HIV-2 (subtype A, isolate BEN) Protein Vpx (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 17.2 kDa and the accession number is P18099.
パッケージサイズ | 在庫状況 | 単価(税別) |
---|---|---|
20 μg | 約20 days | ¥ 83,000 |
100 μg | 約20 days | ¥ 156,000 |
1 mg | 約20 days | ¥ 528,000 |
説明 | HIV-2 (subtype A, isolate BEN) Protein Vpx (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 17.2 kDa and the accession number is P18099. |
Species | HIV-2 |
Expression Host | E. coli |
Tag | N-6xHis |
Accession Number | P18099 |
Amino Acid | MTDPRERVPPGNSGEETIGEAFEWLERTIEALNREAVNHLPRELIFQVWQRSWRYWHDEQGMSASYTKYRYLCLMQKAIFTHFKRGCTCWGEDMGREGLEDQGPPPPPPPGLV |
Construction | 1-113 aa |
Protein Purity | > 90% as determined by SDS-PAGE. |
分子量 | 17.2 kDa (predicted) |
Formulation | Tris-based buffer, 50% glycerol |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage |
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping |
In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice. |
Research Background | 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. |
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