Recombinant HIV1 Protease protein (ab84117)
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
Description
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Product name
Recombinant HIV1 Protease protein
See all HIV1 Protease proteins and peptides -
Biological activity
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.
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Purity
> 95 % SDS-PAGE.
Purified by an affinity chromatography in combination with FPLC chromatography -
Expression system
Escherichia coli -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Sequence
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF -
Predicted molecular weight
12 kDa -
Amino acids
1 to 99 -
Tags
His tag C-Terminus
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Associated products
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Related Products
Specifications
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.
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Applications
SDS-PAGE
Functional Studies
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.9
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.
General Info
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Alternative names
- HIV-1 protease
Protocols
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.
Datasheets and documents
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SDS download
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Datasheet download
References (3)
ab84117 has been referenced in 3 publications.
- Borberg E et al. Ultrafast one-minute electronic detection of SARS-CoV-2 infection by 3CLpro enzymatic activity in untreated saliva samples. Nat Commun 13:6375 (2022). PubMed: 36289211
- 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