HIV-2 Protease

HIV-2 Protease Recombinant
Cat. No.
BT24490
Source
Escherichia Coli.
Synonyms
Appearance
Sterile filtered colorless clear solution.
Purity
Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

HIV-2 protease is an active homodimer having a molecular mass of 10.7kDa.

Product Specs

Introduction
HIV-2 protease plays a crucial role in the HIV life cycle. It is produced within infected cells as part of the Gag-Pol polyprotein. Once an immature viral particle forms, HIV-2 protease auto-catalytically cleaves itself from the polyprotein. The enzyme then proceeds to cleave other components of viral polyproteins, which is essential for viral maturation. The enzyme undergoes significant mutagenesis in HIV-infected individuals. This leads to the emergence of drug-resistant mutants due to the selective pressure exerted by antiviral therapies.
Description
HIV-2 protease is a functional homodimer with a molecular weight of 10.7kDa.
Physical Appearance
The product is a clear, colorless solution that has been sterilized through filtration.
Formulation
This HIV-2 Protease solution (0.25mg/ml) is supplied in a buffer consisting of 20mM Tris pH 7.0, 20mM MES, 200mM NaCl, 1mM EDTA, 0.5mM DTT, 0.05% PEG 8000, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial at 4°C. For long-term storage, store the product frozen at -20°C. Repeated freeze-thaw cycles should be avoided.
Source
Escherichia Coli.
Storage Buffer
20mM HEPES, pH7.0 and 10% Glycerol.
Kinetic Parameters
Km=740µM, Kcat = 30s-1, Kcat/Km=4.1mM-1s-1 with peptide substrate ATLNFPISPW.

Product Science Overview

Introduction

Human Immunodeficiency Virus (HIV) is a retrovirus that causes Acquired Immunodeficiency Syndrome (AIDS). There are two main types of HIV: HIV-1 and HIV-2. While HIV-1 is more prevalent globally, HIV-2 is primarily found in West Africa. Both types of HIV have similar modes of transmission and clinical manifestations, but HIV-2 progresses more slowly and is less transmissible than HIV-1.

HIV-2 Protease

HIV-2 protease is an enzyme crucial for the maturation and replication of the virus. Proteases are enzymes that cleave peptide bonds in proteins, and the HIV-2 protease specifically cleaves the viral polyprotein precursors into functional proteins necessary for the assembly of new virions. This process is essential for the virus to become infectious.

Recombinant HIV-2 Protease

Recombinant HIV-2 protease refers to the enzyme produced through recombinant DNA technology. This involves inserting the gene encoding the HIV-2 protease into a host organism, such as bacteria, to produce the enzyme in large quantities. The recombinant form of the enzyme is used extensively in research to study its structure, function, and interactions with potential inhibitors.

Structural Insights

The structure of HIV-2 protease has been extensively studied to understand its catalytic mechanism and to develop inhibitors that can block its activity. The enzyme is a homodimer, meaning it consists of two identical subunits. Each subunit contributes to the formation of the active site, where substrate cleavage occurs. The active site contains two aspartic acid residues that are critical for the enzyme’s catalytic activity .

Drug Development

The study of HIV-2 protease has been instrumental in the development of antiretroviral drugs. Protease inhibitors are a class of antiretroviral drugs that specifically target the protease enzyme, preventing it from cleaving the viral polyproteins. This inhibition results in the production of immature, non-infectious viral particles. The development of protease inhibitors has significantly improved the treatment of HIV/AIDS .

Challenges and Future Directions

One of the major challenges in targeting HIV-2 protease is the development of drug resistance. The high mutation rate of HIV allows it to rapidly evolve and develop resistance to protease inhibitors. Ongoing research aims to develop new inhibitors that are effective against resistant strains of the virus. Additionally, structural studies of the protease continue to provide insights into its function and potential vulnerabilities that can be targeted by new drugs .

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