Quick Search
Products Polyclonal Anti-TH
| Catalogue number: | PA1732 |
| Price: | $200.00 |
| Reactivities: | Human, Mouse, Rat |
| Applications: | Immunohistochemistry, Western Blot |
| Size: | 100ug/vial |
| Gene: | TH |
| Swiss prot: | P07101 |
| Form: | Lyophilized |
| Format: | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
| Storage temp: | At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing. |
| Scientific background: | TH(Tyrosine hydroxylase) is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). It does so using molecular oxygen (O2), as well as iron (Fe2+) and tetrahydrobiopterin as cofactors. L-DOPA is a precursor for dopamine, which, in turn, is a precursor for the important neurotransmitters norepinephrine (noradrenaline) and epinephrine (adrenaline). Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines. In humans, tyrosine hydroxylase is encoded by the TH gene, and the enzyme is present in the central nervous system (CNS), peripheral symphatic neurons and the adrenal medulla. Tyrosine hydroxylase, phenylalanine hydroxylase and tryptophan hydroxylase together make up the family of aromatic amino acid hydroxylases (AAAHs). The human tyrosine hydroxylase gene is mapped to chromosome 11p15 using somatic cell hybridization. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. |
| References: | 1.Bartholome, K., Dworniczak, B., Ludecke, B.Linkage of the tyrosine hydroxylase gene and Segawa's syndrome. (Abstract)Am. J. Hum. Genet. 53 (suppl.): A889 only, 1993. 2.Bodeau-Pean, S., Ravassard, P., Neuner-Jehle, M., Faucheux, B., Mallet, J., Dumas, S.A human tyrosine hydroxylase isoform associated with progressive supranuclear palsy shows altered enzymatic activity.J. Biol. Chem. 274: 3469-3475, 1999. 3.Nagatsu, T., Ichinose, H.Comparative studies on the structure of human tyrosine hydroxylase with those of the enzyme of various mammals.Comp. Biochem. Physiol. 98: 203-210, 1991. |
| Additional info: | A synthetic peptide corresponding to a sequence in the middle region of human TH, identical to the related rat sequence, and different from the related mouse sequence by one amino acid. |
Get the Best Promotions
