Search results for: B-Phycoerythrin antibody Isotype IgG Host Rabbit
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SCM, the M Protein of Binds Immunoglobulin G.The M protein of (SCM) is a virulence factor and serves as a surface-associated receptor with a particular affinity for mini-plasminogen, a cleavage product of the broad-spectrum serine protease plasmin. Here, we report that SCM has an additional high-affinity immunoglobulin G (IgG) binding activity. The ability of a particular isolate to bind to IgG significantly correlates with a -positive phenotype, suggesting a dominant role of SCM as an IgG receptor. Subsequent heterologous expression of SCM in non-IgG binding and Western Blot analysis with purified recombinant SCM proteins confirmed its IgG receptor function. As expected for a zoonotic agent, the SCM-IgG interaction is species-unspecific, with a particular affinity of SCM for IgGs derived from human, cats, dogs, horses, mice, and rabbits, but not from cows and goats. Similar to other streptococcal IgG-binding proteins, the interaction between SCM and IgG occurs via the conserved Fc domain and is, therefore, non-opsonic. Interestingly, the interaction between SCM and IgG-Fc on the bacterial surface specifically prevents opsonization by C1q, which might constitute another anti-phagocytic mechanism of SCM. Extensive binding analyses with a variety of different truncated SCM fragments defined a region of 52 amino acids located in the central part of the mature SCM protein which is important for IgG binding. This binding region is highly conserved among SCM proteins derived from different isolates but differs significantly from IgG-Fc receptors of and sub. , respectively. In summary, we present an additional role of SCM in the pathogen-host interaction of . The detailed analysis of the SCM-IgG interaction should contribute to a better understanding of the complex roles of M proteins in streptococcal pathogenesis.
ANIMAL IMMUNOGLOBULINS , Pfu DNA Polymerase protei Myelin Basic Protein Heat Shock Protein 70 (H nm23 (NDPK-A Protein); C nm23 (NDPK-A Protein); C MIC2 Gene Protein, CD99; MIC2 Gene Protein, CD99; Glial Fibrillary Acidic Glial Fibrillary Acidic nm23 (NDPK-A Protein); C MIC2 Gene Protein, CD99;
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A New Enzyme-Linked Immunosorbent Assay for a Total Anti-T Lymphocyte Globulin Determination: Development, Analytical Validation, and Clinical Applications.Anti-T lymphocyte globulin (ATLG) modulates the alloreactivity of T lymphocytes, reducing the risk of immunological posttransplant complications, in particular rejection and graft-versus-host disease, after allogeneic hematopoietic stem cell transplantation (HSCT). We developed and validated a new enzyme-linked immunosorbent assay (ELISA) method to measure serum levels of total ATLG and evaluate the pharmacokinetics (PK) of the drug in children with β-Thalassemia, receiving allogeneic HSCT.
2416 related Products with: A New Enzyme-Linked Immunosorbent Assay for a Total Anti-T Lymphocyte Globulin Determination: Development, Analytical Validation, and Clinical Applications.MOUSE ANTI BOVINE ROTAVIR RABBIT ANTI GSK3 BETA (pS FDA Standard Frozen Tissu FDA Standard Frozen Tissu Mouse Anti-Insulin-Like G MarkerGene™ Total Prote MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI APAAP COMPLEX, Mouse anti-chick type I c
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Immunoreactivity Analysis of the Nonstructural Proteins of Human Enterovirus 71.Human enterovirus 71 (EV-A71) is one of the main etiological agents of hand, foot, and mouth disease (HFMD), which has been prevalent mainly in the Asia-Pacific region in the past several decades. The nonstructural proteins of EV-A71 will be expressed significantly during viral replication in host cells after EV-A71 infection. For the determination of the antibodies response against nonstructural proteins of EV-A71, in this study, the complete 2ABC, 3ABC, and 3D proteins were expressed in Escherichia coli and were then studied for their immunoreactivity by immunoblot assay and indirect enzyme-linked immunosorbent assay (ELISA), respectively. Three His-tagged fusion proteins were expressed effectively in E. coli, which were in agreement with the expected molecular mass. The results from immunoblot assay and indirect ELISA showed that all three purified fusion proteins can react with IgG antibodies from EV-A71-infected patients, but can hardly be recognized by IgG antibodies derived from mice or rabbits immunized by inactivated EV-A71 virus particles. The IgG antibody response against nonstructural proteins of EV-A71 is associated with viral infection or replication, which indicate that these nonstructural proteins could be used as candidate antigen for early diagnosis of EV-A71 infection, or to distinguish the EV-A71-specific antibodies after viral infection from inactivated vaccine immunization.
