Anti-HIV protease antibody [1696] (ab8327)
Overview
- Product nameAnti-HIV protease antibody [1696]
- DescriptionMouse monoclonal [1696] to HIV protease
- SpecificityThe antibody recognizes free N-terminus of mature HIV protease (HIV-1 and HIV-2). Does not react with precursor.
- Tested applicationsWB, ELISA, Inhibition Assay more details
- Immunogen
Recombinant HIV-1 protease.
Properties
- FormLiquid
- Storage instructionsStore at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: 15mM Sodium Azide
Constituents: PBS, pH 7.4 -
Concentration information loading... - Purity>95% by SDS-PAGE
- Purification notesPurified from ascites using protein A-affinity chromatography.
- Clonality Monoclonal
- Clone number1696
- Myelomaunknown
- IsotypeIgG1
- Research Areas
Applications
Our Abpromise guarantee covers the use of ab8327 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
| Application | Notes |
|---|---|
| WB | WB: Use at an assay dependent concentration. |
| ELISA | ELISA: Use at an assay dependent concentration. |
| Inhibition Assay | Inhib: Use at an assay dependent dilution. Strongly inhibits the activity of HIV-1 and HIV-2 proteases. |
Target
- RelevanceThe HIV1 core consists of a viral genome housed within a conical viral capsid that is generated during virion maturation. Human immunodeficiency virus type 1 (HIV1) matures after the viral protease processes the Gag and Pol polyproteins at 10 substrate locations. The protease of HIV1 is an aspartic protease and is functional only as a dimer; dimerization results in the formation of a binding cleft in which each of the two catalytic aspartic acids in which each monomer contributes each of the 2 catalytic aspartic acids. Because the protease is active only as a dimer, two of the GagPol precursors must themselves dimerize during virus assembly so that their protease domains can dimerize, become active, and process the precursors. Both the order and kinetics of cleavage as well as the extent of precursor processing appear to be critical steps in the generation of fully infectious, appropriately assembled viral particles. Inhibition of HIV-1 protease represents an important avenue for antiviral therapy. Currently available combination chemotherapy with reverse transcriptase inhibitors (RTIs) and protease inhibitors (PIs) for human immunodeficiency virus type 1 (HIV1) infection and AIDS have been shown to suppress the replication of HIV1 and extend the life expectancy of HIV1 infected individuals.
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Alternative names
- HIV-1 protease antibodyHuman immunodeficiency virus protease antibodyPR antibodyRetropepsin antibody
References for Anti-HIV protease antibody [1696] (ab8327)
This product has been referenced in:
- O'loughlin TL et al. Diversification and Specialization of HIV Protease Function During In Vitro Evolution. Mol Biol Evol 23:764-72 (2006). Read more (PubMed: 16423863) »
- Lescar J et al. Inhibition of the HIV-1 and HIV-2 proteases by a monoclonal antibody. Protein Sci 8:2686-96 (1999). Read more (PubMed: 10631984) »