Recombinant Human NPEPPS/PSA, N-His

Description of Recombinant Human NPEPPS/PSA, N-His

Recombinant human NPEPPS/PSA (Nuclear Protein Enzyme Peptidase with Plasminogen Activator Activity) is a type II transmembrane protein that belongs to the peptidase M16 family. It is also known as prostate-specific antigen (PSA) due to its high expression in the prostate gland. This protein is encoded by the NPEPPS gene and is expressed in various tissues, including the prostate, brain, and kidney.

Recombinant human NPEPPS/PSA is a 354 amino acid protein with a molecular weight of approximately 40 kDa. It contains a signal peptide, a propeptide, a catalytic domain, and a transmembrane domain. The catalytic domain is responsible for the peptidase activity of NPEPPS, while the transmembrane domain anchors the protein to the cell membrane.

Recombinant human NPEPPS/PSA is a zinc-dependent metalloprotease that cleaves peptide bonds in proteins. It has been found to have both exopeptidase and endopeptidase activities. NPEPPS can cleave a variety of substrates, including plasminogen, insulin-like growth factor binding protein-3, and amyloid precursor protein. It has also been shown to have a role in the degradation of extracellular matrix proteins, suggesting its involvement in tissue remodeling.

One of the most well-known activities of NPEPPS is its role in the activation of plasminogen. Plasminogen is a precursor of the serine protease plasmin, which is involved in fibrinolysis and extracellular matrix degradation. NPEPPS cleaves plasminogen at specific sites, leading to the formation of active plasmin. This activity of NPEPPS is particularly important in the prostate, where it contributes to the liquefaction of semen.

Recombinant human NPEPPS/PSA has been widely used as an antigen in diagnostic tests for prostate cancer. PSA levels in the blood are commonly measured as a screening tool for prostate cancer, as elevated levels of PSA can indicate the presence of the disease. Recombinant NPEPPS is used as a standard in these tests to ensure accurate and consistent results.

In addition to its diagnostic applications, recombinant human NPEPPS/PSA has also been studied as a potential therapeutic target. It has been found to be overexpressed in various types of cancer, including prostate, breast, and ovarian cancer. Inhibiting the activity of NPEPPS has been shown to reduce tumor growth and metastasis in animal models, making it a potential target for cancer treatment.

Furthermore, NPEPPS has been shown to play a role in various physiological processes, such as immune response and blood pressure regulation. Its involvement in these processes makes it a potential target for the development of treatments for diseases such as autoimmune disorders and hypertension.

In summary, recombinant human NPEPPS/PSA is a zinc-dependent metalloprotease with both exopeptidase and endopeptidase activities. It is involved in the activation of plasminogen and has a role in tissue remodeling. Its high expression in the prostate makes it a useful antigen in diagnostic tests for prostate cancer. Additionally, NPEPPS has potential therapeutic applications in cancer treatment and other diseases. Further research on this protein may uncover new insights into its functions and potential therapeutic uses.