Anti-HIV Designer Antigen (DAG19)

DAGs ‘designer antigens’ carry epitopes that can lead to the elicitation of broadly neutralising antibodies (bNAbs) in HIV patients. Identification of effective epitopes is a key area of research as bNAbs are a consistent protective immune correlate in human immunodeficiency virus (HIV) patients as well as in passive immunotherapy studies.The DAG16,19 and 23 polyclonal antibodies […]

Contributors

Inventor Institute
Tuck-Weng Kok The University of Adelaide
Cat. #: 154855
Unit size: 100 ug
Research Fields: Immunology;Microbiology
Application: ELISA ; IF ; WB
Target: DAG19
Reactivity: Human ; Guinea Pig ; Rat
Clone: DAG19
Host: Guinea Pig
Class: Polyclonal
Alternate name: human immunodeficiency virus designer antigen
Product description: DAGs ‘designer antigens’ carry epitopes that can lead to the elicitation of broadly neutralising antibodies (bNAbs) in HIV patients. Identification of effective epitopes is a key area of research as bNAbs are a consistent protective immune correlate in human immunodeficiency virus (HIV) patients as well as in passive immunotherapy studies.The DAG16,19 and 23 polyclonal antibodies lock onto epitopes on HIV pre-fusion intermediates. Lots of research focuses on identifying mAbs that target these pre-fusion intermediates, though this work has also identified some interest polyclonal antibodies that have shown to target pre-fusion epitopes and be useful tools in HIV research. The DAG16,19 and 23 have been used in experimentation to neutralise both T cell-tropic and macrophage-tropic HIV. The antibodies have been shown to be used to generate absorbed sera which contained antibodies against the viral DAG pre-fusion intermediates, but minimal or no antibodies against static/native HIV antigens and cellular antigens that are not involved in viral fusion. The antibodies have been shown to reduce T-cell tropic HIV-HXB2 infectivity by 65–68% and, importantly, reduce macrophage-tropic HIV-Bal infectivity by 39–46%. Please see publication (PMID: 25505973) for more details. Developing antibodies specific to novel epitopes on HIV pre-fusion intermediates is an incredibly important area of research and these polyclonals provide an interesting tool in this work. They have been shown to be instrumental in developing monoclonal antibodies specific to novel epitopes on HIV pre-fusion intermediates.
Conjugation: Unconjugated
Immunogen: HIV DAG 19
Target background: DAGs ‘designer antigens’ carry epitopes that can lead to the elicitation of broadly neutralising antibodies (bNAbs) in HIV patients. Identification of effective epitopes is a key area of research as bNAbs are a consistent protective immune correlate in human immunodeficiency virus (HIV) patients as well as in passive immunotherapy studies.The DAG16,19 and 23 polyclonal antibodies lock onto epitopes on HIV pre-fusion intermediates. Lots of research focuses on identifying mAbs that target these pre-fusion intermediates, though this work has also identified some interest polyclonal antibodies that have shown to target pre-fusion epitopes and be useful tools in HIV research. The DAG16,19 and 23 have been used in experimentation to neutralise both T cell-tropic and macrophage-tropic HIV. The antibodies have been shown to be used to generate absorbed sera which contained antibodies against the viral DAG pre-fusion intermediates, but minimal or no antibodies against static/native HIV antigens and cellular antigens that are not involved in viral fusion. The antibodies have been shown to reduce T-cell tropic HIV-HXB2 infectivity by 65–68% and, importantly, reduce macrophage-tropic HIV-Bal infectivity by 39–46%. Please see publication (PMID: 25505973) for more details. Developing antibodies specific to novel epitopes on HIV pre-fusion intermediates is an incredibly important area of research and these polyclonals provide an interesting tool in this work. They have been shown to be instrumental in developing monoclonal antibodies specific to novel epitopes on HIV pre-fusion intermediates.
Format: Liquid
Shipping conditions: Dry ice
References:

Kok et al. 2014. Clin Transl Immunology. 3(9):e24. PMID: 25505973.

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