Recombinant Human WAS Protein, N-GST & C-His

Description of Recombinant Human WAS Protein, N-GST & C-His

Introduction

Recombinant proteins have become essential tools in various fields of research, diagnostics and therapeutics. These proteins are produced by genetic engineering techniques, where the DNA sequence encoding for a particular protein is inserted into a host cell, allowing for large-scale production of the desired protein. One such recombinant protein is the Recombinant Human WAS Protein, which has gained significant attention for its structural and functional properties.

Structure of Recombinant Human WAS Protein

The Recombinant Human WAS Protein, also known as Wiskott-Aldrich syndrome protein, is a cytoplasmic protein that plays a crucial role in the regulation of actin cytoskeleton. It is encoded by the WAS gene located on the X chromosome. The protein is composed of 502 amino acids and has a molecular weight of approximately 55 kDa. It consists of multiple domains, including an N-terminal WH1 domain, a central proline-rich region, and a C-terminal verprolin homology, cofilin homology, and acidic (VCA) domain. These domains are responsible for the protein’s interaction with other proteins and its role in actin polymerization.

Activity of Recombinant Human WAS Protein

The primary function of Recombinant Human WAS Protein is to regulate the actin cytoskeleton, which is essential for various cellular processes such as cell shape, movement, and division. It does so by binding to actin monomers and promoting their polymerization into filaments. The WH1 domain of the protein binds to the proline-rich region of the WIP (WASP-interacting protein), which in turn binds to the actin monomers. This interaction leads to the activation of the VCA domain, which promotes actin polymerization. Additionally, the protein also interacts with various other proteins, including actin-binding proteins and signaling molecules, to regulate actin dynamics and cell motility.

Applications of Recombinant Human WAS Protein

Due to its crucial role in actin regulation, Recombinant Human WAS Protein has several applications in research, diagnostics, and therapeutics.

Research

The protein is widely used in research to study the mechanisms of actin dynamics and its role in various cellular processes. It is also used to investigate the pathophysiology of Wiskott-Aldrich syndrome, a rare genetic disorder caused by mutations in the WAS gene, which leads to a deficiency of the WAS protein.

Diagnostics

Defects in the WAS gene and subsequent deficiency of the WAS protein can result in Wiskott-Aldrich syndrome, which is characterized by immune system dysfunction, eczema, and low platelet counts. Recombinant Human WAS Protein is used in diagnostic tests to detect mutations in the WAS gene and diagnose this syndrome.

Therapeutics

Recombinant Human WAS Protein has shown potential as a therapeutic agent for Wiskott-Aldrich syndrome. Studies have demonstrated that the protein can improve platelet function and immune system function in patients with this syndrome. Additionally, it has also been investigated as a potential treatment for other disorders involving actin dysregulation, such as cancer and autoimmune diseases.

Conclusion

In summary, Recombinant Human WAS Protein is a crucial protein involved in the regulation of actin cytoskeleton. Its structural and functional properties make it a valuable tool in various fields of research, diagnostics, and therapeutics. With ongoing research and advancements in genetic engineering techniques, the potential of this protein in various applications is continuously expanding.