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AntibodySystem
Recombinant Proteins
Recombinant Human PIN1 Protein, also known as Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, is a highly conserved enzyme that plays a crucial role in regulating cell cycle progression and cellular signaling pathways. PIN1 is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, which catalyzes the cis-trans isomerization of proline residues in proteins, thereby regulating their conformation and function.
Recombinant Human PIN1 Protein is a 163 amino acid protein with a molecular weight of approximately 18 kDa. It consists of two domains, an N-terminal WW domain and a C-terminal PPIase domain. The WW domain is responsible for binding to phosphorylated serine/threonine-proline motifs in target proteins, while the PPIase domain catalyzes the isomerization of proline residues.
The crystal structure of Recombinant Human PIN1 Protein has been extensively studied, revealing a unique conformation with a twisted beta-sheet structure in the WW domain and a catalytic site in the PPIase domain. This structure allows PIN1 to interact with a wide range of target proteins and regulate their function through conformational changes.
Recombinant Human PIN1 Protein is a key regulator of cell cycle progression and cellular signaling pathways. It is involved in a variety of cellular processes, including DNA damage repair, transcriptional regulation, and apoptosis. PIN1 achieves its regulatory function by binding to and isomerizing specific proline residues in target proteins, thereby altering their conformation and activity.
One of the most well-studied targets of PIN1 is the tumor suppressor protein p53. PIN1 binds to phosphorylated serine-proline motifs in p53 and induces a conformational change that enhances its stability and transcriptional activity. This ultimately leads to increased expression of p53 target genes involved in cell cycle arrest and apoptosis, thus promoting tumor suppression.
Due to its crucial role in regulating cellular processes, Recombinant Human PIN1 Protein has been extensively studied and has potential applications in various fields.
In cancer research, PIN1 has been identified as a potential therapeutic target for various types of cancer, as its overexpression has been linked to increased tumor growth and progression. Inhibitors of PIN1 have been developed and are being investigated for their potential in cancer treatment.
Recombinant Human PIN1 Protein has also been studied in the context of neurodegenerative diseases. It has been shown to interact with and regulate the activity of proteins involved in Alzheimer’s disease, such as tau and amyloid beta, suggesting a potential role in disease pathogenesis. Furthermore, PIN1 has been proposed as a biomarker for Alzheimer’s disease, as its levels have been found to be altered in patients with the disease.
In addition, PIN1 has been implicated in other diseases and disorders, such as cardiovascular diseases, viral infections, and autoimmune disorders. Its role in regulating immune responses and inflammation makes it a potential target for therapeutic intervention in these conditions.
Recombinant Human PIN1 Protein is a highly conserved enzyme with a crucial role in regulating cell cycle progression and cellular signaling pathways. Its unique structure and activity make it an important target for research in various fields, including cancer, neurodegenerative diseases, and immune disorders. Further studies and developments in understanding the function and regulation of PIN1 may lead to potential therapeutic interventions for these diseases.
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