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TH Protein (His tag)

Recombinant TH-Protein exprimiert in Escherichia coli (E. coli).
Produktnummer ABIN7669818

Kurzübersicht für TH Protein (His tag) (ABIN7669818)

Target

TH

Protein-Typ

Recombinant

Biologische Aktivität

Inactive

Spezies

Maus

Quelle

  • 1
Escherichia coli (E. coli)

Reinheit

> 95 %
  • Aufreinigungstag / Konjugat

    Dieses TH Protein ist gelabelt mit His tag.

    Verwendungszweck

    Recombinant Mouse TH protein (His tag)

    Sequenz

    Phe 34-Leu 301

    Aufreinigung

    > 95 % as determined by reducing SDS-PAGE.

    Sterilität

    0.2 μm filtered

    Endotoxin-Niveau

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

    Nur für Forschungszwecke einsetzbar
  • Format

    Lyophilized

    Rekonstitution

    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.

    Lagerung

    4 °C,-20 °C,-80 °C

    Informationen zur Lagerung

    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.

    Haltbarkeit

    12 months
  • Target

    TH

    Hintergrund

    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

    Molekulargewicht

    calculated_mw: 29.4 kDa

    observed_mw: 32 kDa

    UniProt

    P24529
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