Recombinant Human USP1 Protein, N-His

Description of Recombinant Human USP1 Protein, N-His

Introduction

Recombinant Human USP1 Protein is a type of recombinant protein that has been produced through genetic engineering techniques. It is a highly purified and biologically active protein that has been extensively studied for its structure, activity and various applications in the field of biotechnology and medicine.

Structure of Recombinant Human USP1 Protein

The recombinant form of USP1 protein is a 74 kDa protein consisting of 622 amino acids. It belongs to the deubiquitinating enzyme family and contains a catalytic domain that is essential for its enzymatic activity. The protein also has a C-terminal domain that is responsible for its interaction with other proteins and plays a crucial role in its function.

Activity of Recombinant Human USP1 Protein

USP1 protein is a deubiquitinating enzyme that plays a vital role in the regulation of DNA damage response and repair. It is involved in the removal of ubiquitin molecules from various target proteins, thereby controlling their stability and function. USP1 has been found to specifically target and deubiquitinate several DNA repair proteins, including FANCD2 and PCNA, which are important for maintaining genomic stability.

Additionally, USP1 has been shown to interact with and regulate the activity of various other proteins involved in DNA damage response, such as ATR, CHK1, and RPA. This highlights the crucial role of USP1 in maintaining the integrity of the genome and preventing the development of diseases such as cancer.

Applications of Recombinant Human USP1 Protein

Recombinant Human USP1 Protein has a wide range of applications in both research and clinical settings. Its role in DNA damage response and repair makes it a valuable tool for studying the mechanisms of various diseases, particularly cancer. USP1 has been implicated in the development and progression of several types of cancer, making it a potential target for therapeutic interventions.

Moreover, the enzymatic activity of USP1 makes it a useful tool for protein purification and production. Recombinant USP1 protein can be used to remove ubiquitin tags from target proteins, thereby facilitating their purification and downstream applications.

Furthermore, USP1 has been shown to modulate the activity of certain proteins involved in immune response, making it a potential target for immunotherapy. The recombinant form of USP1 can be used to study its interactions with immune-related proteins and its role in regulating immune response.

Conclusion

In summary, Recombinant Human USP1 Protein is a highly purified and biologically active protein that plays a crucial role in DNA damage response and repair. Its structure, activity and various applications make it a valuable tool for studying diseases, protein purification, and immunotherapy. Further research on USP1 and its interactions with other proteins may lead to the development of novel therapeutic strategies for diseases such as cancer.