Recombinant Human UGDH Protein

Beta LifeScience SKU/CAT #: BLA-9478P

Recombinant Human UGDH Protein

Beta LifeScience SKU/CAT #: BLA-9478P
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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

  1. Data indicate that the A136M substitution in UDP-glucose dehydrogenase (hUGDH) stabilizes the hexamer. PMID: 27966912
  2. 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
  3. UGDH protein level in osteoarthritis cartilage was much lower than in control cartilage. PMID: 25465897
  4. 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
  5. 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
  6. 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
  7. 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
  8. Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates. PMID: 22123821
  9. An alternate crystal structure of human UGDH (hUGDH) in complex with UDP-glucose at 2.8 A resolution, is reported. PMID: 21984906
  10. 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
  11. high UGDH levels may underlie susceptibility of the orbit to localized overproduction of hyaluronan in Graves disease. PMID: 21576248
  12. Structure and mechanism of human UDP-glucose 6-dehydrogenase. PMID: 21502315
  13. 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
  14. UGDH can regulate cell motility through the production of glycosaminoglycans PMID: 20691680
  15. 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
  16. UGDH core promoter has a role in up- and down-regulation of UGDH after TGF-beta stimulation and in hypoxic conditions PMID: 12682078
  17. 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
  18. Gly-13 plays an important role for efficient binding of NAD(+) to human UDP-glucose dehydrogenase PMID: 15247292
  19. C276 plays an important role for efficient binding of UDP-glucose to hUGDH PMID: 15898741
  20. 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
  21. 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
  22. UGDH was purified and crystallized, and diffraction data proposes that the biological unit of UGDH is a tetramer. PMID: 17073734
  23. Alteration of lysine 220 to alanine, histidine, or arginine significantly impaired enzyme function. PMID: 17209547
  24. 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
  25. 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
  26. 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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