Mouse TH / Tyrosine Hydroxylase Protein (His Tag)

Tyrosine hydroxylase Protein Datasheet

TH / Tyrosine Hydroxylase Protein Product Information

• Synonym: TH
• Protein Construction: A DNA sequence encoding the mouse TH (P24529) (Pro 2-Ser 498) was fused with a polyhistidine tag at the N-terminus.
• Source: Mouse
• Expression Host: Baculovirus

TH / Tyrosine Hydroxylase Protein QC Testing

• Purity: > 85% as determined by SDS-PAGE.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met
• Molecular Mass: The recombinant mouse TH consists of 516 amino acids and has a calculated molecular mass of 58 KDa. It migrates as an approximately 65KDa band in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10%gly
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: TH / Tyrosine Hydroxylase protein

TH / Tyrosine Hydroxylase Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

TH / Tyrosine Hydroxylase Protein Description

Tyrosine Hydroxylase (TH, or TyrH) is the rate-limiting enzyme of catecholamine biosynthesis. Tyrosine Hydroxylase uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to DOPA. Its amino terminal 150 amino acids comprise a domain whose structure is involved in regulating the enzyme's activity. The TH enzyme is inhibited in feedback fashion by the catecholamine neurotransmitters. Dopamine binds to Tyrosine Hydroxylase competitively with tetrahydrobiopterin, and interacts with the R domain. Activity of tyrosine hydroxylase is regulated by feedback inhibition and inactivation by catecholamines, and activation by protein phosphorylation. Tyrosine Hydroxylase is modified in the presence of NO, resulting in nitration of tyrosine residues and the glutathionylation of cysteine residues. Tyrosine Hydroxylase involved in the pathogenesis of PD at several different levels, in addition to being a promising candidate for developing new treatments of this disease.

References

1. Fujisawa H. et al., 2005, Biochem Biophys Res Commun. 338 (1): 271-6.
2. Daubner SC. et al., 2011, Arch Biochem Biophys. 508 (1): 1-12.
3. Haavik J. et al., 1998, Mol Neurobiol. 16 (3): 285-309.