Analytical Data
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Gene name
PAH
- Application
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Alternative Names
PAH；Phenylalanine-4-hydroxylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00439
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Expression Region
2-452aa
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AA Sequence
STAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK
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Molecular Weight
52.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
PAH, or phenylalanine hydroxylase, is a crucial enzyme responsible for the conversion of phenylalanine to tyrosine, which is an important step in the metabolism of amino acids. Deficiencies in PAH activity can lead to phenylketonuria (PKU), an inherited metabolic disorder characterized by the accumulation of phenylalanine, resulting in severe neurological impairment if left untreated. The study of PAH, particularly the recombinant expression of the enzyme, has gained traction in the field of biotechnology and medicine. Recombinant PAH is produced using various expression systems, allowing for studies on enzyme kinetics, structure-function relationships, and the development of potential gene therapies. Researchers are exploring methods to enhance the stability and activity of the enzyme, as well as the production of PAH variants that can restore function in PKU patients with specific mutations. Additionally, understanding the molecular mechanisms underlying PAH deficiencies facilitates the design of small molecule drugs that can mimic or enhance its activity, offering novel therapeutic avenues. Overall, the research on PAH recombinant protein holds promise not only for treating PKU but also for advancing our knowledge of enzyme regulation and its implications in metabolic diseases.
