TH / Tyrosine Hydroxylase Antibody (Antigen Affinity Purified)

TH / Tyrosine Hydroxylase Antibody ( Antigen Affinity Purified ) Datasheet

TH / Tyrosine Hydroxylase Antibody Product Information

• Immunogen: Recombinant Mouse TH / Tyrosine Hydroxylase protein (Catalog#50997-M07B)
• Antibody Type: Rabbit Polyclonal Antibody ( Antibody Purification Platform )
• Ig Type: Rabbit IgG
• Formulation: 0.2 μm filtered solution in PBS with 5% trehalose
• Preparation: Produced in rabbits immunized with purified, recombinant Mouse TH / Tyrosine Hydroxylase (rM TH / Tyrosine Hydroxylase; Catalog#50997-M07B; P24529; Pro 2-Ser 498). TH / Tyrosine Hydroxylase specific IgG was purified by Mouse TH / Tyrosine Hydroxylase affinity chromatography.

TH / Tyrosine Hydroxylase Antibody Usage Guide

• Specificity: Mouse TH / Tyrosine Hydroxylase
• Immunochemistry: IHC-P: 0.1-2 μg/mL

  

  Immunochemical staining of mouse TH in mouse brain with rabbit polyclonal antibody (1 μg/mL, formalin-fixed paraffin embedded sections).

• Direct ELISA: This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect Mouse TH.
• Storage: This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.
  Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.

TH / Tyrosine Hydroxylase Antibody Background

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, 508 (1): 1-12.
3. Haavik J. et al., 1998, Mol Neurobiol. 16 (3): 285-309.