Phenylalanine Hydroxylase Protein (His tag)

Catalog No. ABIN7669418

This Recombinant Phenylalanine Hydroxylase protein is expressed in Baculovirus infected Insect Cells.

Quick Overview for Phenylalanine Hydroxylase Protein (His tag) (ABIN7669418)

Target: Phenylalanine Hydroxylase

Protein Type: Recombinant

Biological Activity: Inactive

Origin: Human

Source: Baculovirus infected Insect Cells

Purity: > 70 %

Product Details

Purification tag / Conjugate: This Phenylalanine Hydroxylase protein is labelled with His tag.

Purpose: Recombinant Human PAH/PH Protein (415 Asn/Asp, His Tag)

Sequence: Met 1-Lys 452

Purification: > 70 % as determined by reducing SDS-PAGE.

Sterility: 0.2 μm filtered

Endotoxin Level: < 1.0 EU per μg of the protein as determined by the LAL method.

Application Details

Restrictions: For Research Use only

Handling

Format: Lyophilized

Buffer: Lyophilized from sterile 20 mM Tris, 500 mM NaCl, pH 8.0, 10 % glycerol
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 Details

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: 54.0 kDa

observed_mw: 50 kDa

UniProt: P00439