Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P00439 |
express system | Baculovirus-Insect Cells |
product tag | N-His |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Phenylalanine hydroxylase (PAH) is a member of aromatic amino acid hydroxylase (AAAHs) family, and catalyze phenylalanine (Phe) into tyrosine (Tyr). PAH is also an allosteric enzyme that maintains phenylalanine (Phe) below neurotoxic levels; its failure results in phenylketonuria, an inborn error of amino acid metabolism. |
molecular weight | The protein has a predicted MW of 52.82 kDa same as Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human PAH (D415N) Protein 2333
$300.00 – $1,000.00
Summary
- Expression: Baculovirus-Insect Cells
- Pure: Yes (HPLC)
- Amino Acid Range: Met1-Lys452 (D415N)
Human PAH (D415N) Protein 2333
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Phenylalanine hydroxylase (PAH) is a member of aromatic amino acid hydroxylase (AAAHs) family, and catalyze phenylalanine (Phe) into tyrosine (Tyr). PAH is also an allosteric enzyme that maintains phenylalanine (Phe) below neurotoxic levels; its failure results in phenylketonuria, an inborn error of amino acid metabolism. |
Protein names Phenylalanine-4-hydroxylase (PAH) (EC 1.14.16.1) (Phe-4-monooxygenase) |
Gene names PAH,PAH |
Protein family Biopterin-dependent aromatic amino acid hydroxylase family |
Mass 9606Da |
Function Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. |
Catalytic activity BINDING 285; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P04176"; BINDING 290; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P04176"; BINDING 330; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000250|UniProtKB:P04176" |
Pathway PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6. |
Structure Homodimer and homotetramer. |
Post-translational modification Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine. |
Target Relevance information above includes information from UniProt accession: P00439 |
The UniProt Consortium |
Data
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The purity of Human PAH (D415N) is greater than 95% as determined by SEC-HPLC. |
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Human PAH (D415N) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. |
Publications
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