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.
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.
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
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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

Gene Functions References

  1. 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
  2. zinc binding appears to mitigate flexibility of the three-helix fold of Vpx, thereby preventing dysfunction. PMID: 28284276
  3. 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
  4. HIV-2 Vpr can trigger G2 cell cycle arrest through either CUL4A or CUL4B. PMID: 24719410
  5. Vpx expression results in decreased promoter binding activity of IRF5 PMID: 24532789
  6. Poly-proline motif in Vpx is critical for its efficient expression in cells. PMID: 24114794
  7. 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
  8. 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
  9. 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
  10. Effective immune control of viral replication in HIV-2-infected individuals is not associated with increased Vpx-mediated degradation of SAMHD1. PMID: 23497283
  11. there are several Vpx residues required for SAMHD1 degradation PMID: 23076149
  12. The Vpx lentiviral accessory protein targets human SAMHD1 for degradation in the nucleus. PMID: 22973040
  13. Vpx targets SAMHD1 for degradation in a viral strategy to control cellular deoxynucleotide levels for efficient replication PMID: 22069334
  14. structure and cytopathogenic activity PMID: 16153874
  15. These studies map critical residues of the Vpx nuclear localization signal that are required for efficient infection of non-dividing cells. PMID: 16325220
  16. 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
  17. results indicated that Vpx and Vpr of HIV-2 may cooperatively contribute to virion infectivity without affecting virion morphogenesis PMID: 16953064
  18. 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
  19. when transferred in the context of a replication-competent viral clone, Vpx was required for replication in dendritic cells PMID: 18829761
  20. Vpx diverts the Cul4A-DDB1(DCAF1) ligase to inactivate an evolutionarily conserved factor, which restricts macrophage infection by HIV-2. PMID: 19264781

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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