Recombinant Human IFT140 Protein, N-His

Description of Recombinant Human IFT140 Protein, N-His

Introduction

Recombinant Human IFT140 Protein, also known as intraflagellar transport protein 140, is a highly conserved protein that plays a critical role in the formation and maintenance of cilia, which are hair-like structures found on the surface of cells. Cilia are involved in various cellular processes such as cell signaling, movement, and sensing the environment. Defects in the IFT140 gene have been linked to a number of genetic disorders, highlighting the importance of this protein in human health. In this article, we will provide a detailed description of the structure, activity, and applications of Recombinant Human IFT140 Protein.

Structure of Recombinant Human IFT140 Protein

Recombinant Human IFT140 Protein is a large protein consisting of 1,437 amino acids. It belongs to the intraflagellar transport (IFT) protein family, which is involved in the transport of molecules within cilia. The protein is composed of multiple domains, including a coiled-coil domain, a WD40 repeat domain, and a C-terminal domain. The coiled-coil domain is responsible for protein-protein interactions, while the WD40 repeat domain is involved in the binding of other proteins and molecules. The C-terminal domain is essential for the proper localization of IFT140 to the base of cilia.

Activity of Recombinant Human IFT140 Protein

Recombinant Human IFT140 Protein is a key component of the IFT complex, which is responsible for the transport of materials between the base and tip of cilia. This process is crucial for the formation and maintenance of cilia. IFT140 forms a complex with other IFT proteins, including IFT122, IFT43, and IFT20, and together they form the IFT-A complex. This complex is involved in the retrograde movement of materials from the tip of cilia back to the base. It is also involved in the assembly and disassembly of cilia, which is necessary for ciliary function.

Applications of Recombinant Human IFT140 Protein

Recombinant Human IFT140 Protein has several important applications in both research and medicine. One of the main applications is in the study of cilia-related disorders. Mutations in the IFT140 gene have been linked to several genetic disorders, including Jeune syndrome, Mainzer-Saldino syndrome, and Sensenbrenner syndrome. These disorders are characterized by abnormal cilia formation and function, leading to a range of symptoms including skeletal abnormalities, kidney disease, and vision problems. Recombinant IFT140 protein can be used to study the effects of these mutations on cilia function and to develop potential treatments for these disorders.

Additionally, Recombinant Human IFT140 Protein has been used in various studies to understand the role of cilia in different cellular processes. For example, cilia have been shown to play a critical role in the development and maintenance of the central nervous system. Recombinant IFT140 protein has been used to study the function of cilia in the brain, which could lead to a better understanding of neurological disorders.

Furthermore, Recombinant Human IFT140 Protein has potential applications in the development of therapeutic interventions. As cilia play a crucial role in various cellular processes, targeting IFT140 could be a potential strategy for treating cilia-related disorders. Recombinant IFT140 protein can be used to screen for potential drugs that can modulate its activity, which could lead to the development of new treatments for these disorders.

Conclusion

In summary, Recombinant Human IFT140 Protein is a vital component of the IFT complex, which is essential for the formation and maintenance of cilia. Its structure and activity have been extensively studied, and it has important applications in the study of cilia-related disorders, understanding the role of cilia in different cellular processes, and the development of potential therapeutic interventions. Further research on Recombinant IFT140 protein could lead to a better understanding of cilia function and the development of