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

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

Introduction

Recombinant proteins have revolutionized the field of biotechnology, allowing for the production of large quantities of specific proteins for various applications. One such protein is Recombinant Human WAS Protein, which plays a critical role in the immune system. In this article, we will explore the structure, activity, and application of this important protein.

Structure of Recombinant Human WAS Protein

Recombinant Human WAS Protein is a 502 amino acid protein with a molecular weight of approximately 52 kDa. It is encoded by the Wiskott-Aldrich syndrome protein (WAS) gene, which is located on the X chromosome. The protein consists of several domains, including a GTPase-binding domain, a proline-rich domain, and a verprolin homology/cofilin homology (VCA) domain. These domains are essential for the protein’s function in actin cytoskeleton regulation.

The VCA domain of Recombinant Human WAS Protein is responsible for binding to the Arp2/3 complex, a key regulator of actin polymerization. This interaction allows for the activation of the Arp2/3 complex, leading to the formation of new actin filaments. The proline-rich domain of the protein is involved in protein-protein interactions, while the GTPase-binding domain is responsible for binding to small GTPases, such as Cdc42 and Rac1, which are also involved in actin regulation.

Activity of Recombinant Human WAS Protein

The primary function of Recombinant Human WAS Protein is to regulate the actin cytoskeleton, which is essential for a variety of cellular processes, including cell motility, cell shape, and cell division. The protein does this by activating the Arp2/3 complex, which promotes the formation of branched actin networks. These networks are crucial for cell movement and the formation of specialized structures, such as filopodia and lamellipodia.

In addition to its role in actin regulation, Recombinant Human WAS Protein also plays a crucial role in the immune system. It is primarily expressed in hematopoietic cells, including T cells, B cells, and natural killer cells. The protein is involved in the formation of immunological synapses, which are crucial for the activation and function of immune cells. Defects in the WAS gene can lead to Wiskott-Aldrich syndrome, a rare X-linked immunodeficiency disorder characterized by recurrent infections, eczema, and thrombocytopenia.

Application of Recombinant Human WAS Protein

Recombinant Human WAS Protein has diverse applications in both research and clinical settings. In research, the protein is used to study actin cytoskeleton regulation and its role in various cellular processes. It is also used to investigate the mechanisms of Wiskott-Aldrich syndrome and other immunodeficiency disorders.

In clinical settings, Recombinant Human WAS Protein has shown potential as a therapeutic agent for Wiskott-Aldrich syndrome. Studies have shown that the protein can improve the function of immune cells and reduce the severity of symptoms in patients with this disorder. Additionally, the protein has been used in gene therapy approaches to treat Wiskott-Aldrich syndrome by introducing functional WAS gene into affected cells.

Furthermore, Recombinant Human WAS Protein has been used in the development of vaccines and immunotherapies. The protein’s ability to regulate the immune response and form immunological synapses makes it a promising candidate for enhancing vaccine efficacy and improving immune responses against cancer and infectious diseases.

Conclusion

In conclusion, Recombinant Human WAS Protein is a crucial protein involved in actin cytoskeleton regulation and immune system function. Its diverse applications in research and clinical settings make it