Recombinant Human Phenylalanine-4-hydroxylase(PAH)

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Code CSB-EP017396HU
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names PAH
Uniprot No. P00439
Research Area Signal Transduction
Alternative Names PAH; PH; PH4H_HUMAN; Phe 4 monooxygenase; Phe-4-monooxygenase; Phenylalanine 4 hydroxylase; Phenylalanine hydroxylase; Phenylalanine-4-hydroxylase; PKU; PKU1
Species Homo sapiens (Human)
Source E.coli
Expression Region 2-452aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 67.7kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or 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.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution 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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life 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.
Lead Time Basically, we can dispatch the products out in 3-7 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Gene References into Functions
  1. Molecular diagnostics for DNAJC12 variants are thus mandatory in all patients in which deficiencies of PAH and BH4 are genetically excluded. PMID: 29174366
  2. Mutational spectrum of the phenylalanine hydroxylase gene in patients with phenylketonuria in the central region of China has been reported. PMID: 29390883
  3. a spectrum of PAH mutations complied from 35 PKU children who are all Chinese Han population from north Jiangsu, is reported in this study. PMID: 29413232
  4. strong association between particular mutations and minihaplotypes could be useful for prenatal diagnosis and preimplantation genetic diagnosis in affected families PMID: 28676969
  5. PAH mutation was associated with hyperphenylalaninemia. PMID: 29032371
  6. Report a novel intron 11 regulatory element, which is involved in exon 11 splicing, as revealed by the investigated pathogenic effect of variants c.1199+17G>A and c.1199+20G>C, identified in PKU patients. Both mutations cause exon 11 skipping in a minigene system. PMID: 29684050
  7. three novel variants of the PAH gene, p.E178K (c.532G>A), p.V245M (c.733G>A), p.S250F (c.749C>T), showed impaired protein expression and enzyme activity. PMID: 29653233
  8. Among phenylketonuria patients, some with autism at the time of evaluation, six mutations were identified: p.E280K, p.G352Vfs, IVS10nt11, p.I224T, p.R261Q, and p.R252W. Study found no correlation between autism and mutations affecting the phenylalanine hydroxylase gene, but the age of die PMID: 26759449
  9. Studies involving co-expression of differently phenylalanine hydroxylase (PAH) alleles have shown that one variant form can influence the other when assembled into a tetramer and have effect on enzyme activity in vitro, and on BH4 responsiveness and PKU phenotype in patients carrying them. [review] PMID: 26919687
  10. 17 VUS (37%; 7 in ACADM, 9 in GALT, and 1 in PAH) were reclassified from uncertain (6 to benign or likely benign and 11 to pathogenic or likely pathogenic). We identified common types of missing information that would have helped make a definitive classification and categorized this information by ease and cost to obtain PMID: 27308838
  11. Our findings contribute to better understanding of structure and function of PAH mutated enzymes and optimal treatment of PKU patients carrying these mutations using BH4 supplementation. PMID: 28653649
  12. We obtained a PAH gene variant spectrum for the Northern Chinese population and devised a strategy for gene diagnosis using phenylketonuria pedigrees. PMID: 28982351
  13. Phenylalanine hydroxylase gene mutations are associated with phenylketonuria. PMID: 28604955
  14. DNA methylated alleles of the phenylalanine hydroxylase promoter remodeled at elevated phenylalanine levels in newborns with hyperphenylalaninemia have been characterized. PMID: 28389235
  15. In this study, we assigned the phenotypic outcome of three of the five novel mutations and furthermore six not previously classified mutations to one of the four PKU categories. PMID: 26542770
  16. PAH mutation analyses provided further support for genotype-phenotype correlations in patients with hyperphenylalaninemia. The high incidence of phenylketonuria in Nagasaki, the westernmost part of Japan, might be due to migration of people with PAH mutations from China and Korea, and geographic factors. PMID: 27173423
  17. Our study highlighted two novel promoter KLF1 and 3'-region C/EBPalpha motifs in the phenylalanine hydroxylase (PAH) gene which decrease transcription in vitro and, thus, could be considered as PAH expression modifiers. PMID: 27447460
