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The protein encoded by UGDH converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. Additionally we are shipping UGDH Proteins (16) and UGDH Kits (6) and many more products for this protein.
Showing 10 out of 70 products:
Human Polyclonal UGDH Primary Antibody for EIA, IHC (p) - ABIN955441
Wang, Pan, Fu, Chang: Down-regulation of UDP-glucose dehydrogenase affects glycosaminoglycans synthesis and motility in HCT-8 colorectal carcinoma cells. in Experimental cell research 2010
Show all 4 references for ABIN955441
Human Polyclonal UGDH Primary Antibody for IHC (p), WB - ABIN656544
Huang, Casale, Tian, Lele, Pisarev, Simpson, Hemstreet: Udp-glucose dehydrogenase as a novel field-specific candidate biomarker of prostate cancer. in International journal of cancer. Journal international du cancer 2009
UDP-glucose dehydrogenase has a role in hyaluronan synthesis
UGDH protein level in osteoarthritis cartilage was much lower than in control cartilage.
UGDH displays hysteresis because of a slow isomerization from an inactive state (E*) to an active state (E). We show that the structure of E* constrains UGDH in a conformation that favors feedback inhibition at physiological pH.
Kinetic analysis of wild-type UGDH and hexamer T325A showed that upon increasing enzyme concentration, which favors the hexameric species, activity was decreased and exhibited cooperativity. Cooperative kinetics was not observed in obligate dimer T325D.
Mammalian UGDH displays hysteresis (observed as a lag (show STMN1 Antibodies) in progress curves), indicating that the enzyme undergoes a slow transition from an inactive to an active state. Human UGDH is sensitive to product inhibition during the lag (show STMN1 Antibodies).
both missense mutations significantly reducing the ability of UGDH to provide precursors for cardiac cushion formation, which is essential to subsequent valve formation.
Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates.
An alternate crystal structure of human UGDH (hUGDH) in complex with UDP-glucose (show UGCG Antibodies) at 2.8 A resolution, is reported.
A structurally detailed model of UDP-alpha-D-glucose 6-dehydrogenase (UGDH) demonstrates hinge-bending motion that represents allosteric feedback inhibition and substrate-product exchange during the catalytic cycle.
high UGDH levels may underlie susceptibility of the orbit to localized overproduction of hyaluronan in Graves disease.
Structure and mechanism of human UDP-glucose 6-dehydrogenase.
Six proteins were regulated at both basal and inducible levels exhibiting the largest dynamic range of Nrf2 (show NFE2L2 Antibodies) regulation: cytochrome CYP2A5, GSTM3 (show glutathione S-transferase mu 3 (brain) Antibodies), GSTM1 (show GSTM1 Antibodies), ENTPD5 (show ENTPD5 Antibodies),UDPGDH, and EPHX1 (show EPHX1 Antibodies).
The protein encoded by this gene converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated compounds are common components of the extracellular matrix and likely play roles in signal transduction, cell migration, and cancer growth and metastasis. The expression of this gene is up-regulated by transforming growth factor beta and down-regulated by hypoxia. Alternative splicing results in multiple transcript variants.
, UDP-glucose 6-dehydrogenase
, UDP-glucose dehydrogenase
, distal W5.4 group XIII
, UDP-glucose dehydrogenase b
, UDP-glucose dehydrogenase a
, UDP-Glc dehydrogenase
, uridine diphospho-glucose dehydrogenase
, UDP-glucose dehydrogeanse