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Phenylalanine Hydroxylase Protein (His tag)

Recombinant Phenylalanine Hydroxylase protein expressed in Escherichia coli (E. coli).
Catalog No. ABIN7669419

Quick Overview for Phenylalanine Hydroxylase Protein (His tag) (ABIN7669419)

Target

See all Phenylalanine Hydroxylase Proteins
Phenylalanine Hydroxylase

Protein Type

Recombinant

Biological Activity

Inactive

Origin

  • 6
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Human

Source

  • 4
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Escherichia coli (E. coli)

Purity

> 95 %
  • Purification tag / Conjugate

    This Phenylalanine Hydroxylase protein is labelled with His tag.

    Purpose

    Recombinant Human PAH protein (His tag)

    Sequence

    Ser 2-Lys 452

    Purification

    > 95 % as determined by reducing SDS-PAGE.

    Sterility

    0.2 μm filtered

    Endotoxin Level

    < 10 EU/mg of the protein as determined by the LAL method.
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  • Restrictions

    For Research Use only
  • Format

    Lyophilized

    Reconstitution

    It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.

    Buffer

    Lyophilized from sterile PBS, pH 7.4.
    Normally 5 % -8 % trehalose, mannitol and 0.01 % Tween 80 are added as protectants before lyophilization.

    Storage

    4 °C,-20 °C,-80 °C

    Storage Comment

    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

    Expiry Date

    12 months
  • Target

    Phenylalanine Hydroxylase

    Alternative Name

    PAH

    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.,PH,PKU,PKU1

    Molecular Weight

    calculated_mw: 49.5 kDa

    observed_mw: 50 kDa

    UniProt

    P00439
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