  18. The results of the in vitro residual PAH activity have major implications, both for our understanding of genotype-phenotype correlations, and thereby existing inconsistencies, but also for the elucidation of the molecular basis of tetrahydrobiopterin (BH4) responsiveness. PMID: 27620137
  19. Data provide the structural evidence for a dietary I-phenylalanine (Phe) binding pocket at the subunit-subunit interface of a N-terminal regulatory domain (PAH-RD) dimer, and demonstrate that PAH-RD dimerization depends on Phe binding. PMID: 27049649
  20. The co-expression of two distinct PAH variants revealed possible dominance effects (positive or negative) by one of the variants on residual PAH activity as a result of interallelic complementation. PMID: 26803807
  21. PAH gene mutation analysis combined with STR linkage analysis can provide rapid and accurate prenatal diagnosis for phenylketonuria families PMID: 26600521
  22. The mutation spectrum of PAH gene in Henan seems to differ from that of other regions. Independent assortment of mutant alleles may result in a complex genotype-phenotype correlation. PMID: 27264808
  23. This study identified one novel PAH variant-c.699C>G-and and tries to show a genotype-phenotype relationship also regarding BH4-responsiveness. PMID: 25894915
  24. This study is the first report on tested population genetic structure using VNTR alleles at the PAH gene PMID: 26025954
  25. Aberrant methylation is observed in leukocytes of PAH deficient phenylketonuria patients and is influenced by phenylalanine exposure. PMID: 25990862
  26. We determined phenylalanine hydroxylase function of 30 frequent homozygous and compound heterozygous genotypes covering 55% of the study population. PMID: 25596310
  27. Mutational spectrum was presented for PAH gene in PAH deficiency patients from different parts of Mexico. New mutations were described. PMID: 24941924
  28. mutation spectrum of the gene PAH in the Qinghai population was similar to that in other populations in North China PMID: 26575882
  29. Combining in silico analysis and molecular dynamics simulations (in total 3 mus) we described the structural impact of the mutations, which allowed us to separate 32 out of 34 mutations between groups A and B. PMID: 25750018
  30. 15 different mutations of phenylalanine hydroxylase gene were detected in patients with phenylketonuria. PMID: 25863075
  31. R241C, R408Q and Ex6-96A>G are the most common mutations in PAH in phenylalanine hydroxylase deficiency patients. PMID: 25863076
  32. 15 different mutations were found in 27 unrelated Kurdish PKU patients. IVS4 + 1G > C (c.441 + 1G > C) and IVS7 - 5 T > C (c.843 - 5 T > C) are novel mutations. PAH mutations differ between the Kermanshah province and other parts of Iran. PMID: 24048906
  33. We demonstrated the high expression of PAH and a large increase of PAH activity in differenciated liver progenitor cells. PMID: 24825084
  34. findings suggest that common genetic variations in Phenylalanine hydroxylase are associated with verbal memory in healthy adults. PMID: 23898865
  35. In this study of the PAH mutation spectrum in the Taiwanese population, 139 alleles were identified including 34 different mutations. PMID: 24401910
  36. Mutations were detected in the exons and flaking introns of PAH gene of 44 families with classical phenylketonuria. PMID: 25449068
  37. lipoprotein synthesis in PAH-deficient children, particularly in PKU children, was suppressed in early life. PMID: 24607329
  38. Two polymorphic variants of PAH appear to be risk factors for NSCL/P, rs7485331 and rs12425434 in a Polish population. PMID: 24606907
  39. This is probably the first report of identification of a significantly low proportion of missense PAH mutations from PKU families and together with the presence of a high proportion of splice, insertion-deletion, and nonsense mutations. PMID: 24130151
  40. Analysis of the published data shows similar percentage of the "BH4-responsive" variants of a PAH gene in patients from other countries of Eastern Europe PMID: 24350308
  41. Twenty phenylalanine hydroxylase gene mutations were discovered. PMID: 24510552
  42. A total of 98 mutations were detected in 110 phenylalanine hydroxylase alleles. PMID: 24510568
  43. 125 new mutations were found in exons 6, 7 and 12 of PAH in patients with hyperphenylalaninemia. PMID: 24078561
  44. Genotype-phenotype correlation of PAH gene mutations in phenylketonuria in a Syrian population. PMID: 23856132
  45. The observed phenotype is not always consistent with genotype predicting effect in Chinese phenylalanine hydroxylase deficiency patients. PMID: 23932990