2416 related Products with: Immunoreactivity Analysis of the Nonstructural Proteins of Human Enterovirus 71.Rabbit Anti-Enterovirus ( Rabbit Anti-Enterovirus ( Recombinant Human PKC the Recombinant Human PKC the Recombinant Human PKC the Enterovirus Type 71 Lysat TCP-1 theta antibody Sour Recombinant Human YWHAB P Recombinant Human YWHAB P Recombinant Human YWHAB P Recombinant Human TNFRSF9 Recombinant Human TNFRSF9
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Intranasal immunization with recombinant Toxoplasma gondii actin depolymerizing factor confers protective efficacy against toxoplasmosis in mice.Toxoplasma gondii is an opportunistic protozoan closely associated with AIDS and vertical transmission. T. gondii actin depolymerizing factor (TgADF) plays an important role in actin cytoskeleton remodeling, and it is required to invade host cells. TgADF was a promising vaccine candidate. To observe the immunological changes and protective efficacy of recombinant TgADF protein (rTgADF) against T. gondii infection, we optimized the intranasal immunization dose of rTgADF and analyzed the survival rate and tachyzoite loads in mouse tissues after oral challenge with T. gondii tachyzoites.
1709 related Products with: Intranasal immunization with recombinant Toxoplasma gondii actin depolymerizing factor confers protective efficacy against toxoplasmosis in mice.Toxoplasma gondii GRA8, r Toxoplasma gondii MIC 3 r Toxoplasma gondii P24 (GR Toxoplasma gondii P29 (GR Toxoplasma gondii P30 (SA Macrophage Colony Stimula Macrophage Colony Stimula Recombinant Human Intrins Recombinant Human Intrins Recombinant Human Intrins Recombinant Toxoplasma go Recombinant Toxoplasma go
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[Prokaryotic expression of Staphylococcus aureus Clumping factor B and evaluation of the antiserum-mediated opsonic activity].Staphylococcus aureus is a major cause of hospital-acquired infection. Because the bacteria are very easy to become resistant to antibiotics, vaccination is a main method against S. aureus infection. Clumping factor B (ClfB) is an adhesion molecule essential for S. aureus to colonize in the host mucosa and is regarded as an important target antigen. In this study, we successfully used Escherichia coli to express a segment encoding the N1-N3 regions of ClfB protein (Truncated-ClfB) cloned from S. aureus. The protein was purified by affinity and ion exchange chromatographies and gel filtration. Rabbits were immunized three times with purified Truncated-ClfB. After that, blood was collected to prepare serum which were then used for measurement of antibody level. Phagocytosis of S. aureus opsonized by the serum was determined by a flow cytometry. Results show that the serum IgG titer reached 1:640 000. Phagocytosed S. aureus by polymorphonuclear leukocytes were significantly more when the bacteria were opsonized by the serum from Truncated-ClfB immunized rabbits than those from no immunized group (P < 0.01). Therefore, the results indicated that Truncated-ClfB could be a promising vaccine candidate against S. aureus infection.
2545 related Products with: [Prokaryotic expression of Staphylococcus aureus Clumping factor B and evaluation of the antiserum-mediated opsonic activity].Growth Differentiation Fa Growth Differentiation Fa BACTERIOLOGY BACTEROIDES Bacillus anthracis (Anthr Bacillus anthracis (Anthr Human Brain Derived Neuro Human Transforming Growth Human Fibroblast Growth F Human Stromal Cell-Derive Human Platelet Derived Gr Human Fibroblast Growth F Human Nerve Growth Factor
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A peptide immunization approach to counteract a Staphylococcus aureus protease defense against host immunity.Pathogens that induce acute and chronic infections, as well as certain cancers, employ numerous strategies to thwart host cellular and humoral immune defenses. One proposed evasion mechanism against humoral immunity is a localized expression of extracellular proteases that cleave the IgG hinge and disable host IgG functions. Host immunity appears to be prepared to counter such a proteolytic tactic by providing a group of autoantibodies, denoted anti-hinge antibodies that specifically bind to cleaved IgGs and provide compensating functional restoration in vitro. These respective counter-measures highlight the complex interrelationships among pathogens and host immunity and suggested to us a possible means for therapeutic intervention. In this study, we combined an investigation of pathogen-mediated proteolysis of host IgGs with an immunization strategy to boost host anti-hinge antibodies. In a Staphylococcus aureus infection model using an artificial tissue cage (wiffle ball) implanted into rabbits, cleaved rabbit IgGs were detected in abundance in the abscesses of untreated animals early after infection. However, in animals previously immunized with peptide analogs of the cleaved IgG hinge to generate substantial anti-hinge antibody titers, S. aureus colony formation was markedly reduced compared to control animals or those similarly immunized with a scrambled peptide sequence. The results of this study demonstrate that extensive local proteolysis of IgGs occurs in a test abscess setting and that immunization to increase host anti-hinge antibodies provided substantial acute protection against bacterial growth.
