Recombinant HIV1 Protease protein is a Human immunodeficiency virus type 1 (BRU ISOLATE) Full Length protein, in the 501 to 599 aa range, expressed in Escherichia coli, with =95% purity and suitable for SDS-PAGE, FuncS, WB, ELISA, Dot.
P Q I T L W Q R P L V T I K I G G Q L K E A L L D T G A D D T V L E E M S L P G R W K P K M I G G I G G F I K V R Q Y D Q I L I E I C G H K A I G T V L V G P T P V N I I G R N L L T Q I G C T L N F
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application Dot | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). Matrix protein p17 targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). Capsid protein p24. Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding (By similarity). Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase. Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
Gag-Pol polyprotein, Pr160Gag-Pol, gag-pol
Recombinant HIV1 Protease protein is a Human immunodeficiency virus type 1 (BRU ISOLATE) Full Length protein, in the 501 to 599 aa range, expressed in Escherichia coli, with =95% purity and suitable for SDS-PAGE, FuncS, WB, ELISA, Dot.
pH: 6 - 8.5
Constituents: 10% Glycerol (glycerin, glycerine), 1.16% Sodium chloride, 0.39% MES, 0.24% Tris, 0.03% EDTA, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity).
Gag-Pol polyprotein
This product is an active protein and may elicit a biological response in vivo, handle with caution.
When necessary freezing (with liquid or ethanol in dry-ice) and thawing (in water at room temperature with shaking) should be done rapidly.
HIV-1 protease also called aspartyl protease is an enzyme vital for the life cycle of the HIV virus. It has a molecular mass of around 22 kilodaltons. This protease cleaves the viral polyprotein precursors generating mature protein components essential for a functional viral particle. HIV-1 protease is expressed in the cytoplasmic region of HIV-infected cells. Its unique structure with a symmetrical dimer makes it an attractive target for antiviral drugs.
HIV-1 protease functions to cleave the Gag and Gag-Pol polyprotein precursors into functional proteins. This proteolytic activity is essential in viral maturation and assembly transforming the virus into an infectious particle. HIV-1 protease does not form a complex with other proteins but operates independently to process numerous substrates within the viral lifecycle.
HIV-1 protease participates in the HIV replication pathway. It is important for the maturation process directly impacting the infectivity of the virus. The enzyme operates alongside other viral enzymes such as reverse transcriptase and integrase together facilitating the spread of the virus within the host. The integration of the protease activity in these pathways is necessary for the progression of the virus from a latent to an active state.
HIV-1 protease plays a central role in the progression of Human Immunodeficiency Virus (HIV) and subsequent development of Acquired Immunodeficiency Syndrome (AIDS). Inhibitors targeting HIV-1 protease such as saquinavir and ritonavir act to halt the maturation of the virus and reduce viral load in patients. Connections exist between HIV-1 protease and CD4 receptor proteins which are targets in the pathogenesis of HIV. Understanding and targeting this protease remain important strategies in HIV/AIDS treatment and management.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
ELISA of ab215523 using an anti-HIV protease antibody. Purified protease was spotted on wells.
SDS-PAGE analysis of ab215523.
Dot of ab215523. A anti-HIV-1 protease antibody was used at 1/2000 dilution, followed by a goat anti-rabbit IgG antibody conjugated with HRP secondary antibody at 1/5000 dilution.
Analysis of proteolytic processing of HIV-1 Gag p55 proprotein by ab215523 in vitro. Recombinant Gag p55 (1 μg) was used as the substrate in a 20 μl reaction volume. The reaction was carried by incubating at 37℃ for 3 h and stopped by adding sample buffer. 1; no protease, 2: 0.16 pg. 3; 1.6 pg. 4; 16 pg 5; 0.16 μg . 6; 1.6 μg ab215523. Note that two degradation bands are observed in the preparation of p55 substrate. In lane 4, p25 band is visible and in lane 5, p13 band is visible.
ab215523 as a control antigen for Western blot analysis.
All lanes: Anti HIV1 protease at 1/2000 dilution
Lane 1: Western blot - Recombinant HIV1 Protease protein (ab215523) at 0.001 µg
Lane 2: Extract of MT4 cells
Lane 3: Extract of MT4 cells infected with HIV-1 (LAI strain)
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com