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Reconstitute at 0.2 mg/mL in sterile PBS.
Plasminogen Kringle 5 is a domain within the plasminogen gene, which encodes the precursor to plasmin, an important enzyme involved in the breakdown of blood clots (fibrinolysis). The plasminogen protein contains multiple kringle domains, each contributing to its function. Kringle 5, in particular, has garnered interest due to its potent anti-angiogenic properties, meaning it can inhibit the formation of new blood vessels. This function is crucial in regulating processes such as wound healing, tissue regeneration, and the suppression of tumor growth, as tumors often rely on angiogenesis to obtain nutrients and grow. Kringle 5 exerts its effects by binding to specific receptors on endothelial cells, thereby inhibiting their proliferation and migration. This makes it a promising target for therapeutic strategies aimed at treating diseases characterized by excessive angiogenesis, such as cancer and certain eye diseases like diabetic retinopathy and age-related macular degeneration. Understanding the mechanisms of action and regulatory pathways involving Plasminogen Kringle 5 is essential for developing novel anti-angiogenic therapies and improving clinical outcomes in angiogenesis-related disorders.
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