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This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene consists of three direct repeats of the ubiquit

This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene consists of three direct repeats of the ubiquit

PAI1 (plasminogen activator inhibitor 1) is originally cloned from human endothelial cell (Pannekoek 1986, Ginsburg 1986) and rat hepatoma cell 3 cDNA libraries. As a member of the serpin family of serine protease inhibitors, PAI1 inhibits both tissue type plasminogen activator (tPA) and urokinase type plasminogen activator (uPA). High PAI1 levels are associated with an increased risk of thromboembolic disease while PAI1 deficiency may represent an inherited autosomal recessive bleeding disor

PAI1 (plasminogen activator inhibitor 1) is originally cloned from human endothelial cell (Pannekoek 1986, Ginsburg 1986) and rat hepatoma cell 3 cDNA libraries. As a member of the serpin family of serine protease inhibitors, PAI1 inhibits both tissue type plasminogen activator (tPA) and urokinase type plasminogen activator (uPA). High PAI1 levels are associated with an increased risk of thromboembolic disease while PAI1 deficiency may represent an inherited autosomal recessive bleeding disor

PAI1 (plasminogen activator inhibitor 1) is originally cloned from human endothelial cell (Pannekoek 1986, Ginsburg 1986) and rat hepatoma cell 3 cDNA libraries. As a member of the serpin family of serine protease inhibitors, PAI1 inhibits both tissue type plasminogen activator (tPA) and urokinase type plasminogen activator (uPA). High PAI1 levels are associated with an increased risk of thromboembolic disease while PAI1 deficiency may represent an inherited autosomal recessive bleeding disor

This gene encodes tissue-type plasminogen activator, a secreted serine protease which converts the proenzyme plasminogen to plasmin, a fibrinolytic enzyme. Tissue-type plasminogen activator is synthesized as a single chain which is cleaved by plasmin to a two chain disulfide linked protein. This enzyme plays a role in cell migration and tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysis w