• Species Reactivity

  Human, Mouse

• Specificity

  Detects human Tyrosine Hydroxylase in direct ELISAs and human, mouse and rat Tyrosine Hydroxylase in Western blots. In direct ELISAs, no cross-reactivity with recombinant human Tryptophan Hydroxylase-1 is observed.

• Source

  Monoclonal Mouse IgG    _2B Clone # 779427

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  E. coli-derived recombinant human Tyrosine Hydroxylase    
  Ala278-Tyr401    
  Accession # P07101

• Formulation

  Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Western Blot

  0.25 µg/mL

  See below

• 
  

• Simple Western

  5 µg/mL

  See below

• 
  

• Immunohistochemistry

  8-25 µg/mL

  See below

• 
  

• Immunocytochemistry

  8-25 µg/mL

  See below

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Reconstitution

  Sterile PBS to a final concentration of 0.5 mg/mL.

• Shipping

  The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

• Stability & Storage

  Use a manual defrost freezer and avoid repeated freeze-thaw cycles.    

• 12 months from date of receipt, -20 to -70 °C as supplied.

• 1 month, 2 to 8 °C under sterile conditions after reconstitution.

• 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Tyrosine Hydroxylase

TH (Tyrosine 3-hydroxylase), also known as Tyrosine 3-monooxygenase, is a 60-62 kDa member of the biopterin-dependent aromatic amino acid hydroxylase family of molecules. It is expressed by neurons of the dopamine and autonomic nervous system, plus the neuroendocrine cells of the adrenal medulla. TH is considered the rate limiting enzyme for catecholamine synthesis, and serves to catalyze the hydroxylation of L-tyrosine. It maintains stores of catecholamines following secretion, and its activity is regulated by targeted site phosphorylation. Human TH is 528 amino acids (aa) in length. It contains an N-terminal ACT domain (aa 69-190) that binds small molecules and regulates enzyme activity, and a C-terminal enzymatic region (aa 196-493). There are three significant utilized phosphorylation sites. Two at Ser31 and Ser40 increase enzyme activity, while phosphorylation at Ser19 promotes subsequent Ser40 phosphorylation. TH functions as a 240 kDa noncovalent homotetramer. There are four potential splice variants. One shows a deletion of aa 31-34, a second shows a deletion of aa 31-61, while a third contains a Met substitution for aa 1-34. A fourth isoform variant shows a deletion of aa 35-61. Over aa 278-401, human TH shares 94% aa sequence identity with mouse TH, a molecule that most closely resembles the fourth human isoform variant described above.

• Entrez Gene IDs:

  7054 (Human); 21823 (Mouse); 25085 (Rat)

• Alternate Names:

  DYT14; DYT5b; EC 1.14.16; EC 1.14.16.2; TH; TYH dystonia 14; TYH; Tyrosine 3-hydroxylase; tyrosine 3-monooxygenase; Tyrosine Hydroxylase