Search results for: Rabbit Anti-HIV p55+P6-Gag Polyclonal Antibody
#25045827 
2014/07/18
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Vaccine focusing to cross-subtype HIV-1 gp120 variable loop epitopes.
We designed synthetic, epitope-focused immunogens that preferentially display individual neutralization epitopes targeted by cross-subtype anti-HIV V3 loop neutralizing monoclonal antibodies (mAbs). Vaccination of rabbits with these immunogens resulted in the elicitation of distinct polyclonal serum Abs that exhibit cross-subtype neutralization specificities mimicking the mAbs that guided the design. Our results prove the principle that a predictable range of epitope-specific polyclonal cross-subtype HIV-1 neutralizing Abs can be intentionally elicited in mammals by vaccination. The precise boundaries of the epitopes and conformational flexibility in the presentation of the epitopes in the immunogen appeared to be important for successful elicitation. This work may serve as a starting point for translating the activities of human broadly neutralizing anti-HIV-1 monoclonal antibodies (bNAbs) into matched immunogens that can contribute to an efficacious HIV-1 vaccine.Timothy Cardozo, Shixia Wang, Xunqing Jiang, Xiang-Peng Kong, Catarina Hioe, Chavdar Krachmarov
1476 related Products with: Vaccine focusing to cross-subtype HIV-1 gp120 variable loop epitopes.
25 G100ug1x96 well plate100ug 100ul100ug10001000100ug 5 G100ug100ug
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#17597142 2007/06/14
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Development and evaluation of an immunoassay for the monitoring of the anti-HIV drug amprenavir.
An assay for routine therapeutic drug monitoring of anti-HIV HAART drugs in clinical use is highly desirable, in order to rapidly measure the pharmacokinetic parameters on single patients. We have started a project to develop a panel of enzyme-linked immunosorbent assays (ELISA) for the whole set of HAART drugs, and the development, performance and evaluation of the assay for amprenavir is described here. A diazo conjugate of amprenavir has been used in order to raise polyclonal anti-amprenavir antibodies in rabbits. Antisera have been used to set up a quantitative and rapid competitive assay. Plasma samples are simply diluted in the assay buffer after thermal inactivation, before running the assay. The assay allows the detection of amprenavir in the quantification range 400-5000 ng/ml, in a diluted plasma sample. The assay has been compared with an HPLC reference technique, on 27 samples from treated patients. Within the quantification range, the ELISA data are well correlated with the HPLC results by a regression line close to the identity, and a Bland-Altman analysis shows the agreement between the two methods.Erica Bastiani, Fabio Benedetti, Federico Berti, Pietro Campaner, Elena Donadel, Michela Montagna, Mario Regazzi, Serena Rinaldi, Adriano Savoini, Romina Venturini
2736 related Products with: Development and evaluation of an immunoassay for the monitoring of the anti-HIV drug amprenavir.
1 ml100.00 ul100.00 ul1 ml0.1 mg100
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#14522014 //
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Peptide immunogens based on the envelope region of HIV-1 are recognized by HIV/AIDS patient polyclonal antibodies and induce strong humoral immune responses in mice and rabbits.
Peptide immunogens produced by novel synthesis techniques and based on envelope proteins have repeatedly proven successful in inducing anti-HIV and anti-SIV responses in addition to producing anti-peptide immunity [Vaccine 12 (8) (1994) 736; AIDS Res. Hum. Retroviruses 14 (9) (1998) 751; Vaccine (2002) 2680]. We report here the design and evaluation of synthetic peptide constructs mimicking the variability of the third variable (V3) loop, or representing the conservation of the CD4 region of HIV-1 envelope. Three peptides based on the V3 region of HIV-1 subtype C gp120 and designated multiple epitope immunogens (MEI) differ in that one was randomly branched containing a spacer (b-MEI-s), another conjugated to a tetrameric lysine core (MEIV3b(4)) and the third conjugated to poly-L-lysine (poly-L-MEI). The method of synthesis employed produced peptides that were either linear, dimeric or tetramerically branched thereby providing differing levels of conformation. In addition the peptides also differed in their levels of variability. A fourth peptide designated B138 was based on a conserved region of HIV-1 envelope. The aim of this work was to evaluate the effect of variability and level of conformation on the immunogenicity of variable region peptides (MEI's) when compared to that of a known immunogenic and conserved region peptide (B138). Anti-peptide humoral immunity induced in BALB/c mice and New Zealand White rabbits produced antigen-recognizing antibody titres of R Hewer, D Meyer 2945 related Products with: Peptide immunogens based on the envelope region of HIV-1 are recognized by HIV/AIDS patient polyclonal antibodies and induce strong humoral immune responses in mice and rabbits.
100ug100 μg1000 TESTS/0.65ml200ul100 μg100 μg100ug Lyophilized100 μg100ug Lyophilized100ug Lyophilized100ug100ug
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#1283720 //
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[The immunoenzyme test system for detection of HIV-1 antigens based on using immune polyclonal anti-HIV serum and monoclonal antibodies against gene GAG HIV-1 proteins].
