Tph1 (phospho S260) polyclonal antibody
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More Files
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Western Blot (Tissue lysate)
Western blot of rat brainstem lysate showing specific immunolabeling of the ~55k Tph1 protein phosphorylated at Ser260. The labeling is specifically blocked by the phosphopeptide (Phos-pep, lane 1) used as antigen. The corresponding non-phosphopeptide (Nonphos-pep, lane 2) did not block the immunolabeling.
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Specification
Product Description
Rabbit polyclonal antibody raised against synthetic phosphopeptide of Tph1.
Immunogen
Synthetic phosphopeptide corresponding to residues surrounding S260 of rat Tph1.
Host
Rabbit
Theoretical MW (kDa)
55
Reactivity
Bovine, Chicken, Dog, Human, Mouse, Rat, Zebra fish
Specificity
Specific for the ~55 KDa tryptophan hydroxylase protein phosphorylated at Ser260. It is anticipated that This antibody will react with bovine, canine, chicken, mouse and zebra fish based on the fact that these species have 100% homology with the amino acid sequence used as antigen.
Form
Liquid
Purification
Affinity purification
Recommend Usage
Western Blot (1:1000)
The optimal working dilution should be determined by the end user.Storage Buffer
In 10 mM HEPES, 150 mM NaCl, pH 7.5 (50% glycerol, 10% BSA)
Storage Instruction
Store at -20°C.
Aliquot to avoid repeated freezing and thawing. -
Applications
Western Blot (Tissue lysate)
Western blot of rat brainstem lysate showing specific immunolabeling of the ~55k Tph1 protein phosphorylated at Ser260. The labeling is specifically blocked by the phosphopeptide (Phos-pep, lane 1) used as antigen. The corresponding non-phosphopeptide (Nonphos-pep, lane 2) did not block the immunolabeling. -
Gene Info — Tph1
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Publication Reference
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A structural approach into human tryptophan hydroxylase and its implications for the regulation of serotonin biosynthesis.
Martinez A, Knappskog PM, Haavik J.
Current Medicinal Chemistry 2001 Jul; 8(9):1077.
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Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling.
Jiang GC, Yohrling GJ 4th, Schmitt JD, Vrana KE.
Journal of Molecular Biology 2000 Sep; 302(4):1005.
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Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A.
Johansen PA, Jennings I, Cotton RG, Kuhn DM.
Journal of Neurochemistry 1996 Feb; 66(2):817.
Application：IP, Purified proteins.
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A structural approach into human tryptophan hydroxylase and its implications for the regulation of serotonin biosynthesis.
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