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Phenylalanine Hydroxylase Protein (His tag)

Protéine Recombinant Phenylalanine Hydroxylase exprimée dans Escherichia coli (E. coli).
N° du produit ABIN7669419

Aperçu rapide pour Phenylalanine Hydroxylase Protein (His tag) (ABIN7669419)

Antigène

Voir toutes Phenylalanine Hydroxylase Protéines
Phenylalanine Hydroxylase

Type de proteíne

Recombinant

Activité biologique

Inactive

Origine

  • 6
  • 1
  • 1
  • 1
  • 1
  • 1
Humain

Source

  • 4
  • 3
  • 2
  • 1
  • 1
Escherichia coli (E. coli)

Pureté

> 95 %
  • Purification/Conjugué

    Cette Phenylalanine Hydroxylase protéine est marqué à la His tag.

    Fonction

    Recombinant Human PAH protein (His tag)

    Séquence

    Ser 2-Lys 452

    Purification

    > 95 % as determined by reducing SDS-PAGE.

    Stérilité

    0.2 μm filtered

    niveau d'endotoxine

    < 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.

    Stock

    4 °C,-20 °C,-80 °C

    Stockage commentaire

    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.

    Date de péremption

    12 months
  • Antigène

    Phenylalanine Hydroxylase

    Autre désignation

    PAH

    Sujet

    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

    Poids moléculaire

    calculated_mw: 49.5 kDa

    observed_mw: 50 kDa

    UniProt

    P00439
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