Recombinant Human Phenylalanine-4-Hydroxylase (PAH)

Name: Recombinant Human Phenylalanine-4-Hydroxylase (PAH)
Brand: Beta LifeScience
SKU: BLC-07327P
Price: 299.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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100ug

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Product Overview

Description	Recombinant Human Phenylalanine-4-Hydroxylase (PAH) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00439
Target Symbol	PAH
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	STAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK
Expression Range	2-452aa
Protein Length	Full Length of Mature Protein
Mol. Weight	51.9 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine.
Protein Families	Biopterin-dependent aromatic amino acid hydroxylase family
Database References	HGNC: 8582 OMIM: 261600 KEGG: hsa:5053 STRING: 9606.ENSP00000448059 UniGene: Hs.560019
Associated Diseases	Phenylketonuria (PKU); Non-phenylketonuria hyperphenylalaninemia (Non-PKU HPA); Hyperphenylalaninemia (HPA)

Gene Functions References

Molecular diagnostics for DNAJC12 variants are thus mandatory in all patients in which deficiencies of PAH and BH4 are genetically excluded. PMID: 29174366
Mutational spectrum of the phenylalanine hydroxylase gene in patients with phenylketonuria in the central region of China has been reported. PMID: 29390883
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
strong association between particular mutations and minihaplotypes could be useful for prenatal diagnosis and preimplantation genetic diagnosis in affected families PMID: 28676969
PAH mutation was associated with hyperphenylalaninemia. PMID: 29032371
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
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
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
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
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
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
We obtained a PAH gene variant spectrum for the Northern Chinese population and devised a strategy for gene diagnosis using phenylketonuria pedigrees. PMID: 28982351
Phenylalanine hydroxylase gene mutations are associated with phenylketonuria. PMID: 28604955
DNA methylated alleles of the phenylalanine hydroxylase promoter remodeled at elevated phenylalanine levels in newborns with hyperphenylalaninemia have been characterized. PMID: 28389235
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
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
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
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
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
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
PAH gene mutation analysis combined with STR linkage analysis can provide rapid and accurate prenatal diagnosis for phenylketonuria families PMID: 26600521
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
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
This study is the first report on tested population genetic structure using VNTR alleles at the PAH gene PMID: 26025954
Aberrant methylation is observed in leukocytes of PAH deficient phenylketonuria patients and is influenced by phenylalanine exposure. PMID: 25990862
We determined phenylalanine hydroxylase function of 30 frequent homozygous and compound heterozygous genotypes covering 55% of the study population. PMID: 25596310
Mutational spectrum was presented for PAH gene in PAH deficiency patients from different parts of Mexico. New mutations were described. PMID: 24941924
mutation spectrum of the gene PAH in the Qinghai population was similar to that in other populations in North China PMID: 26575882
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
15 different mutations of phenylalanine hydroxylase gene were detected in patients with phenylketonuria. PMID: 25863075
R241C, R408Q and Ex6-96A>G are the most common mutations in PAH in phenylalanine hydroxylase deficiency patients. PMID: 25863076
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
We demonstrated the high expression of PAH and a large increase of PAH activity in differenciated liver progenitor cells. PMID: 24825084
findings suggest that common genetic variations in Phenylalanine hydroxylase are associated with verbal memory in healthy adults. PMID: 23898865
In this study of the PAH mutation spectrum in the Taiwanese population, 139 alleles were identified including 34 different mutations. PMID: 24401910
Mutations were detected in the exons and flaking introns of PAH gene of 44 families with classical phenylketonuria. PMID: 25449068
lipoprotein synthesis in PAH-deficient children, particularly in PKU children, was suppressed in early life. PMID: 24607329
Two polymorphic variants of PAH appear to be risk factors for NSCL/P, rs7485331 and rs12425434 in a Polish population. PMID: 24606907
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
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
Twenty phenylalanine hydroxylase gene mutations were discovered. PMID: 24510552
A total of 98 mutations were detected in 110 phenylalanine hydroxylase alleles. PMID: 24510568
125 new mutations were found in exons 6, 7 and 12 of PAH in patients with hyperphenylalaninemia. PMID: 24078561
Genotype-phenotype correlation of PAH gene mutations in phenylketonuria in a Syrian population. PMID: 23856132
The observed phenotype is not always consistent with genotype predicting effect in Chinese phenylalanine hydroxylase deficiency patients. PMID: 23932990
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
A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics. PMID: 23296088
Thirteen different mutations were identified in the PAH gene in Lebanese patients with phenylalanine hydroxylase deficiency. PMID: 23220018
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
PAH exon 11 is vulnerable due to a weak 3' splice site. PMID: 22698810

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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.

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