Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Tags: His tag C-Terminus
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant HIV1 Protease protein
See all HIV1 Protease proteins and peptides
One unit of HIV Protease hydrolyzes 1 picomole of a peptide (SQNYPIVQ) per minute at pH 4.7 at 25oC. 20-200ng is sufficient for an in vitro protease assay. HIV Protease can be applied in in vitro assay development and screening of protease inhibitors.
Purity> 95 % SDS-PAGE.
Purified by an affinity chromatography in combination with FPLC chromatography
Expression systemEscherichia coli
Protein lengthFull length protein
SequencePQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF
Predicted molecular weight12 kDa
Amino acids1 to 99
TagsHis tag C-Terminus
Our Abpromise guarantee covers the use of ab84117 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 3.75% Potassium chloride, 0.0154% DTT, 0.316% Tris HCl, 0.00584% EDTA, 20% Glycerol (glycerin, glycerine)
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- HIV-1 protease
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab84117 has been referenced in 2 publications.
- Imamura T et al. Isolation of amaranthin synthetase from Chenopodium quinoa and construction of an amaranthin production system using suspension-cultured tobacco BY-2 cells. Plant Biotechnol J 17:969-981 (2019). PubMed: 30451369
- Boso G et al. The nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase in viral particles. J Virol 89:1286-97 (2015). PubMed: 25392207