Anti-TRPC6, clone TRPC6/7671

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Phenylalanine hydroxylase (PAH), tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) comprise a small family of monooxygenases that use tetrahydropterine as a cofactor during the catabolism of aromatic L-amino acids. PAH, TH and TPH all contain catalytic domains with an amino-terminal regulatory domain and a short carboxy-terminal tetramerization domain. Each of these enzymes also contains a single ferrous iron atom, which is bound to two histidines and a glutamate, and is likely to be involved in the formation of the hydroxylating intermediate. TPH is both the first and rate-limiting-step in the biosynthesis of serotonin in the central nervous system and melatonin in the pineal gland. Alteration of TPH function may be a key factor in the pathology of several neuropsychiatric disorders associated with serotonin, including depression, aggression, alcoholism and schizophrenia. For instance, LDOPA, which is used as a common therapy for Parkinson s disease (PD) patients, inhibits TPH function which, subsequently, is thought to contribute to the onset of depression in PD patients. Protein function: Thought to form a receptor-activated non-selective calcium permeant cation channel (PubMed:19936226, PubMed:23291369). Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C (PubMed:26892346). Seems not to be activated by intracellular calcium store depletion. [The UniProt Consortium]