The paper describes the enzyme immunoassay system for detection of human immunodeficiency virus antigens, which is based on the use of rabbit anti-HIV antibodies and monoclonal antibodies to HIV-1 gene proteins gag. The system may be useful in the examination of laboratory and clinical samples to reveal both free and conjugated antigens in the composition of immune complexes. The sensitivity of the assay system under development is 0.5 ng/ml at 100% specificity.G N Trushinskaia, V I Simonov, N E Makarova, D N Nosik, A A Kushch, R A Gibadulin
2899 related Products with: [The immunoenzyme test system for detection of HIV-1 antigens based on using immune polyclonal anti-HIV serum and monoclonal antibodies against gene GAG HIV-1 proteins].
1000 TESTS/0.65ml100ug100ug100ug Lyophilized1000 TESTS/1ml100ug Lyophilized100ul1000 TESTS/50 100UG100ug Lyophilized100ug Lyophilized100ug/vial
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#1694432 //
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Anti-idiotypic antisera raised against monoclonal antibody specific for a p24 gag region epitope detects a common interspecies idiotype associated with anti-HIV responses.
One potential strategy for the control of human immunodeficiency virus (HIV) infection is immune network manipulation using anti-idiotypic antibodies: this study was undertaken to demonstrate experimentally the potential of such an approach which, in a more highly evolved form, could be used for the treatment of the acquired immune deficiency virus (AIDS) and related disorders. Anti-idiotypic antibodies were generated in rabbits against a murine monoclonal antibody identifying an epitope on the p24 gag core protein of HIV. After extensive absorption on affinity columns to remove isotype- and allotype-specific antibodies, the purified anti-idiotypic antibody preparation was shown to have specific complementarity with the immunizing mouse monoclonal antibody. This anti-idiotypic antibody was also shown to recognize a common idiotype associated with HIV-specific antibodies from both humans and chimpanzees infected with the AIDS virus. In addition a group of rats immunized with the anti-Id responded with significant antibody titers to recombinant derived p24 gag. These data indicate that at least a subpopulation of these polyclonal anti-Id antibodies structurally mimics an HIV gag region epitope and suggest that immunoregulation by anti-idiotypic antibodies may have therapeutic utility for the AIDS epidemic.W J Morrow, I Gaston, T Anderson, N Haigwood, M S McGrath, J Rosen, K S Steimer
2045 related Products with: Anti-idiotypic antisera raised against monoclonal antibody specific for a p24 gag region epitope detects a common interspecies idiotype associated with anti-HIV responses.
25 µg1 ml0.25 mg25 µg100 TESTS0.2 mg0.2 mg0.1 ml100ug100ug100ul100ug Lyophilized
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#2428879 //
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Binding of the human retrovirus HTLV-III/LAV/ARV/HIV to the CD4 (T4) molecule: conformation dependence, epitope mapping, antibody inhibition, and potential for idiotypic mimicry.
Human immunodeficiency virus (HIV), the retrovirus that causes the acquired immunodeficiency syndrome, is cytopathic for CD4+ T cells and binds to these cells via a complex of the 110,000 m.w. viral-envelope glycoprotein, gp110, and the CD4 molecule. We treated virus with several physical, chemical, and enzymic agents to determine their effect on the capacity of HIV to bind to the CD4+ T cell line, CEM. Reduction and alkylation (but not alkylation alone) and trypsin digestion (but not glycolytic enzyme digestions) of HIV destroyed its capacity to bind. If the tertiary protein structure conferred by disulfide bonding is not disrupted, the tertiary and secondary conformations dependent on noncovalent forces appear to be thermodynamically favored, because treatment with denaturants such as sodium dodecyl sulfate, 8 M urea, alcohol, or heat (56 degrees C or 65 degrees C for 30 min) followed by removal of the denaturants did not affect binding. Irreversible denaturation and loss of binding occurred after heating at 100 degrees C for 10 min. HIV binding to CD4+ T cells was inhibited either by murine monoclonal antibodies to the CD4 molecule or by human polyclonal or murine monoclonal antibodies to the gp110 molecule. On the basis of results of binding inhibition obtained with a panel of alpha-CD4 monoclonal antibodies, the receptor site for virus on the CD4 molecule was mapped to the amino-terminal portion of the molecule. Four candidate alpha-CD4 monoclonal antibodies that were potent inhibitors of virus binding (OKT4A, OKT4D, OKT4F, and Leu-3a) were examined for the possibility that their binding sites (idiotopes) might share structural and conformational similarity with the CD4-binding site on gp110. Polyclonal human or rabbit anti-HIV sera (that reacted with gp110 and inhibited virus binding) did not react with or inhibit the binding of these four alpha-CD4 monoclonal antibodies. Conversely, rabbit anti-idiotypic sera raised against each of the four candidate CD4 monoclonal antibodies did not react with virus or inhibit virus binding to CD4+ T cells. Further search or different approaches may yet yield an idiotype that is a structural and conformational "internal image" of the CD4-binding site of virus.J S McDougal, J K Nicholson, G D Cross, S P Cort, M S Kennedy, A C Mawle