Neurotensin (NT) is an endogenous tridecapeptide neurotransmitter that influences distinct central and peripheral physiological functions in mammals. Central administration of NT modulates dopaminergic transmission and triggers hypothermic and naloxone-insensitive analgesic responses, whereas peripheral effects include hypotension, decrease gastric acid release, potentiation of lipid digestion. NT is widely distributed throughout the CNS. It has been localized to catecholamine-containing neurons. NT initiates its biological action by interacting with two distinct G-protein coupled receptors (NTR1 and NTR2). Recently, a third receptor NTR3 has been identified that is identical to gp95/sortilin and it is not coupled via the G-proteins. All three receptors bind NT through its C-terminal hexapeptide sequence (8 RRPYIL 13). Biologically active NT (NT8-13) has also been shown to interact with the extracellular domain 3 (between TM6-7) of NTR1.

NTR1/NTRH/NTSR1/NT1 (mouse/rat 424 aa; human 418 aa, chromosome 20q1; ~84% interspecies sequence homology) is the levocabastine-insensitive, high affinity receptor for NT. It has the typical structure of GPCR: 7 TM domains with extracellular N-terminus and cytoplasmic C-terminus. It is shown to mediate a number of peripheral and central NT responses, including the neuroleptic-like effects of the peptide. It is highly expressed in the brain, small intestine, and other peripheral tissues.

Mouse synthetic peptide

Highly purified

As reported

Supplied as a liquid in PBS, pH 7.2

The mouse sequence 84% conserved in rat and human NTR1

This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.