Anti-Pin1 antibody [EP1479Y] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Pin1 also known as Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 is a small isomerase enzyme with a molecular weight of approximately 18 kDa. This protein is unique because of its specificity for phosphorylated serine/threonine-proline bonds. Pin1 catalyzes the cis-trans isomerization of these bonds with high efficiency. Expression of the Pin1 protein occurs widely across various tissues such as the brain heart and liver. It predominantly functions in the cytoplasm and nucleus where it modulates the activity of its target proteins by inducing conformational changes.

Biological function summary

Pin1 is essential in regulating cell cycle progression and cellular signaling. It influences a variety of cellular processes including cell proliferation transcriptional regulation and apoptosis. By altering the conformation of specific phosphorylated proteins Pin1 ensures the precise control of cell cycle checkpoints impacting the stability of many proteins such as cyclin D1 and p53. Despite not being part of a large protein complex Pin1 interacts with numerous other proteins thereby coordinating complex regulatory networks essential for maintaining normal cell function.

Pathways

Pin1 plays an important role in both the Wnt signaling pathway and the MAPK signaling pathway. In the Wnt pathway Pin1 maintains stability and the accumulation of β-catenin which affects transcription of target genes critical for cell proliferation. Within the MAPK pathway Pin1 regulates the activity of proteins like c-Jun and ERK1/2 which are vital for transmitting extracellular signals to cellular responses. Through these pathways Pin1 helps modulate responses to external stimuli and maintains cellular homeostasis by adjusting protein function dynamically in response to changes in phosphorylation status.

Associated diseases and disorders

Changes in Pin1 activity have been linked to cancer and Alzheimer's disease. In cancer increased Pin1 expression accelerates the degradation of tumor suppressor proteins like p53 contributing to uncontrolled cell proliferation and reduced apoptosis. In Alzheimer's disease Pin1 dysfunction leads to the accumulation of phosphorylated tau protein which forms neurofibrillary tangles and disrupts normal neuronal function. Through these connections Pin1 represents a potential therapeutic target for developing treatments aimed at restoring balance in these pathways and alleviating disease symptoms.