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  4. Recombinant Human Purine nucleoside phosphorylase (PNP)

Recombinant Human Purine nucleoside phosphorylase (PNP)

  • 货号：
    CSB-YP355527HU
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 货号：
    CSB-EP355527HU-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 货号：
    CSB-BP355527HU
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 货号：
    CSB-MP355527HU
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
    PNP
  • Uniprot No.：
  • 别名：
    FLJ94043; FLJ97288; FLJ97312; Inosine phosphorylase; Inosine-guanosine phosphorylase; MGC117396; MGC125915; MGC125916; NP; Np1; Nucleoside phosphorylase; PNP; Pnp1; PNPH_HUMAN; PRO1837; PUNP; Purine nucleoside orthophosphate ribosyltransferase; Purine nucleoside phosphorylase 5a; Purine nucleoside phosphorylase
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    full length protein
  • 表达区域：
    1-289
  • 氨基酸序列
    MENGYTYEDY KNTAEWLLSH TKHRPQVAII CGSGLGGLTD KLTQAQIFDY GEIPNFPRST VPGHAGRLVF GFLNGRACVM MQGRFHMYEG YPLWKVTFPV RVFHLLGVDT LVVTNAAGGL NPKFEVGDIM LIRDHINLPG FSGQNPLRGP NDERFGDRFP AMSDAYDRTM RQRALSTWKQ MGEQRELQEG TYVMVAGPSF ETVAECRVLQ KLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE SLEKANHEEV LAAGKQAAQK LEQFVSILMA SIPLPDKAS
  • 蛋白标签：
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式：
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 复溶：
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    Catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine.
  • 基因功能参考文献：
    1. The study suggests that mass-constrained femtosecond motions at the catalytic site of PNP can improve transition state barrier crossing by more frequent sampling of essential catalytic site contacts. PMID: 29915028
    2. The PNP rs1049564 T allele is a loss-of-function variant that induces S-phase block and IFN pathway activation in lymphocytes. The S-phase block could be rescued in our in vitro experiments, suggesting the potential for personalized treatment. PMID: 28859258
    3. Data show that the mutations in purine nucleoside phosphorylase (PNP) alters the enthalpy-entropy balance with little effect on the catalytic rates. PMID: 27976868
    4. Data (including data from empirical valence bond/molecular dynamic simulations) suggest that PNP substrate specificity for inosine and guanosine is a direct result of electrostatic preorganization energy along the reaction coordinate. PMID: 26985580
    5. the binding mechanism of a transition state analogue (DADMe-immucillin-H) to the purine nucleoside phosphorylase (PNP) enzyme, is reported. PMID: 25625196
    6. Data show that [15N, 2H]His8-purine nucleoside phosphorylase (PNP) had reduced catalytic site chemistry larger than proportional to the enzymatic mass difference. PMID: 26305965
    7. Study of genetic heterogeneity in systemic lupus erythematosus, the top associations in European ancestry were protein kinase, cyclic GMP-dependent, type I (PRKG1) rs7897633 (P(Meta) = 2.75 x 10(-8)) and purine nucleoside phosphorylase (PNP) rs1049564 (P(Meta) = 1.24 x 10(-7)). PMID: 25338677
    8. Human small intestine is a key site for ribavirin phosphorolysis and that PNP is primarily involved in the metabolism. PMID: 24107682
    9. insufficient data to evaluated impact of genetic polymorphisms on disease susceptibility PMID: 24792412
    10. Complete lack of PNP triggers accumulation of deoxyguanosine, thereby disrupting B-cell development, the consequence of which is more profound with time, as was found in the older sister. PMID: 22578971
    11. Biochemical and genetic data on a cohort of seven patients from six families identified as PNPase deficient, is reported. PMID: 22132981
    12. This study for the first time describes elevated levels of alpha synuclein in pancreatic adenocarcinoma as well as highlights the potential of evaluating NP protein expression. PMID: 21448452
    13. investigation of catalytic mechanisms involved in catalysis by PNP: transition states in arsenolysis and phosphorolysis PMID: 21348499
    14. Results show that some regions, responsible for entrance and exit of substrate, present a conformational variability, which is dissected by dynamics simulation analysis. PMID: 19932753
    15. PNP operating at maximum catalytic potential permits more rapid peptide amide deuterium exchange and greater conformational flexibility of water-peptide bond exchange rate than in either of the complexes with transition state analogues. PMID: 20108972
    16. The optimum pH for PNP from human erythrocytes with xanthosine and xanthine is in the range 5-6, whereas those with guanosine, guanine, inosine & hypoxanthine are in the range 7-8. Possible PNP binding modes of Xan and Xao by mammalian PNPs are proposed. PMID: 12180982
    17. Crystal structure of human purine nucleoside phosphorylase. PMID: 12914785
    18. These data provide a framework in which to conduct genetic association studies of these two genes in relevant populations, thereby allowing hNP and hGSTO1-1 to be evaluated as potential susceptibility genes in human arsenicism. PMID: 12928150
    19. investigation of the quaternary structure of recombinant human purine nucleoside phosphorylase PMID: 13679062
    20. crystal structures in complex with inosine and 2',3'-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The structures provide explanation for ligand binding, refine the purine-binding site and can be used for future inhibitor design. PMID: 14706628
    21. several recurring mutations were found in PNP in patients with purine nucleoside phosphorylase deficiency by DNA sequence analysis PMID: 15571269
    22. crystal structure of human PNP in complex with hypoxanthine, refined to 2.6A resoluti PMID: 15582582
    23. findings suggest that the G51S PNP polymorphism is associated with a faster rate of cognitive decline in Alzheimer's disease patients, highlighting the important role of purine metabolism in the progression of this neurodegenerative disorder PMID: 17221831
    24. Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase PMID: 17639373
    25. Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase. PMID: 18281956
    26. New interactions caused by the mutations increase the catalytic efficiency of the enzyme for formation of a late transition state with increased participation of the phosphate nucleophile. PMID: 18281957
    27. Structural studies on NP are reported with a view towards a new specific scoring function. PMID: 18790691
    28. Protein dynamics on the femtosecond to picosecond timescale are linked to enzymatic function. PMID: 18946041
    29. Comparative analysis of the model of BfPNP and the structure of HsPNP allowed identification of structural features responsible for differences in the computationally determined ligand affinities PMID: 19172318
    30. Results describe a tryptophan-free mutant of purine nucleoside phosphorylase and its dynamic activity. PMID: 19191546
    31. Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase PMID: 19425594

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  • 相关疾病：
    Purine nucleoside phosphorylase deficiency (PNPD)
  • 亚细胞定位：
    Cytoplasm.
  • 蛋白家族：
    PNP/MTAP phosphorylase family
  • 组织特异性：
    Expressed in red blood cells; overexpressed in red blood cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic anemia of unknown etiology.
  • 数据库链接：

    HGNC: 7892

    OMIM: 164050

    KEGG: hsa:4860

    STRING: 9606.ENSP00000354532

    UniGene: Hs.75514