoconjugate vaccine using a mixture of antigens derived by polymerization targeted the same pathogen. Still, a detailed understanding concerning the correlation between oligosaccharide chain length and the immune response towards the polyribosyl-ribitol-phosphate (PRP) capsular polysaccharide that surrounds Hib remains elusive. The design of semisynthetic and synthetic Hib vaccines critically depends on the identification of the minimally protective epitope. Here, we demonstrate that an octasaccharide antigen containing four repeating disaccharide units resembles PRP polysaccharide in terms of immunogenicity and recognition by anti-Hib antibodies. Key to this discovery was the development of a modular synthesis that enabled access to oligosaccharides up to decamers. Glycan arrays containing the synthetic oligosaccharides were used to analyze anti-PRP sera for antibodies. Conjugates of the synthetic antigens and the carrier protein CRM197, which is used in licensed vaccines, were employed in immunization studies in rabbits.
1152 related Products with: A modular synthetic route to size-defined immunogenic b antigens is key to the identification of an octasaccharide lead vaccine candidate.Clostridium botulinum D T Rabbit Anti-Clostridium b Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi
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Characterization of Three Novel Linear Neutralizing B-Cell Epitopes in the Capsid Protein of Swine Hepatitis E Virus.Hepatitis E virus (HEV) causes liver disease in humans and is thought to be a zoonotic infection with domestic animals being a reservoir including swine and rabbits. One of the proteins encoded by the virus is the capsid protein. This is likely the major immune-dominant protein and a target for vaccination. Four monoclonal antibodies (MAbs); three novel; 1E4, 2C7, 2G9, and one previously characterized (1B5), were evaluated for binding to the capsid protein from genotype 4 (swine) hepatitis E virus (HEV). The results indicated that DFCP, PSRPF, and EPTV peptides on the capsid protein comprised minimal amino acid sequence motifs recognized by 1E4, 2C7, and 2G9, respectively. The data suggested that 2C7 and 2G9 epitopes were partially exposed on the surface of the capsid protein. Truncated genotype 4 swine HEV capsid protein (sp239, amino acids 368-606), can exist in multimeric forms. Pre-incubation of swine HEV with 2C7, 2G9, or 1B5 before addition to HepG2 cells partially blocked sp239 cell binding and inhibited swine HEV infection. The study indicated that 2C7, 2G9, and 1B5 partially blocked swine HEV infection of rabbits better than 1E4 or normal mouse IgG. The cross reactivity of antibodies suggested that capsid epitopes recognized by 2C7 and 2G9 are common to HEV strains infecting most host species. Collectively, MAbs 2C7, 2G9, and 1B5 were shown to recognize three novel linear neutralizing B-cell epitopes of genotype 4 HEV capsid protein. These results enhance understanding of HEV capsid protein structure to guide vaccine and anti-viral design. Genotype 3 and 4 HEVs are zoonotic viruses. Here, genotype 4 HEV was studied due to its prevalence in human populations and pig herds in China. To improve HEV disease diagnosis and prevention, a better understanding of antigenic structure and neutralizing epitopes of HEV capsid protein are needed. In this study, the locations of three novel linear B-cell recognition epitopes within genotype 4 swine HEV capsid protein were characterized. Moreover, the neutralizing abilities of three MAbs specific for this protein, 2C7, 2G9, and 1B5, were studied and Collectively, these findings reveal structural details of genotype 4 HEV capsid protein and should facilitate development of applications for design of vaccines and antiviral drugs for broader prevention, detection, and treatment of HEV infection of diverse human and animal hosts.
