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
製品の詳細
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製品名
Recombinant HIV1 Protease protein
HIV1 Protease タンパク質・ペプチド 製品一覧 -
生理活性
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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精製度
> 95 % SDS-PAGE.
Purified by an affinity chromatography in combination with FPLC chromatography -
発現系
Escherichia coli -
タンパク質長
Full length protein -
Animal free
No -
由来
Recombinant -
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配列
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF -
予測される分子量
12 kDa -
領域
1 to 99 -
タグ
His tag C-Terminus
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関連製品
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Related Products
特性
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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アプリケーション
SDS-PAGE
Functional Studies
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製品の状態
Liquid -
Concentration information loading...
前処理および保存
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保存方法および安定性
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.
関連情報
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別名
- HIV-1 protease
プロトコール
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.
データシートおよび資料
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SDS download
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Datasheet download
参考文献 (3)
ab84117 は 3 報の論文で使用されています。
- 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