Recombinant Human RUVBL2 Protein, N-His

Description of Recombinant Human RUVBL2 Protein, N-His

The Structure of Recombinant Human RUVBL2 Protein

Recombinant Human RUVBL2 Protein, also known as RuvB-like 2 protein, is a highly conserved member of the AAA+ (ATPases associated with diverse cellular activities) family of proteins. It is encoded by the RUVBL2 gene and is found in all eukaryotic organisms. The protein is composed of 465 amino acids and has a molecular weight of approximately 52 kDa.

The primary structure of Recombinant Human RUVBL2 Protein consists of three main domains: an N-terminal domain, a central AAA+ domain, and a C-terminal domain. The N-terminal domain is responsible for protein-protein interactions and contains a conserved arginine finger motif, which is important for ATP hydrolysis. The central AAA+ domain is the main catalytic domain and contains the characteristic Walker A and B motifs, which are essential for ATP binding and hydrolysis. The C-terminal domain is involved in protein-protein interactions and has been shown to play a role in the assembly of large protein complexes.

The Activity of Recombinant Human RUVBL2 Protein

Recombinant Human RUVBL2 Protein is a multifunctional protein with diverse activities in various cellular processes. It is primarily known for its role as a molecular chaperone, which assists in the proper folding of other proteins. It also acts as an ATPase, utilizing the energy from ATP hydrolysis to drive its various functions.

One of the key activities of Recombinant Human RUVBL2 Protein is its involvement in the assembly and remodeling of large protein complexes. It has been shown to interact with a variety of proteins, including transcription factors, chromatin remodelers, and DNA repair proteins, and facilitate their assembly into functional complexes. This activity is crucial for various cellular processes, such as DNA replication, transcription, and DNA repair.

Recombinant Human RUVBL2 Protein also plays a role in regulating gene expression. It has been shown to interact with transcription factors and co-activators, and modulate their activity. This function is important for maintaining proper gene expression and ensuring normal cellular function.

In addition, Recombinant Human RUVBL2 Protein has been implicated in cell cycle regulation. It interacts with key regulators of the cell cycle, such as cyclins and cyclin-dependent kinases, and is involved in the proper progression of the cell cycle. It has also been shown to play a role in cell proliferation and apoptosis.

The Application of Recombinant Human RUVBL2 Protein

Recombinant Human RUVBL2 Protein has a wide range of applications in both basic research and biotechnology. Its role as a molecular chaperone and its involvement in the assembly of large protein complexes make it a valuable tool for studying protein-protein interactions and protein complex assembly. It has been used in various in vitro assays to study the function of specific proteins and their interactions.

In the field of biotechnology, Recombinant Human RUVBL2 Protein has been used in the production of recombinant proteins. Its chaperone activity can aid in the proper folding and assembly of recombinant proteins, ensuring their functionality. It has also been used in the development of gene therapy and drug delivery systems, as it can interact with viral proteins and assist in their assembly.

Furthermore, Recombinant Human RUVBL2 Protein has been linked to various diseases and disorders, including cancer, neurodegenerative diseases, and developmental disorders. Its involvement in key cellular processes makes it a potential target for therapeutic interventions and a biomarker for disease diagnosis.

In conclusion, Recombinant Human RUVBL2 Protein is a highly versatile and important protein with a diverse range of activities and applications. Its structure and function make it a valuable tool for studying various cellular processes and its potential therapeutic applications make it a promising target for future research.