1558 related Products with: Characterization of Three Novel Linear Neutralizing B-Cell Epitopes in the Capsid Protein of Swine Hepatitis E Virus.Anti-Infectious Pancreati Anti-Infectious Pancreati Anti C Reactive Protein A Human Epstein-Barr Virus Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Mouse Epstein-Barr Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus
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Recombinant Protein Containing B-Cell Epitopes of Different Spider Toxins Generates Neutralizing Antibodies in Immunized Rabbits.Loxoscelism is the most important form of araneism in South America. The treatment of these accidents uses heterologous antivenoms obtained from immunization of production animals with crude loxoscelic venom. Due to the scarcity of this immunogen, new alternatives for its substitution in antivenom production are of medical interest. In the present work, three linear epitopes for Loxosceles astacin-like protease 1 (LALP-1) (SLGRGCTDFGTILHE, ENNTRTIGPFDYDSIMLYGAY, and KLYKCPPVNPYPGGIRPYVNV) and two for hyaluronidase (LiHYAL) (NGGIPQLGDLKAHLEKSAVDI and ILDKSATGLRIIDWEAWR) from spider venom were identified by SPOT-synthesis technique. One formerly characterized linear epitope (DFSGPYLPSLPTLDA) of sphingomyelinase D (SMase D) SMase-I from was also chosen to constitute a new recombinant multiepitopic protein. These epitopes were combined with a previously produced chimeric multiepitopic protein (rCpLi) composed by linear and conformational B-cell epitopes from SMase D from venom, generating a new recombinant multiepitopic protein derived from loxoscelic toxins (rMEPLox). We demonstrated that rMEPLox is non-toxic and antibodies elicited in rabbits against this antigen present reactivity in ELISA and immunoblot assays with Brazilian , and spider venoms. and neutralization assays showed that anti-rMEPLox antibodies can efficiently neutralize the sphingomyelinase, hyaluronidase, and metalloproteinase activity of venom. This study suggests that this multiepitopic protein can be a suitable candidate for experimental vaccination approaches or for antivenom production against spp. venoms.
2359 related Products with: Recombinant Protein Containing B-Cell Epitopes of Different Spider Toxins Generates Neutralizing Antibodies in Immunized Rabbits.Goat Anti- T-cell differe Macrophage Colony Stimula Macrophage Colony Stimula Recombinant Influenza HA Recombinant Influenza HA Recombinant Influenza HA Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant Human HGF [fr Recombinant Human HGF [fr Recombinant Human HGF [fr
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Autoimmunity to Tropomyosin-Specific Peptides Induced by in Leprosy Patients: Identification of Mimicking Proteins.It has been shown earlier that there is a rise in the levels of autoantibodies and T cell response to cytoskeletal proteins in leprosy. Our group recently demonstrated a rise in both T and B cell responses to keratin and myelin basic protein in all types of leprosy patients and their associations in type 1 reaction (T1R) group of leprosy.
1361 related Products with: Autoimmunity to Tropomyosin-Specific Peptides Induced by in Leprosy Patients: Identification of Mimicking Proteins.Native Influenza HA (A To Native Influenza HA (A To Native Influenza HA (A To BYL-719 Mechanisms: PI3K- Apoptosis Phospho-Specifi EGF Phospho-Specific Arra Influenza B (B Tokio 53 9 Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Human Epstein-Barr Virus
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Use of rabbit antibodies raised against GII.4 virus-like particles for diagnosis of infection.