  46. The five most prevalent PAH mutations found in patients were p.R408W, IVS12 + 1G>A, p.R261Q, p.R158Q and IVS2 + 5G>C. PMID: 22526846
  47. A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics. PMID: 23296088
  48. Thirteen different mutations were identified in the PAH gene in Lebanese patients with phenylalanine hydroxylase deficiency. PMID: 23220018
  49. The p.G352fsdelG mutation in the PAH gene does not appear to be prevalent in the Moroccan population and would be responsible for only few cases of phenylketonuria. PMID: 22808937
  50. PAH exon 11 is vulnerable due to a weak 3' splice site. PMID: 22698810
  51. Phenylketonuria (PKU) associated multiple mutations in phenylalanine hydroxylase (PAH) gene were identified in Balto-Russian population studied. PMID: 23074961
  52. Eleven different mutations were found, with the most frequent mutation, IVS10-11G>A, accounting for 19% of Khorasan-Razavi PKU alleles. PMID: 22763404
  53. Disease-causing mutations were identified on 209 alleles of the phenylalanine hydroxylase gene. PMID: 22513348
  54. The mutations of phenylketonuria patients from Hebei Province are scattered throughout the PAH gene. Most of them are of single nucleotide substitutions, but large deletions are not rare. PMID: 22333022
  55. The spectrum of phenylalanine hydroxylase (PAH) gene mutations upon investigating 35 index patients identified with hyperphenylalaninemia in Armenia, is presented. PMID: 21890392
  56. mutations in exons 3, 6, 7, 11 and 12 of the phenylalanine hydroxylase gene in patients with phenylketonuria PMID: 21811977
  57. The mutation spectrum and frequency of the PAH gene of patients with phenylketonuria in Henan province were slightly different from those from other parts of China. PMID: 21154324
  58. Data indicate that PAH G46S mutation results in a N-terminal extension of alpha-helix 1 which perturbs the wild-type alpha-beta sandwich motif in the R-domain and promotes new intermolecular contacts, self-association and non-amyloid fibril formation. PMID: 20937381
  59. Activation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactor. PMID: 20667834
  60. c.30C>G causes aberrant mRNA splicing in PAH in two different reporter minigenes and this is abolished if a preexisting flanking GGG triplet is disrupted. PMID: 20457534
  61. 13 different mutations have been detected, which account for 75% of the total mutant alleles. Two mutations were found at high frequencies: IVS10-11G>A (19.3%) and P281L (19.3%), possibly due to consanguinity and genetic drift, among other factors. PMID: 20187763
  62. 3' splice site mutation c.168-2A>G resulted in activation of a cryptic 3' splice site that generated a premature termination codon leading to very low levels of mutant transcript, probably due to activation of nonsense-mediated decay (NMD) pathway PMID: 20188615
  63. Mutations were found in all exons or flanking introns of the PAH gene except for exons 9 and 13. PMID: 20140859
  64. The data presented in this study indicate that the total pool of mutant PAH alleles in phenylketonuria in Chinese Han population consisted of a small number of common mutations and a very high number of rare mutations. PMID: 19915519
  65. Results provide information on the distribution of phenylalanine hydroxylase mutations in phenylketonuria in the Mediterranean area. PMID: 19786003
  66. Missense p.S231F should be classified as a functionally null PAH gene mutation as it drastically reduces stability and activity of the PAH enzyme in vitro. PMID: 19629656
  67. Mutations were identified in 45/58 alleles (detection rate: 96.4%} of PAH in patients with phenylketonuria in China. PMID: 20017307
  68. Sixteen different mutations have been detected, two mutations were found at unexpectedly high frequencies, E280K and R261Q. PMID: 11524738
  69. The spectrum of PAH gene mutations in Sicily reflects the complex demographic history of this island at the crossroad of prehistoric and historical migrations in the Mediterranean sea. PMID: 11708866
  70. X ray cystallography of the catalytic domain in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin ytic domain PMID: 11718561
  71. Tetrahydrobiopterin regulates gene's expression in phenylalanine hydroxylase deficiency. PMID: 11855940
  72. Identification and characterization of a novel liver-specific enhancer of the human phenylalanine hydroxylase gene. PMID: 11935335
  73. Analysis of differential scanning calorimetry thermograms shows that thermal denaturation of PAH occurs in three stages: unfolding of the four regulatory domains; unfolding of two (out of the four) catalytic domains; and irreversible protein denaturation. PMID: 12056888
