Recombinant Human USP22 Protein, N-His

Description of Recombinant Human USP22 Protein, N-His

Introduction to Recombinant Human USP22 Protein

Recombinant Human USP22 Protein, also known as Ubiquitin-Specific Protease 22, is a highly conserved enzyme that belongs to the deubiquitinating enzyme (DUB) family. This protein plays a crucial role in regulating various cellular processes, including transcriptional regulation, DNA damage response, and cell cycle progression. Recombinant Human USP22 Protein is produced through recombinant DNA technology and has been widely studied for its structure, activity, and potential applications.

Structure of Recombinant Human USP22 Protein

The gene encoding Recombinant Human USP22 Protein is located on chromosome 17 and consists of 18 exons. The protein itself is composed of 525 amino acids with a molecular weight of approximately 60 kDa. It contains a conserved catalytic domain, a zinc finger domain, and a ubiquitin-like domain. The catalytic domain is responsible for its deubiquitinating activity, while the zinc finger domain is involved in protein-protein interactions. The ubiquitin-like domain is thought to play a role in substrate recognition and binding.

Recombinant Human USP22 Protein is expressed in various tissues, with the highest levels found in the testes, ovaries, and brain. It is also found in both the cytoplasm and nucleus of cells, indicating its diverse functions in different cellular compartments.

Activity of Recombinant Human USP22 Protein

As a member of the DUB family, Recombinant Human USP22 Protein has the ability to remove ubiquitin molecules from target proteins. This process, known as deubiquitination, is crucial for maintaining proper protein turnover and stability. USP22 is known to interact with several other proteins, including transcription factors, chromatin modifiers, and DNA repair proteins, suggesting its involvement in multiple cellular pathways.

One of the key functions of Recombinant Human USP22 Protein is its role in transcriptional regulation. It has been shown to interact with various transcription factors, such as p53 and E2F1, and regulate their activity by deubiquitinating them. This activity can either activate or repress gene expression, depending on the target protein and cellular context.

Recombinant Human USP22 Protein also plays a crucial role in the DNA damage response. It has been shown to interact with and deubiquitinate several proteins involved in DNA repair, such as BRCA1 and RAD51. This suggests its involvement in maintaining genome stability and preventing the development of cancer.

Applications of Recombinant Human USP22 Protein

Due to its diverse functions and interactions with various proteins, Recombinant Human USP22 Protein has been studied for its potential applications in different fields. One of the most promising applications is in cancer research. USP22 has been found to be overexpressed in various types of cancer, and its inhibition has been shown to reduce tumor growth and sensitize cancer cells to chemotherapy.

Recombinant Human USP22 Protein has also been studied for its potential as a therapeutic target for other diseases, such as neurodegenerative disorders and viral infections. Its role in regulating transcription and protein stability makes it a promising target for drug development.

Additionally, Recombinant Human USP22 Protein has been used in biochemical and structural studies to understand its interactions with other proteins and its role in cellular pathways. Its recombinant production allows for large-scale purification, making it a valuable tool for research and drug discovery.

Conclusion

Recombinant Human USP22 Protein is a highly conserved enzyme with diverse functions in various cellular pathways. Its structure, activity, and potential applications have been extensively studied, and it holds great promise for future research and drug development. Its role in transcriptional regulation and DNA damage response make it a potential target