2934 related Products with: Use of rabbit antibodies raised against GII.4 virus-like particles for diagnosis of infection.Rabbit Anti-B. anthracis Rabbit Anti-B. anthracis Rabbit Anti-Human HPA-1 A Rabbit Anti-SARS Virus Nu Rabbit Anti-Polyprotein(H Rabbit Anti-polyprotein[C Rabbit Anti-Hepatitis C V Rabbit Anti-Human 4EBP1 A Rabbit Anti-Human 4EBP1 ( Rabbit Anti-Human Amyloid Rabbit Anti-Human Amyloid Rabbit Anti-Rat Connexin
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Treating Anthrax-Induced Meningitis in Rabbits.Treatment of Anthrax is challenging, especially during the advanced stages of the disease. Recently the CDC updated its recommendations for post-exposure prophylaxis and treatment of exposed populations (pre and post symptoms onset). These recommendations distinguished, for the first time, between the systemic disease with and without meningitis, a common and serious complication of anthrax. The CDC considers all systemic patients as meningeal unless positively proven otherwise. The treatment of patients suffering from systemic Anthrax with suspected or confirmed meningitis includes the combination of three antibiotics -- a fluoroquinolone (Levofloxacin or Ciprofloxacin), a β-lactam (Meropenem or Imipenem) and a protein-synthesis inhibitor (Linezolid or Clindamycin). In addition, treatment with an antitoxin (αPA antibodies) and Dexamethasone should also be applied. Since the efficacy of most of these treatments was not demonstrated, especially in meningeal animal models, we developed an Anthrax-meningitis model in rabbits and tested several of these recommendations. We demonstrate that in this model, Ciprofloxacin, Linezolid and Meropenem are ineffective as single treatments while Clindamycin is highly effective. Furthermore, combined treatments of Ciprofloxacin and Linezolid, or Ciprofloxacin and Dexamethasone failed in treating meningeal rabbits. We demonstrate that Dexamethasone actually hinders the blood brain barrier penetration of antibiotics, reducing the effectiveness of antibiotic treatment of Anthrax-meningitis in the rabbit model.
Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Human Epstein-Barr Virus Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Mouse Epstein-Barr Virus TGF beta induced factor 2 Bovine prolactin-induced
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Type VI collagen α1 chain polypeptide in non-triple helical form is an alternative gene product of COL6A1.Expression of type IV collagen α1 chain in non-triple helical form, NTH α1(IV), is observed in cultured human cells, human placenta, and rabbit tissues. Biological functions of NTH α1(IV) are most likely to be distinct from type IV collagen, since their biochemical characteristics are quite different. To explore the biological functions of NTH α1(IV), we prepared some anti-NTH α1(IV) antibodies. In the course of characterization of these antibodies, one antibody, #141, bound to a polypeptide of 140 kDa in size in addition to NTH α1(IV). In this study, we show evidence that the 140 kDa polypeptide is a novel non-triple helical polypeptide of type VI collagen α1 chain encoded by COL6A1, or NTH α1(VI). Expression of NTH α1(VI) is observed in supernatants of several human cancer cell lines, suggesting that the NTH α1(VI) might be involved in tumorigenesis. Reactivity with lectins indicates that sugar chains of NTH α1(VI) are different from those of the α1(VI) chain in triple helical form of type VI collagen, suggesting a synthetic mechanism and a mode of action of NTH α1(VI) is different from type VI collagen.
1177 related Products with: Type VI collagen α1 chain polypeptide in non-triple helical form is an alternative gene product of COL6A1.MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI CANINE DISTEMP MOUSE ANTI BORRELIA BURGD RABBIT ANTI GSK3 BETA (pS Goat Anti-Rat Collagen, t MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI APAAP COMPLEX, Anti CML Monoclonal Antib NATIVE HUMAN PROLACTIN, P 10x ELISA WASH BUFFER, Pr
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Expression of a Recombinant Nucleocapsid Protein of Rift Valley Fever Virus in Vero Cells as an Immunofluorescence Antigen and Its Use for Serosurveillance in Traditional Cattle Herds in Zambia.The open reading frame of the nucleocapsid protein (NP) of Rift Valley fever virus (RVFV) strain MP12 was cloned and expressed in Vero E6 cells. The recombinant NP (rNP)-expressing cells were used as antigens for an indirect immunofluorescent antibody assay (IFA). The rNP-based IFA and RVFV-infected Vero E6 cell (authentic antigen)-based IFA showed similar IFA profiles with immune rabbit serum, which was prepared by immunization with rNP expressed using a baculovirus vector. A total of 942 traditional cattle sera obtained in five districts in Central, Southern, and Western provinces of Zambia were screened for anti-RVFV antibodies by the authentic antigen-based and rNP-based IFAs. Significant agreement was obtained between the two IFAs. The findings show that the rNP-based IFA is a safe and useful diagnostic tool as an alternative to the authentic antigen-based IFA. The antibody titers given by the rNP-based IFA were higher than those by the authentic antigen-based IFA. Therefore, the rNP-based IFA might be useful for serosurveillance of RVFV infection among cattle. Antibody prevalence rates in the five districts were 1.3% to 13.5% in the authentic antigen-based IFA and 6.0% to 21.4% in the rNP-based IFA. The results indicated that despite no reports of active cases of RVF in these provinces of Zambia, the virus is circulating among cattle herds.