  74. Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. PMID: 12096915
  75. crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine PMID: 12126628
  76. the mutation spectrum in the Republic of Ireland PMID: 12173030
  77. determination of molecular basis for the effects of phosphorylation on the catalytic efficiency and enzyme stability PMID: 12185072
  78. Genetic evaluation of the family members of subjects with the PAH K274E mutation showed that all individuals with the K274E mutation also exhibited the PAH L321L polymorphism in the catalytic domain of the PAH enzyme. PMID: 12210276
  79. Both the on- and off-rates for the conformational transition were biphasic, which is interpreted in terms of a difference in the energy barrier and the rate by which the two domains (catalytic and regulatory) undergo a conformational change. PMID: 12379147
  80. study of deamidation of labile asparagine residues in the autoregulatory sequence PMID: 12603326
  81. studies on the regulatory properties of the pterin cofactor and dopamine bound at the active site PMID: 12603331
  82. To investigate further the involvement of Cys237 and Arg68 in the activation of the enzyme, we have prepared mutants of hPAH at these positions, with substitutions of different charge and size. PMID: 12653545
  83. A review of studies of PAH gene mutations causing hyper-phenylalaninemia points in particular to a prevalent general mechanism that appears to play a major role in the pathogenicity of many PAH mutations. PMID: 12655545
  84. Two catalytic mutations (Y277D and E280K) and two severe structural defects (IVS10-11G>A and L311P) have been found to abolish PAH specific activity. PMID: 12655546
  85. Two novel amino acid subsittutions, L249P in exon 7 and F402L in exon 12 and one nucleotide substitution 912T>C in intron 8 of the PAH gene in Phenylketonuria families. PMID: 12655552
  86. mutations and polymorphisms of phenylalanine hydroxylase are associated with phenylketonuria PMID: 12765842
  87. Variation is not a highly penetrant autosomal dominant susceptibility locus for mood disorder in families. PMID: 12782966
  88. Parental attitudes regarding newborn screening of PKU were compiled and evaluated. PMID: 12833401
  89. Results describe the crystal structures of the catalytic domain of human phenylalanine hydroxylase in complex with 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine at 2.0A resolution. PMID: 14568534
  90. mutant forms revealed a variably reduced global conformational stability compared with wild-type human PAH, as measured by thermal denaturation and limited proteolysis PMID: 15060071
  91. the denatured state properties of the AAAHs (TH, TPH and PAH) contribute significantly to the stability of these enzymes and their tolerance towards missense mutations PMID: 15135070
  92. Eleven mutations and 3 polymorphisms in PAH gene were found in 40 phenylketonuria (PKU) patients. PMID: 15300621
  93. Hence, generation of H(2)O(2) by UVB can activate epidermal PAH leading to an increased L-tyrosine pool for melanogenesis. PMID: 15313177
  94. seven mild PKU mutations resulted in catalytic defects; I65T, R68S, P244L, and most probably A309V, showed reduced binding affinity for tetrahydrobiopterin PMID: 15459954
  95. Tetrahydrobopterin protects PAH activity in vitro and has implications for phenylketonurias. PMID: 15556637
  96. Study demonstrated the variety of the mutation type PAH gene of PKU in Inner Mongolia population, and confirmed that R243Q, Y356X, Y204C were the hot spots of PAH gene mutation. PMID: 15793771
  97. Tyr325 appears to have an important role ensuring stoichiometric binding of iron, correct geometry of the complexes with substrate and cofactor and, consequently, a right coupling efficiency of the PAH reaction. PMID: 15917086
  98. Hyperphenylalaninemia may be caused by deficiency of Phe hydroxylase or by deficiency of co-factor BH(4). PMID: 16086286
  99. both subunits of phenylalanine hydroxylase were expressed and that the purified heteroallelic enzymes, were catalytically active PMID: 16545551
  100. Results showed that both arginine amino acid and exon 7 is of great significance with regards to the structure and function of the enzyme. PMID: 16765994

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Involvement in disease Phenylketonuria (PKU); Non-phenylketonuria hyperphenylalaninemia (Non-PKU HPA); Hyperphenylalaninemia (HPA)
Protein Families Biopterin-dependent aromatic amino acid hydroxylase family
Database Links

HGNC: 8582

OMIM: 261600

KEGG: hsa:5053

STRING: 9606.ENSP00000448059

UniGene: Hs.560019

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