|Tested species reactivity||Human, Rat|
|Host / Isotype||Sheep / IgG|
|Immunogen||Recombinant rabbit tryptophan hydroxylase, isolated as inclusion bodies from E. coli and purified by preparative SDS-PAGE|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 100µg/ml BSA, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunohistochemistry (Frozen) (IHC (F))||1:1000|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody is predicted to react with wide variety of mammals based on 100% sequence homology, however it does not recognize TPH in rabbit tissues.
This antibody is specific for the ~55 kDa TPH protein in Western blots of human dorsal Raphe nucleus. Immunolabeling has been demonstrated in rat brain extracts.
Tryptophan hydroxylase (TPH) catalyzes the first step in the biosynthesis of serotonin and melatonin (Martinez et al., 2001). Thus expression of TPH can be used as an indicator of the localization of serotonin and melatonin in brain. In mammals, serotonin biosynthesis occurs predominantly in neurons which originate in the Raphe nuclei of the brain, and melatonin synthesis takes place within the pineal gland (Haycock et al., 2002) . Although TPH catalyzes the same reaction within the Raphe nuclei and the pineal gland, TPH activity is rate-limiting for serotonin but not melatonin biosynthesis (Martinez et al., 2001).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.