Recombinant Human Immunodeficiency Virus Type 2 Subtype A Protein Vpx (VPX) Protein (His)
Beta LifeScience
SKU/CAT #: BLC-04265P

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) vpx.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) vpx.
Recombinant Human Immunodeficiency Virus Type 2 Subtype A Protein Vpx (VPX) Protein (His)
Beta LifeScience
SKU/CAT #: BLC-04265P
Collections: High-quality recombinant proteins, Other recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Immunodeficiency Virus Type 2 Subtype A Protein Vpx (VPX) Protein (His) is produced by our E.coli expression system. This is a full length protein. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | P18099 |
Target Symbol | VPX |
Synonyms | vpxProtein Vpx; Viral protein X; X ORF protein |
Species | Human immunodeficiency virus type 2 subtype A (isolate BEN) (HIV-2) |
Expression System | E.coli |
Tag | N-6His |
Target Protein Sequence | MTDPRERVPPGNSGEETIGEAFEWLERTIEALNREAVNHLPRELIFQVWQRSWRYWHDEQGMSASYTKYRYLCLMQKAIFTHFKRGCTCWGEDMGREGLEDQGPPPPPPPGLV |
Expression Range | 1-113aa |
Protein Length | Full Length |
Mol. Weight | 17.2kDa |
Research Area | Others |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target Function | Plays a role in nuclear translocation of the viral pre-integration complex (PIC), thus is required for the virus to infect non-dividing cells. Targets specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity results in the degradation of host SAMHD1. In turn, SAMHD1 depletion allows viral replication in host myeloid cells by preventing SAMHD1-mediated hydrolysis of intracellular dNTPs necessary for reverse transcription. |
Subcellular Location | Virion. Host nucleus. |
Protein Families | Lentivirus VPX protein family |
Database References | KEGG: vg:1724714 |
Gene Functions References
- These results indicate that Vpx, in addition to SAMHD1, overcomes a previously unappreciated restriction for lentiviruses at the level of reverse transcription (RT)that acts independently of dNTP concentrations and is specific to resting CD4 T cells. PMID: 28228523
- zinc binding appears to mitigate flexibility of the three-helix fold of Vpx, thereby preventing dysfunction. PMID: 28284276
- Data indicate that proline residue P109 within the C-terminal poly-proline motif (PPM) of Vpx protein plays a unique role in the regulation of SAM domain and HD domain 1 protein SAMHD1 degradation. PMID: 25936766
- HIV-2 Vpr can trigger G2 cell cycle arrest through either CUL4A or CUL4B. PMID: 24719410
- Vpx expression results in decreased promoter binding activity of IRF5 PMID: 24532789
- Poly-proline motif in Vpx is critical for its efficient expression in cells. PMID: 24114794
- Data suggest that, in an evolutionary model of virus-host interactions, binding of Vpx/Vpr with SAMHD1 (and subsequent degradation of SAMHD1 [SAM domain/HD domain-containing protein 1]) exhibits dynamic requirements that have toggled back and forth. PMID: 23874202
- the crystal structure of a ternary complex of Vpx with the human E3 ligase substrate adaptor DCAF1 and the carboxy-terminal region of human SAMHD1 PMID: 24336198
- direct down-modulation of Vpx catalytic activity, mediated by the same binding event that leads to SAMHD1 recruitment to the E3 ubiquitin ligase for proteasome-dependent degradation PMID: 23677995
- Effective immune control of viral replication in HIV-2-infected individuals is not associated with increased Vpx-mediated degradation of SAMHD1. PMID: 23497283
- there are several Vpx residues required for SAMHD1 degradation PMID: 23076149
- The Vpx lentiviral accessory protein targets human SAMHD1 for degradation in the nucleus. PMID: 22973040
- Vpx targets SAMHD1 for degradation in a viral strategy to control cellular deoxynucleotide levels for efficient replication PMID: 22069334
- structure and cytopathogenic activity PMID: 16153874
- These studies map critical residues of the Vpx nuclear localization signal that are required for efficient infection of non-dividing cells. PMID: 16325220
- We found that insertion within the polyproline-containing C-terminus destabilizes nuclear localization, whereas mutating a second helix in the central domain disrupts viral packaging. PMID: 16457868
- results indicated that Vpx and Vpr of HIV-2 may cooperatively contribute to virion infectivity without affecting virion morphogenesis PMID: 16953064
- The results here clearly demonstrated that the entire Vpx protein is critical for reverse transcription of the HIV-2 genome in human monocyte-derived macrophages. PMID: 18495778
- when transferred in the context of a replication-competent viral clone, Vpx was required for replication in dendritic cells PMID: 18829761
- Vpx diverts the Cul4A-DDB1(DCAF1) ligase to inactivate an evolutionarily conserved factor, which restricts macrophage infection by HIV-2. PMID: 19264781