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ProteoGenix
Recombinant Proteins
Insect
Elisa, WB
Mouse Protein-arginine deiminase type-2 (PAD2) is a calcium-dependent enzyme that plays a crucial role in the post-translational modification of proteins by catalyzing the conversion of peptidyl-arginine to peptidyl-citrulline. This modification, known as citrullination, has been implicated in various physiological and pathological processes, making PAD2 an important drug target. The recombinant form of this enzyme, known as Mouse Recombinant Protein – GST-Tag, has been extensively studied and has shown promising results in various applications.
The crystal structure of Mouse Protein-arginine deiminase type-2 has been determined at a resolution of 2.2 Å. It consists of a catalytic core domain and two calcium-binding EF-hand domains. The catalytic core domain is composed of a beta-barrel structure with a central active site containing a zinc ion. The two EF-hand domains are located at the N-terminus and C-terminus of the catalytic core and are responsible for calcium binding, which is essential for the enzyme’s activity.
Mouse Protein-arginine deiminase type-2 is a highly specific enzyme that catalyzes the hydrolysis of peptidyl-arginine residues to form peptidyl-citrulline. This activity is dependent on the presence of calcium ions and is regulated by the concentration of calcium in the cellular environment. The enzyme has been shown to have a preference for large and flexible substrates, making it suitable for the post-translational modification of histones and other proteins with long unstructured regions.
The recombinant form of Mouse Protein-arginine deiminase type-2, known as Mouse Recombinant Protein – GST-Tag, has been used in various applications due to its high specificity and activity. Some of the key applications of this protein are listed below:
Citrullination, the modification catalyzed by PAD2, has been linked to several diseases, including rheumatoid arthritis, multiple sclerosis, and cancer. As a result, PAD2 has emerged as a potential drug target for these diseases. Mouse Recombinant Protein – GST-Tag has been used in drug discovery studies to screen for inhibitors of PAD2 activity. Inhibitors of this enzyme could potentially be developed into therapeutics for the treatment of citrullination-related diseases.
The ability of Mouse Recombinant Protein – GST-Tag to catalyze the conversion of peptidyl-arginine to peptidyl-citrulline has been utilized in the modification of proteins for various research purposes. This includes the generation of citrullinated proteins for use as antigens in autoimmune disease studies and the modification of histones for epigenetic research.
Citrullination of histones has been linked to the regulation of gene expression and has been implicated in various epigenetic processes. Mouse Recombinant Protein – GST-Tag has been used in studies to investigate the role of citrullination in epigenetic regulation. This includes the modification of histones in vitro and in vivo to study the impact of citrullination on gene expression and chromatin structure.
Mouse Recombinant Protein – GST-Tag has been used in studies to identify and characterize protein-protein interactions involving PAD2. This has provided insights into the role of this enzyme in various cellular processes and has aided in the understanding of its potential as a drug target.
The detection of citrullinated proteins has been used as a diagnostic tool for various diseases, including rheumatoid arthritis.
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