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UGDH Antibody

  • 中文名稱:
    UGDH兔多克隆抗體
  • 貨號:
    CSB-PA025567GA01HU
  • 規格:
    ¥3,900
  • 其他:

產品詳情

  • Uniprot No.:
  • 基因名:
    UGDH
  • 別名:
    GDH antibody; UDP Glc dehydrogenase antibody; UDP GlcDH antibody; UDP glucose 6 dehydrogenase antibody; UDP glucose dehydrogenase antibody; UDP-Glc dehydrogenase antibody; UDP-GlcDH antibody; UDP-glucose 6-dehydrogenase antibody; UDP-glucose dehydrogenase antibody; UDPGDH antibody; UGD antibody; Ugdh antibody; UGDH_HUMAN antibody; Uridine diphospho glucose dehydrogenase antibody
  • 宿主:
    Rabbit
  • 反應種屬:
    Human,Mouse,Rat
  • 免疫原:
    Human UGDH
  • 免疫原種屬:
    Homo sapiens (Human)
  • 抗體亞型:
    IgG
  • 純化方式:
    Antigen Affinity Purified
  • 濃度:
    It differs from different batches. Please contact us to confirm it.
  • 保存緩沖液:
    PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
  • 產品提供形式:
    Liquid
  • 應用范圍:
    ELISA,WB
  • Protocols:
  • 儲存條件:
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 貨期:
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
  • 用途:
    For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產品評價

靶點詳情

  • 功能:
    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.
  • 基因功能參考文獻:
    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

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  • 蛋白家族:
    UDP-glucose/GDP-mannose dehydrogenase family
  • 組織特異性:
    Detected in heart, placenta, liver, pancreas, spleen, thymus, prostate, ovary, small intestine and colon. Widely expressed.
  • 數據庫鏈接:

    HGNC: 12525

    OMIM: 603370

    KEGG: hsa:7358

    STRING: 9606.ENSP00000319501

    UniGene: Hs.572518



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