2696 related Products with: A peptide immunization approach to counteract a Staphylococcus aureus protease defense against host immunity.Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M Clostridium botulinum D T C-Peptide antibody, Monoc C Peptide antibody, Monoc C Peptide antibody, Monoc Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi
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Screening diagnostic candidates for schistosomiasis from tegument proteins of adult Schistosoma japonicum using an immunoproteomic approach.Schistosomiasis is one of the world's most prevalent zoonotic diseases and a serious worldwide public health problem. Since the tegument (TG) of Schistosoma japonicum is in direct contact with the host and induces a host immune response against infection, the identification of immune response target molecules in the schistosome TG is crucial for screening diagnostic antigens for this disease.
2622 related Products with: Screening diagnostic candidates for schistosomiasis from tegument proteins of adult Schistosoma japonicum using an immunoproteomic approach.MOUSE ANTI BOVINE ROTAVIR Mouse Anti-RSV 33kDa & 19 MOUSE ANTI BORRELIA BURGD succinate-CoA ligase, GDP formin-like 1 antibody So Recombinant Human Angiost Recombinant Human Angiost Native Human Angiostatin Native Human Angiostatin Recombinant Human ANGPTL3 Recombinant Human ANGPTL3 Recombinant Human ANGPTL3
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Cloning, expression and characterization of protein disulfide isomerase of Schistosoma japonicum.The excretory/secretory (ES) proteins of schistosomes play important roles in modulating host immune systems and are regarded as potential vaccine candidates and drug targets. Protein disulfide isomerase (PDI) is an essential enzyme that is involved in disulfide bond formation and rearrangement. In the present study, SjPDI, a 52.8 kDa protein previously identified in a proteomics analysis as one of the ES proteins of Schistosoma japonicum, was cloned and characterized. Western blot analysis showed that recombinant SjPDI (rSjPDI) was recognized by serum from rabbits vaccinated with schistosome worm antigen. Worm protein extracts and ES protein extracts from S. japonicum could react with anti-rSjPDI mouse serum. Real-time PCR analysis indicated that SjPDI was expressed at all developmental stages tested, and a high expression level was detected in 42-day-old male worms. Immunofluorescence analysis revealed that SjPDI was mainly distributed on the tegument and parenchyma of S. japonicum worms. An enzyme-linked immunosorbent assay (ELISA) demonstrated that rSjPDI could induce a high level of rSjPDI-specific IgG antibodies. The biological activity of purified rSjPDI was confirmed by isomerization and antioxidative activity assays. The 35.32%, 26.19% reduction in the worm burden and 33.17%, 31.7% lower liver egg count were obtained in mice vaccinated with rSjPDI compared with the blank control group in two independent trials. Our preliminary results suggest that rSjPDI plays an important role in the development of the schistosome and is a potential vaccine candidate for schistosomiasis.
