PAH Protein, Human, Recombinant (415 Asn/Asp, His)

カタログ番号 TMPY-02707

別名: phenylalanine hydroxylase, PH, PKU1, PKU

PAH (phenylalanine hydroxylase), also known as PH, belongs to the biopterin-dependent aromatic amino acid hydroxylase family. It contains 1 ACT domain, N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule. In humans, PAH is expressed both in the liver and the kidney, and there is some indication that it may be differentially regulated in these tissues. PAH catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. It is one of three members of the pterin-dependent amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin and a non-heme iron for catalysis. Defects in PAH are the cause of phenylketonuria (PKU). PKU is an autosomal recessive inborn error of phenylalanine metabolism, due to severe phenylalanine hydroxylase deficiency. It is characterized by blood concentrations of phenylalanine persistently above 1200 mumol.

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PAH Protein, Human, Recombinant (415 Asn/Asp, His)

パッケージサイズ	在庫状況	単価(税別)
50 μg	在庫あり	￥ 88,500
100 μg	約5 days	￥ 151,500
200 μg	約5 days	￥ 257,000
500 μg	約5 days	￥ 521,000

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生物学的特性に関する説明

Technical Params

Product Properties

参考文献

生物学的情報

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説明

Species	Human
Expression Host	Baculovirus-Insect Cells
Tag	His
Accession Number	P00439
別名	phenylalanine hydroxylase, PH, PKU1, PKU
Construction	A DNA sequence encoding the human PAH (P00439) (Met 1-Lys 452) (415 Asn/Asp) was expressed, with a polyhistidine tag at the N-terminus.
Protein Purity	> 70 % as determined by SDS-PAGE
分子量	54 kDa (predicted)

Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method.
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 8.0, 10% glycerol. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage	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.
Shipping	In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background	PAH (phenylalanine hydroxylase), also known as PH, belongs to the biopterin-dependent aromatic amino acid hydroxylase family. It contains 1 ACT domain, N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule. In humans, PAH is expressed both in the liver and the kidney, and there is some indication that it may be differentially regulated in these tissues. PAH catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. It is one of three members of the pterin-dependent amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin and a non-heme iron for catalysis. Defects in PAH are the cause of phenylketonuria (PKU). PKU is an autosomal recessive inborn error of phenylalanine metabolism, due to severe phenylalanine hydroxylase deficiency. It is characterized by blood concentrations of phenylalanine persistently above 1200 mumol.

参考文献

1. Fitzpatrick PF, et al. (1999) Tetrahydropterin-dependent amino acid hydroxylases. Annu Rev Biochem. 68:355-81. 2. Olsson E, et al. (2011) Formation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases. Chemistry. 17(13):3746-58. 3. Bassan A, et al. (2003) Mechanism of aromatic hydroxylation by an activated FeIVO core in tetrahydrobiopterin-dependent hydroxylases. Chemistry. 9(17):4055-67. 4. Panay AJ, et al. (2011) Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase. Biochemistry. 50(11):1928-33. 5. Bassan A, et al. (2003) Mechanism of dioxygen cleavage in tetrahydrobiopterin-dependent amino acid hydroxylases. Chemistry. 9(1):106-15.

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Keywords

PAH Protein, Human, Recombinant (415 Asn/Asp, His) PKU-1 phenylalanine hydroxylase PH PKU1 PKU 1 PKU recombinant recombinant-proteins proteins protein