Search
Search
Invitrogen
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.promotions']}}
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.viewpromo']}}
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.promocode']}}: {{promo.promoCode}} {{promo.promoTitle}} {{promo.promoDescription}}. {{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.learnmore']}}
PA1-763 detects phospho serotonin N-acetyltransferase (AA-NAT) from rat tissues.
PA1-763 has been successfully used in Western blot procedures. By Western blot, this antibody detects an ~23 kDa protein representing phosphorylated AA-NAT from rat pineal gland whole protein extract.
PA1-763 immunizing phosphopeptide (Cat. # PEP-066) corresponds to carboxy-terminal amino acid residues 198-208 of rat AA-NAT. Total anti-carboxy-terminal AA-NAT-specific IgG (Cat. # PA1-762) was affinity purified on resin-coupled non-phosphopeptide (Cat. # PEP-065). Phospho-specific carboxy-terminal IgG (Cat. # PA1-763) was subsequently isolated on resin-coupled phosphopeptide (Cat. # PEP-066). This sequence is completely conserved between rat and mouse AA-NAT protein.
Arylalkylamine N-Acetyltransferase (AANAT) is the penultimate enzyme is melatonin synthesis. Hormonal melatonin has been implicated in sleep and circadian clock function. Large changes in the abundance of AANAT are believed to be responsible for the large day/night rhythms in melatonin synthesis in the pineal gland and retina. Most research shows that AANAT activity is regulated by controlling the steady-state levels of the protein. Recent research, however, suggests that another mechanism may also play a role in controlling melatonin production without altering AANAT protein and activity. This mechanism may explain the sudden physiological increase in circulating melatonin observed at the onset of the dark period in humans.
仅用于科研。不用于诊断过程。未经明确授权不得转售。