2931 related Products with: Cloning, expression and characterization of protein disulfide isomerase of Schistosoma japonicum.PDI (Protein Disulfide Is Protein Disulfide Isomera Protein Disulfide Isomera Protein Disulfide Isomera baculoCOMPLETE protein ex Lentiviral Technology pCD Human dopachrome tautomer Rabbit Anti-Rat Androgen pYLEX1 - Expression Vect AccuRapid™ Cell Free Pr Ofloxacin CAS Number [824 Recombinant Human Androge
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Hyperglycosylated stable core immunogens designed to present the CD4 binding site are preferentially recognized by broadly neutralizing antibodies.The HIV-1 surface envelope glycoprotein (Env) trimer mediates entry into CD4(+) CCR5(+) host cells. Env possesses conserved antigenic determinants, such as the gp120 primary receptor CD4 binding site (CD4bs), a known neutralization target. Env also contains variable regions and protein surfaces occluded within the trimer that elicit nonneutralizing antibodies. Here we engineered additional N-linked glycans onto a cysteine-stabilized gp120 core (0G) deleted of its major variable regions to preferentially expose the conformationally fixed CD4bs. Three, 6, 7, and 10 new NXT/S glycan (G) motifs were engineered into 0G to encode 3G, 6G, 7G, and 10G cores. Following purification, most glycoproteins, except for 10G, were recognized by broadly neutralizing CD4bs-directed antibodies. Gel and glycan mass spectrometry confirmed that additional N-glycans were posttranslationally added to the redesigned cores. Binding kinetics revealed high-affinity recognition by seven broadly neutralizing CD4bs-directed antibodies and low to no binding by non-broadly neutralizing CD4bs-directed antibodies. Rabbits inoculated with the hyperglycosylated cores elicited IgM and IgG responses to each given protein that were similar in their neutralization characteristics to those elicited by parental 0G. Site-specific glycan masking effects were detected in the elicited sera, and the antisera competed with b12 for CD4bs-directed binding specificity. However, the core-elicited sera showed limited neutralization activity. Trimer priming or boosting of the core immunogens elicited tier 1-level neutralization that mapped to both the CD4bs and V3 and appeared to be trimer dependent. Fine mapping at the CD4bs indicated that conformational stabilization of the cores and addition of N-glycans altered the molecular surface of Env sites of vulnerability to neutralizing antibody, suggesting an explanation for why the elicited neutralization was not improved by this rational design strategy.
2476 related Products with: Hyperglycosylated stable core immunogens designed to present the CD4 binding site are preferentially recognized by broadly neutralizing antibodies.Multiple organ cancer tis Multiple organ tumor tiss Signal Transduction Anti CD4 antibody, Monoclonal CD4 antibody, Monoclonal Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Hepatitis C Virus antibod Cholera toxin antibody, M Clostridium botulinum D T Clostridum difficile toxi Clostridum difficile toxi
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Comparison of an indirect fluorescent antibody test with Western blot for the detection of serum antibodies against Encephalitozoon cuniculi in cats.Current clinical research indicates that Encephalitozoon (E.) cuniculi infections in cats may be underdiagnosed, especially in animals with typical ocular signs (cataract/anterior uveitis). Although molecular detection of the pathogen in tissue appears promising, serology remains the major diagnostic tool in the living animal. While serological tests are established for the main host of E. cuniculi, the rabbit, the routine serological diagnosis for cats still needs validation. The aim of the study was to evaluate the consistency of indirect fluorescence antibody test (IFAT) and Western blot (WB) for the detection of IgG antibodies against E. cuniculi in the serum of 84 cats. In addition, PCR of liquefied lens material or intraocular fluid was performed in those of the cats with a suspected ocular E. cuniculi infection. Twenty-one cats with positive PCR results were considered as a positive reference group. Results obtained by IFAT and WB corresponded in 83/84 serum samples, indicating a very good correlation between both serological methods. Using WB as the standard reference, sensitivity and specificity for the detection of antibodies against E. cuniculi by the IFAT were 97.6 and 100%, respectively. The positive and negative predictive values for the IFAT were 100 and 97.7%, respectively. The accuracy (correct classified proportion) for the detection of IgG antibodies against E. cuniculi in cats was 98.8%. The comparison of both serological methods with the PCR results also revealed a good agreement as 20 out of 21 PCR-positive samples were seropositive both in IFAT and WB. Both tests can be considered as equally reliable assays to detect IgG antibodies against E. cuniculi in cats. As the IFAT is quicker and easier to perform, it is recommended for routine use in the diagnosis of feline encephalitozoonosis.
1859 related Products with: Comparison of an indirect fluorescent antibody test with Western blot for the detection of serum antibodies against Encephalitozoon cuniculi in cats.Multiple organ tumor tiss HIV1 integrase antibody, Human Serum Albumin antib Human Serum Albumin antib HCV antibody test strip, H. Pylori antibody test s Beta Amyloid (40) ELISA K Beta Amyloid (1 42) ELISA anti-GFP antibody, rabbit Apoptosis antibody array Cell cycle antibody array Cytokine antibody array i
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