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TH Protein (His tag)

Recombinant TH protein expressed in Escherichia coli (E. coli).
Catalog No. ABIN7669818

Quick Overview for TH Protein (His tag) (ABIN7669818)

Target

TH

Protein Type

Recombinant

Biological Activity

Inactive

Origin

Mouse

Source

  • 1
Escherichia coli (E. coli)

Purity

> 95 %
  • Purification tag / Conjugate

    This TH protein is labelled with His tag.

    Purpose

    Recombinant Mouse TH protein (His tag)

    Sequence

    Phe 34-Leu 301

    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

    TH

    Background

    Tyrosine hydroxylase (TH) is a rate-limiting enzyme in catecholamine synthesis. Tyrosine hydroxylase activity is modulated by protein-protein interactions with enzymes in the same pathway or the tetrahydrobiopterin pathway, structural proteins considered to be chaperones that mediate the neuron's oxidative state. It is phosphorylated at serine (Ser) residues Ser8, Ser19, Ser31 and Ser40 in vitro. The phosphorylation of tyrosine hydroxylase at Ser19 or Ser8 has no direct effect on tyrosine hydroxylase activity. As tyrosine hydroxylase (TH) catalyses the formation of L-DOPA, the rate-limiting step in the biosynthesis of DA, the Parkinson's disease (PD) can be considered as a TH-deficiency syndrome of the striatum. A direct pathogenetic role of TH has also been suggested, as the enzyme is a source of reactive oxygen species (ROS) in vitro and a target for radical-mediated oxidative injury. Recently, it has been demonstrated that L-DOPA is effectively oxidized by mammalian Tyrosine hydroxylase in vitro, possibly contributing to the cytotoxic effects of DOPA.,DYT14,DYT5b,TH,TY3H,TYH,The,Tyrosine 3 hydroxylase,YH

    Molecular Weight

    calculated_mw: 29.4 kDa

    observed_mw: 32 kDa

    UniProt

    P24529
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