Recombinant Human UROS protein is a Human protein, in the 1 to 265 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
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Catalyzes 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 (PubMed:11689424, PubMed:18004775). 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, UROIIIS, UROS, Hydroxymethylbilane hydrolyase [cyclizing], Uroporphyrinogen-III cosynthase
Recombinant Human UROS protein is a Human protein, in the 1 to 265 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl
ab107136 is purified using conventional chromatography techniques.
Catalyzes 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 (PubMed:11689424, PubMed:18004775). 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).
Belongs to the uroporphyrinogen-III synthase family.
Uroporphyrinogen III synthase commonly known as UROS is an enzyme involved in heme biosynthesis. It catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III facilitating a ring closure and isomerization. UROS has a molecular mass of approximately 29 kDa. It is predominantly expressed in the liver bone marrow and erythroid tissues where heme production is essential. The enzyme is vital for maintaining proper levels of porphyrins in cells and ensuring the biosynthesis of heme an important component of hemoglobin.
Uroporphyrinogen III synthase plays a role in heme production converting linear tetrapyrroles into the cyclic form needed for biosynthesis. This enzyme does not function as part of a larger complex but rather works independently to catalyze its specific reaction in porphyrin metabolism. Proper function of UROS is necessary to sustain the production of heme which is critical not only for oxygen transport in the blood but also for other heme-dependent processes in various tissues.
UROS is an essential component of the heme biosynthesis pathway. In this pathway it acts between the steps that involve hydroxymethylbilane synthase (HMBS) and uroporphyrinogen III decarboxylase (UROD). This metabolic pathway is important for the production of heme which is a core component of hemoglobin. HMBS synthesizes the precursor transformed by UROS while UROD further modifies the product of UROS to continue the biosynthesis process emphasizing the enzyme's importance in maintaining the heme biosynthesis pathway's integrity.
Mutations or deficiencies in UROS are linked to a rare inherited condition called congenital erythropoietic porphyria (CEP) also known as Günther's disease. This disorder results from the accumulation of porphyrins owing to impaired heme biosynthesis. Abnormal function in UROS leads to a buildup of its substrates causing severe skin photosensitivity and hemolytic anemia among other symptoms. The functional relationship between UROS and HMBS or UROD in the heme biosynthesis pathway illustrates the enzyme's significant role in preventing the development of such heme-related disorders.
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15% SDS-PAGE showing ab107136 (3μg).
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