Recombinant HIV-1 Protease

Référence B2011380

Conditionnement : 5ug

Marque : Molecular Depot

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Recombinant HIV-1 Protease

Catalog Number: B2011380 (5 µg)
Recombinant HIV-1 Protease is a high quality recombinant HIV-1 protease. This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

SKU: B2011380 Categories: Cell Biology, Proteins Tag: MD 1000

Product Description

4.8/5 - (6 votes)

Recombinant HIV-1 Protease
Catalog number: B2011380
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 5 µg
Molecular Weight or Concentration: 0.2 mg/mL
Supplied as: Solution
Applications: molecular tool for various biochemical applications
Storage: -80 °C
Keywords: HIV-1 protease, recombinant
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Eche S, Gordon ML. Recombinant expression of HIV-1 protease using soluble fusion tags in Escherichia coli: A vital tool for functional characterization of HIV-1 protease Virus Res. 2021 Apr 2;295:198289.
2: Azarnezhad A, Sharifi Z, Seyedabadi R, Hosseini A, Johari B, Sobhani Fard M. Cloning and Expression of Soluble Recombinant HIV-1 CRF35 Protease-HP Thioredoxin Fusion Protein Avicenna J Med Biotechnol. 2016 Oct-Dec;8(4):175-181.
3: Maseko SB, Govender D, Govender T, Naicker T, Lin J, Maguire GEM, Kruger HG. Optimized Procedure for Recovering HIV-1 Protease (C-SA) from Inclusion Bodies Protein J. 2019 Feb;38(1):30-36.
4: Miczi M, Diós Á, Bozóki B, Tőzsér J, Mótyán JA. Development of a Bio-Layer Interferometry-Based Protease Assay Using HIV-1 Protease as a Model Viruses. 2021 Jun 21;13(6):1183.
5: Mótyán JA, Miczi M, Oroszlan S, Tőzsér J. Specificity of the HIV-1 Protease on Substrates Representing the Cleavage Site in the Proximal Zinc-Finger of HIV-1 Nucleocapsid Protein Viruses. 2021 Jun 8;13(6):1092.
6: Eche S, Kumar A, Sonela N, Gordon ML. Acquired HIV-1 Protease Conformational Flexibility Associated with Lopinavir Failure May Shape the Outcome of Darunavir Therapy after Antiretroviral Therapy Switch Biomolecules. 2021 Mar 24;11(4):489.
7: Saladini F, Giannini A, Boccuto A, Vicenti I, Zazzi M. Agreement between an in-house replication competent and a reference replication defective recombinant virus assay for measuring phenotypic resistance to HIV-1 protease, reverse transcriptase, and integrase inhibitors J Clin Lab Anal. 2018 Jan;32(1):e22206.
8: El Moussi A, Thomson MM, Delgado E, Cuevas MT, Nasr M, Abid S, Ben Hadj Kacem MA, Benaissa Tiouiri H, Letaief A, Chakroun M, Ben Jemaa M, Hamdouni H, Tej Dellagi R, Kheireddine K, Boutiba I, Pérez-Álvarez L, Slim A. Genetic Diversity of HIV-1 in Tunisia AIDS Res Hum Retroviruses. 2017 Jan;33(1):77-81.
9: Puertas MC, Buzón MJ, Ballestero M, Van Den Eede P, Clotet B, Prado JG, Martinez-Picado J. Novel two-round phenotypic assay for protease inhibitor susceptibility testing of recombinant and primary HIV-1 isolates J Clin Microbiol. 2012 Dec;50(12):3909-16.
10: Volontè F, Piubelli L, Pollegioni L. Optimizing HIV-1 protease production in Escherichia coli as fusion protein Microb Cell Fact. 2011 Jun 30;10:53.

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Additional Information

Weight 0.15 oz
Dimensions 2 × 0.5 × 0.5 in