Catalog number: 223 - 40-441-0002mg
Product Category: Business & Industrial > Science & Laboratory
Size: 0.002 mg
91-190
beta -Ureidopropionase is a cytoplasmic protein which belongs to the CN hydrolase family of BUP subfamily. beta -Ureidopropionase binds one zinc ion per subunit, catalyzes the last step in the pyrimidine degradation pathway. beta -Ureidopropionase can convert N-carbamyl-beta-aminoisobutyric acid and N-carbamyl-beta-alanine to beta-aminoisobutyric acid and beta-alanine, ammonia and carbon dioxide, respectively. The pyrimidine bases uracil and thymine are degraded via the consecutive action of dihydropyrimidine dehydrogenase (DHPDH), dihydropyrimidinase (DHP) and beta-ureidopropionase (UP) to beta-alanine and beta aminoisobutyric acid, respectively. Defects in beta -Ureidopropionase are the cause of beta -Ureidopropionase deficiency that is characterized by muscular hypotonia, dystonic movements, scoliosis, microcephaly and severe developmental delay.
91-225
Oncomodulin-1 (OM) is a small, calcium-binding protein and a macrophage-derived growth factor, which can promote axon regeneration in retinal ganglion cells. Oncomodulin-1 is constitutively secreted by activated macrophages in the vitreous and retina in response to inflammatory conditions that promote optic nerve regeneration. Oncomodulin-1 binds RGCs with high affinity in vitro, but only when cAMP is pharmacologically elevated or if the membrane is permeabilized allowing Oncomodulin-1 access to the cytosolic compartment. Oncomodulin-1 is a member of the superfamily of calmodulin proteins and is a high-affinity calcium ion-binding protein and contains 2 EF-hand domains. OM is found in early embryonic cells in the placenta and also in tumors. It has some calmodulin-like activity with respect to enzyme activation and growth regulation.
91-229
Phosphomannomutase 1 (PMM1) blongs to the eukaryotic PMM family. Phosphomannomutase 1 can catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose which required for a number of critical mannosyl transfer reactions. PMM1 is highly expressed in liver, heart, brain, and pancreas, but lower expression in skeletal muscle. In addition, PMM1 may be responsible for the degradation of glucose-1,6 bisphosphate in ischemic brain.
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Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via β-catenin mediated Pdgfrα and E-cadherin expression.
96-237
Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via β-catenin mediated Pdgfrα and E-cadherin expression.
96-289
Fatty acid-binding protein 1 (FABP1) is also known as Fatty acid-binding protein, liver (FABPL), Liver-type fatty acid-binding protein (L-FABP). FABP1 / FABPL belongs to the calycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP1 / L-FABP binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. FABP-1 may be involved in intracellular lipid transport.