Recombinant Mouse PADI2 Protein, N-Strep

Description of Recombinant Mouse PADI2 Protein, N-Strep

Introduction

Recombinant proteins have become essential tools in various fields of research, including biotechnology, medicine, and drug development. One such protein is the Recombinant Mouse PADI2 Protein, which has gained attention due to its unique structure and diverse functions. In this article, we will discuss the structure, activity, and applications of this protein in detail.

Structure of Recombinant Mouse PADI2 Protein

PADI2 (Peptidylarginine deiminase 2) is a member of the PAD (Peptidylarginine deiminase) family of enzymes. It is a calcium-dependent enzyme that catalyzes the conversion of arginine residues to citrulline in proteins, a process known as citrullination. The recombinant form of PADI2 is produced by cloning and expressing the PADI2 gene in a suitable host, such as E. coli or mammalian cells.

The recombinant PADI2 protein consists of 663 amino acids with a molecular weight of approximately 74 kDa. It contains a conserved calcium-binding domain and two catalytic domains, which are critical for its enzymatic activity. The protein also has a nuclear localization signal, indicating its role in regulating gene expression.

Activity of Recombinant Mouse PADI2 Protein

The primary function of PADI2 is to catalyze the post-translational modification of arginine residues in proteins. This process plays a crucial role in various physiological and pathological processes, including gene expression, immune response, and inflammation. The recombinant PADI2 protein has been extensively studied for its activity, and it has been shown to exhibit similar catalytic properties as the native form of the protein.

The activity of recombinant PADI2 is regulated by calcium ions, which bind to the calcium-binding domain and promote the enzyme’s catalytic activity. The enzyme has a preference for specific substrates, including histones, keratins, and filaggrin, which are involved in various cellular processes. The citrullination of these proteins by PADI2 has been linked to the regulation of gene expression, cell differentiation, and immune response.

Applications of Recombinant Mouse PADI2 Protein

The recombinant PADI2 protein has a wide range of applications in both basic and applied research. Its ability to catalyze the citrullination of proteins has made it a valuable tool for studying the role of this post-translational modification in various biological processes. Some of the key applications of recombinant PADI2 protein are:

1. Studying the role of citrullination in gene expression

The recombinant PADI2 protein has been used to investigate the role of citrullination in regulating gene expression. It has been shown to citrullinate histones, which are involved in chromatin remodeling and transcriptional regulation. By studying the effects of PADI2-mediated citrullination on histones, researchers can gain insights into the mechanisms of gene expression.

2. Understanding the role of PADI2 in immune response

PADI2 has been implicated in various autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis. The recombinant PADI2 protein has been used to study its role in the immune response and its potential as a therapeutic target for these diseases.

3. Developing diagnostic tools for citrullinated proteins

Citrullinated proteins have been identified as potential biomarkers for various diseases, including cancer. The recombinant PADI2 protein has been used to generate citrullinated proteins in vitro, which can be used to develop diagnostic tools for these diseases.

4. Drug discovery and development

The unique structure and activity of PADI2 make it an attractive target for drug discovery and development. The recombinant form of the protein has been