Human PARP1 Recombinant Protein

Description of Human PARP1 Recombinant Protein

The Structure of Human PARP1 Recombinant Protein

Human PARP1 (Poly ADP-ribose polymerase 1) is a nuclear enzyme that plays a crucial role in DNA repair and regulation of gene expression. It is a 113 kDa protein consisting of 1014 amino acids and is encoded by the PARP1 gene located on chromosome 1. The protein contains three main domains: a DNA binding domain, an automodification domain, and a catalytic domain. The DNA binding domain is responsible for recognizing and binding to damaged DNA, while the automodification domain is involved in the regulation of PARP1 activity. The catalytic domain, also known as the PARP homology domain, is responsible for the enzymatic activity of PARP1.

The Activity of this protein

Human PARP1 is a highly active enzyme that plays a crucial role in DNA repair. When DNA is damaged, PARP1 is activated and binds to the damaged site, where it catalyzes the transfer of ADP-ribose units from NAD+ to a variety of acceptor proteins, including itself. This process, known as poly ADP-ribosylation, results in the formation of long chains of ADP-ribose on the acceptor proteins, which serves as a signal for DNA repair enzymes to be recruited to the site of damage. This allows for efficient and accurate repair of DNA damage, preventing the accumulation of mutations and maintaining genomic stability.

In addition to its role in DNA repair, PARP1 also has other important functions. It is involved in the regulation of gene expression, where it can modify transcription factors and chromatin-associated proteins, influencing the transcription of specific genes. PARP1 also plays a role in cell death, where it can promote cell survival or trigger cell death depending on the cellular context.

The Application of Human PARP1 Recombinant Protein

Given its crucial role in DNA repair and other cellular processes, PARP1 has emerged as a promising drug target for various diseases. In particular, PARP1 inhibitors have been developed as potential therapeutics for cancer treatment. Cancer cells often have defects in DNA repair mechanisms, making them more reliant on PARP1 for survival. By inhibiting PARP1, cancer cells are unable to efficiently repair DNA damage, leading to cell death. Several PARP1 inhibitors, such as olaparib and rucaparib, have been approved for the treatment of certain types of ovarian and breast cancer.

PARP1 has also been implicated in various other diseases, including neurodegenerative disorders, cardiovascular diseases, and inflammatory disorders. In these conditions, PARP1 is believed to contribute to disease progression by promoting DNA damage and inflammation. Therefore, PARP1 inhibitors are being investigated as potential treatments for these diseases.

In addition to its potential as a drug target, Human PARP1 Recombinant Protein also has applications in research and diagnostics. The protein can be used in biochemical assays to study PARP1 activity and its role in DNA repair and other cellular processes. It can also be used to develop diagnostic tests for diseases associated with PARP1 dysfunction.

In conclusion, Human PARP1 Recombinant Protein is a crucial enzyme with diverse functions in DNA repair, gene expression, and cell death. Its structure and activity make it a promising drug target for various diseases, and it also has applications in research and diagnostics. Continued research on this protein and its inhibitors will further our understanding of its role in disease and may lead to the development of new and effective treatments.