2895 related Products with: Expression of a Recombinant Nucleocapsid Protein of Rift Valley Fever Virus in Vero Cells as an Immunofluorescence Antigen and Its Use for Serosurveillance in Traditional Cattle Herds in Zambia.FIV Core Ag, recombinant Recombinant Hemagglutinin Toxoplasma gondii GRA8, r HIV 1 intergase antigen. Anti-Infectious Pancreati Anti-Infectious Pancreati Anti-Infectious Pancreati Mouse AntiInfluenza B Nuc Rabbit AntiFNIP1 Target A Mouse Anti-Insulin-Like G Goat Anti-Influenza A Vir Mouse Anti-Influenza A Vi
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Immunoassay Multiplexing on a Complementary Metal Oxide Semiconductor Photodiode Array.Scalable immunoassay multiplexing offers a route to creating rapid point-of-care (POC) diagnostics. We present a method for multiplexing immunoassays on the surface of a complementary metal oxide semiconductor (CMOS) sensor array integrated circuit (IC) without the use of physical separators such as wells or channels. Major advantages of using a CMOS sensor array include low mass-manufacturing costs, the possibility to multiplex multiple assays on a single IC, and improved signal when averaging multiple sensors, along with providing a platform where wash steps can be incorporated to maximize selectivity and sensitivity compared to paper based lateral flow immunoassay. The device was able to differentiate between samples containing either, neither, or both rabbit anti-mouse (RAM) antibodies and/or anti-HIV gp120 antibodies in serum using a gold-nanoparticle promoted silver enhancement immunoassay. HIV antibody concentrations down to 100 μg/mL were readily detected, which is three times lower than those typically found in infected humans (300-500 μg/mL), and the limit of detection was 10 μg/mL.
2556 related Products with: Immunoassay Multiplexing on a Complementary Metal Oxide Semiconductor Photodiode Array.Oncocytoma tissue array, ELISA Kit for A Disinteg Accessory Kit I for RayBi Blocking Buffer Antibody Detection Buffer A&B Anti Detection Buffer C&D Anti Streptavidin [+HRP] Antib Lysis Buffer Antibody Arr 8 Well Tray Antibody Arra 4-Well Tray Antibody Arra Mouse Anti-Human Matrix M Mouse Anti-Human Matrix M
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Immunohistochemical expression of polo-like kinase 1 in oral squamous cell carcinoma and oral submucous fibrosis.Polo-like kinase 1 (PLK1) is a critical molecule in the proliferation of several human cancers. Overexpression of PLK1 has been correlated with cancer cell proliferation and lower overall survival rates. Although PLK1 has been studied in various tumors, information regarding its expression in oral cancer and precancer is limited. Aims: This study is aimed at evaluating the expression of PLK1 in a potentially malignant and malignant disorder of the oral cavity, namely, oral submucous fibrosis (OSMF) and oral squamous cell carcinoma (OSCC), respectively, using the immunohistochemistry technique. It also intended to evaluate the association of the various histological grades of OSCC with the intensity of PLK1 expression.
1890 related Products with: Immunohistochemical expression of polo-like kinase 1 in oral squamous cell carcinoma and oral submucous fibrosis.Oral cavity squamous cell Lung squamous cell carcin Cervix squamous cell carc Esophagus squamous cell c Esophagus squamous cell c Esophageal squamous cell Oral squamous cell cancer Esophagus squamous cell c Esophagus squamous cell c Kidney clear cell carcino Kidney clear cell carcino Esophagus squamous cell c
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