PNP Antibody

Code CSB-PA355527ESR1HU
Size US$166
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  • Western blot
    All lanes: PNP antibody at 10µg/ml
    Lane 1: Jurkat whole cell lysate
    Lane 2: K562 whole cell lysate
    Secondary
    Goat polyclonal to rabbit IgG at 1/10000 dilution
    Predicted band size: 32 kDa
    Observed band size: 32 kDa

  • Immunohistochemistry of paraffin-embedded human brain tissue using CSB-PA355527ESR1HU at dilution of 1:100

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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) PNP Polyclonal antibody
Uniprot No.
Target Names
PNP
Alternative Names
FLJ94043 antibody; FLJ97288 antibody; FLJ97312 antibody; Inosine phosphorylase antibody; Inosine-guanosine phosphorylase antibody; MGC117396 antibody; MGC125915 antibody; MGC125916 antibody; NP antibody; Np1 antibody; Nucleoside phosphorylase antibody; PNP antibody; Pnp1 antibody; PNPH_HUMAN antibody; PRO1837 antibody; PUNP antibody; Purine nucleoside orthophosphate ribosyltransferase antibody; Purine nucleoside phosphorylase 5a antibody; Purine nucleoside phosphorylase antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Purine nucleoside phosphorylase protein (1-289AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Form
Liquid
Tested Applications
ELISA, WB, IHC
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:2000
IHC 1:20-1:200
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
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.

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Target Background

Function
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.
Gene References into Functions
  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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Involvement in disease
Purine nucleoside phosphorylase deficiency (PNPD)
Subcellular Location
Cytoplasm.
Protein Families
PNP/MTAP phosphorylase family
Tissue Specificity
Expressed in red blood cells; overexpressed in red blood cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic anemia of unknown etiology.
Database Links

HGNC: 7892

OMIM: 164050

KEGG: hsa:4860

STRING: 9606.ENSP00000354532

UniGene: Hs.75514

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