Uroporphyrinogen decarboxylase (UROD), is an enzyme of the heme biosynthetic pathway which belongs to the uroporphyrinogen decarboxylase family. This enzyme is responsible for catalyzing the conversion of uroporphyrinogen to coproporphyrinogen through the removal of four carboxymethyl side chains. UROD is a homodimeric enzyme that catalyzes the fifth step in heme biosynthesis: the elimination of carboxyl groups from the four acetate side chains of uroporphyrinogen III to yield coproporphyrinogen III. Defects in UROD are the cause of familial porphyria cutanea tarda (FPCT) and hepatoerythropoietic porphyria (HEP).
Recombinant Human Urokinase-Type Plasminogen Activator is a serine protease, which specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. Urokinase-Type Plasminogen Activator is a potent marker of invasion and metastasis in many human cancers associated with breast, colon, stomach, bladder, brain, ovary and endometrium. Human Urokinase-Type Plasminogen Activator is initially synthesized as 431 amino acid precursor with a N-terminal signal peptide residues. The single chain molecule is processed into a disulfide-linked two-chain molecule. There exists two forms A chain, the long A chain contains an EGF-like domain that is responsible for binding of the uPA receptor. The B chain corresponds to the catalytic domain.
Plasminogen activator, urokinase, also known as PLAU and uPA, is a serine protease which converts plasminogen to plasmin, a broad-spectrum protease active on extracellular matrix (ECM) components. It is involved in complement activation, cell migration, wound healing, and generation of localized extracellular proteolysis during tissue remodelling, pro-hormone conversion, carcinogenesis and neoplasia. 、uPA and its receptor (uPAR) have been implicated in a broad spectrum of pathophysiological processes, including fibrinolysis, proteolysis, inflammation, atherogenesis and plaque destabilization, all of which are involved in the pathogenesis of MI (myocardial infarction). The role of uPA is not only linked to its action as an enzyme. In fact, the mere binding of uPA on the cell surface also brings about two events that broaden the spectrum of its biological functions: (1) a conformational change of the receptor, which, in turn, affects its interaction with other proteins, (2) a signal transduction which modulates the expression of apoptosis-related genes. Besides its applications as a thrombolytic agent and as a prognostic marker for tumors, uPA may provide the basis for other therapies, as the structure of the receptor-binding domain of uPA has become a model for the design of anti-cancer molecules. Because of the causal involvment of uPA in cancer invasion and metastasis, the blockade of uPA interactions and activity with specific inhibitors is of interest for novel strategies in cancer therapy.
Uroplakin-2 is a single-pass type I membrane protein that belongs to the uroplakin-2 family. Uroplakin-2 is a component of the asymmetric unit membrane (AUM) and expressed in the ureter, a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. Uroplakin-2 forms heterodimer with UPK1A that is necessary for exiting out of the endoplasmic reticulum (ER). Uroplakin-2 may play an important role in regulating the assembly of the AUM. AUM is believed to strengthen the urothelium by preventing cell rupture during bladder distention.
Uroporphyrinogen-III Synthase is an enzyme which belongs to the uroporphyrinogen-III synthase family. Uroporphyrinogen-III Synthase is ubiquitous and it is involved in Porphyrin metabolism. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as Methionine synthesis (Vitamin B12) or oxygen transport (Heme). Uroporphyrinogen-III Synthase can catalyze cyclization of the linear Tetrapyrrole, Hydroxymethylbilane, to the Macrocyclic Uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of Porphyrins. Defects in Uroporphyrinogen-III Synthase are the cause of Congenital Erythropoietic Porphyria (CEP).
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