Recombinant Human UGDH Protein
Beta LifeScience
SKU/CAT #: BLA-9478P
Recombinant Human UGDH Protein
Beta LifeScience
SKU/CAT #: BLA-9478P
Collections: Other recombinant proteins, Recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Host Species | Human |
Accession | O60701 |
Synonym | GDH UDP Glc dehydrogenase UDP GlcDH UDP glucose 6 dehydrogenase UDP glucose dehydrogenase UDP-Glc dehydrogenase UDP-GlcDH UDP-glucose 6-dehydrogenase UDP-glucose dehydrogenase UDPGDH UGD Ugdh UGDH_HUMAN Uridine diphospho glucose dehydrogenase |
Description | Recombinant Human UGDH Protein was expressed in E.coli. It is a Full length protein |
Source | E.coli |
AA Sequence | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM FEIKKICCIG AGYVGGPTCS VIAHMCPEIR VTVVDVNESR INAWNSPTLP IYEPGLKEVV ESCRGKNLFF STNIDDAIKE ADLVFISVNT PTKTYGMGKG RAADLKYIEA CARRIVQNSN GYKIVTEKST VPVRAAESIR RIFDANTKPN LNLQVLSNPE FLAEGTAIKD LKNPDRVLIG GDETPEGQRA VQALCAVYEH WVPREKILTT NTWSSELSKL AANAFLAQRI SSINSISALC EATGADVEEV ATAIGMDQRI GNKFLKASVG FGGSCFQKDV LNLVYLCEAL NLPEVARYWQ QVIDMNDYQR RRFASRIIDS LFNTVTDKKI AILGFAFKKD TGDTRESSSI YISKYLMDEG AHLHIYDPKV PREQIVVDLS HPGVSEDDQV SRLVTISKDP YEACDGAHAV VICTEWDMFK ELDYERIHKK MLKPAFIFDG RRVLDGLHNE LQTIGFQIET IGKKVSSKRI PYAPSGEIPK FSLQDPPNKK PKV |
Molecular Weight | 60 kDa including tags |
Purity | >95% SDS-PAGE. |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
Bioactivity | Specific activity: > 0.1 unit/ml. One unit will oxidize 1.0 µmol of UDP-glucose to UDP-glucuronic acid per minute at pH 8.0 at 25°C. |
Formulation | Liquid Solution |
Stability | The recombinant protein samples are stable for up to 12 months at -80°C |
Reconstitution | See related COA |
Unit Definition | For Research Use Only |
Storage Buffer | Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle. |
Target Details
Target Function | Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans. Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans. Required for proper brain and neuronal development. |
Protein Families | UDP-glucose/GDP-mannose dehydrogenase family |
Database References | |
Tissue Specificity | Detected in heart, placenta, liver, pancreas, spleen, thymus, prostate, ovary, small intestine and colon. Widely expressed. |
Gene Functions References
- Data indicate that the A136M substitution in UDP-glucose dehydrogenase (hUGDH) stabilizes the hexamer. PMID: 27966912
- study has identified several new proteins like RHOC, DLG5, UGDH, TMOD3 in addition to known chemoresistance associated proteins in non-small cell lung carcinoma. PMID: 26898345
- UGDH protein level in osteoarthritis cartilage was much lower than in control cartilage. PMID: 25465897
- 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. PMID: 25478983
- 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. PMID: 24145036
- Mammalian UGDH displays hysteresis (observed as a lag 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. PMID: 23363239
- both missense mutations significantly reducing the ability of UGDH to provide precursors for cardiac cushion formation, which is essential to subsequent valve formation. PMID: 22815472
- Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates. PMID: 22123821
- An alternate crystal structure of human UGDH (hUGDH) in complex with UDP-glucose at 2.8 A resolution, is reported. PMID: 21984906
- 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. PMID: 21961565
- high UGDH levels may underlie susceptibility of the orbit to localized overproduction of hyaluronan in Graves disease. PMID: 21576248
- Structure and mechanism of human UDP-glucose 6-dehydrogenase. PMID: 21502315
- An atypical allosteric mechanism in human UDP-alpha-D-glucose 6-dehydrogenase (UGDH) based on an easily acquired and identifiable structural attribute: packing defects in the protein core. PMID: 21595445
- UGDH can regulate cell motility through the production of glycosaminoglycans PMID: 20691680
- Results support the UGDH content in prostatic acini as a novel candidate biomarker that may complement the development of a multi-biomarker panel for detecting PC within the tumor adjacent field on a histologically normal biopsy specimen. PMID: 19676054
- UGDH core promoter has a role in up- and down-regulation of UGDH after TGF-beta stimulation and in hypoxic conditions PMID: 12682078
- role of Cys-276 as a catalytic residue; Lys-279 is likely to have a role in positioning active site residues and in maintaining the hexameric quaternary structure PMID: 15044486
- Gly-13 plays an important role for efficient binding of NAD(+) to human UDP-glucose dehydrogenase PMID: 15247292
- C276 plays an important role for efficient binding of UDP-glucose to hUGDH PMID: 15898741
- Our results indicate that the region from nucleotide position -486 to -632 relative to the start of the small transcript contains positive regulatory elements that contribute to gene expression. PMID: 16002992
- report the presence of an inhibitory cis-element in the distal region of the UGDH promoter that interacts with putative transcriptional repressors for the negative regulation of the UGDH gene PMID: 16495656
- UGDH was purified and crystallized, and diffraction data proposes that the biological unit of UGDH is a tetramer. PMID: 17073734
- Alteration of lysine 220 to alanine, histidine, or arginine significantly impaired enzyme function. PMID: 17209547
- Results suggest that UGDH Ala222 and Ser233 play an important role in maintaining the hexameric structure and the reduced binding affinities for substrates are attributable to its altered subunit communication. PMID: 17927902
- This demonstrates that the UGDH transcript and protein quantities, the enzyme activity, and glycosaminoglycan contents increase in LMP2A overexpressed human embryonic kidney 293 (HEK293) cells. PMID: 18717819
- perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the UGDH structure PMID: 19358821