Western blot analysis of TH phosphorylation in purified non-phosphorylated rat recombinant TH fusion protein (A) and untreated PC-12 (B) and KCl-stimulated PC-12 (C) whole cell lysates.
recommended for detection of Ser 19 phosphorylated TH of rat origin by WB, IP and IF
Modification
Phosphoralated
Modification Notes
The enzyme tyrosine hydroxylase (TH), also designated tyrosine 3-monooxygenase (TY3H), catalyzes the conversion of tyrosine to L-DOPA. This is the rate limiting step in the biosynthesis of catecholamines such as dopamine, adrenalin and noradrenalin.Protein Kinase A (PKA) mediated phosphosphorylation at Serine 40 causes increased TH catalytic activity. Expressed mainly in the brain and adrenal glands, TH may play a role in the pathogenesis of Parkinson’s disease and the associated reduction in dopamine levels. The human tyrosine hydroxylase gene maps to 11p15. The phosphorylation of rat TH on Ser 19 by CaMKII leads to an increase in TH catalytic activity.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIF
WB:1:500~1:2000 IP:1:100~1:500 IF:1:200~1:500 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Ser 19 phosphorylated TH of rat origin by WB IP and IF
Tissue Specificity
recommended for detection of Ser 19 phosphorylated TH of rat origin by WB, IP and IF
Application
Application
Western blot analysis of TH phosphorylation in purified non-phosphorylated rat recombinant TH fusion protein (A) and untreated PC-12 (B) and KCl-stimulated PC-12 (C) whole cell lysates.
Application Notes
WB:1:500~1:2000 IP:1:100~1:500 IF:1:200~1:500 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.