Galanin (2-12) acid


  • Description

  • Application Data


An N-terminal fragment of galanin (2-12) acid form; galanin is a widely distributed neuropeptide with a wide variety of roles, including weight management and mental health.

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Application Data

Catalogue number crb1001306
Molecular Weight 1193.6
Sequence (one letter code)


Sequence (three letter code)


Purity >95%
Storage -20°C

Ihnatko et al., (2017). Short N-terminal galanin fragments are occurring naturally in vivo. Neuropeptides, 63: 1.  doi: 10.1016/j.npep.2017.03.005.

Liu et al., (2001). Receptor subtype-specific pronociceptive and analgesic actions of galanin in the spinal cord: selective actions via GalR1 and GalR2 receptors. Proc Natl Acad Sci USA, 98: 9960. doi: 10.1073/pnas.161293598.

Manufactured in: United Kingdom
Data Sheet Material Safety Data Sheet (MSDS)

Galanin is a neuropeptide synthesised and released by the brainstem locus coeruleus (LC). Galanin is expressed in most LC neurons in rodents and humans. Galanin has been shown to inhibit LC activity by hyperpolarising LC neurons, suppressing their spontaneous firing rate, and enhancing α2-adrenergic receptor-mediated negative feedback. Galanin is also a potent trophic and neuroprotective factor throughout the nervous system.

Galanin is widely distributed from the central nervous, peripheral, and endocrine systems. Galanin’s overarching function is as an inhibitory, hyper-polarizing neuromodulator for classical neurotransmitters like acetylcholine and serotonin. Galanin interacts with 3 receptor subtypes, GalR1-3 G protein-coupled receptors  which are inserted into the plasma membrane. GalR1 is believed to activate a Gβγ pathway to regulate MAPK activation. GalR2 can also activate the MAPK pathway, but unlike GalR1, there is detectable inositol phosphate production. GalR3 is associated with the Gαi/o pathway. Activation of the receptor leads to a cellular influx of K+. Each receptor has been associated with neurological diseases such as GalR3 and epilepsy.

Some N-terminal fragments naturally occur in vivo but their relevance is unclear. The physiological relevance of the galanin fragment (2-12) and its affinity to the various GalR receptors has yet to be made clear. Binding assays and displacement assays in rat brain tissue have been performed with similar N-terminal galanin fragments to try and elucidate their function. . The use of N-terminal fragments such as galanin (2-12) can help clarify the function of full-length galanin. This may highlight new agonists/antagonists for the galanin GalR receptors that can be putative therapeutic targets for treatments of conditions such as cardiovascular disease.

NMR has used this galanin fragment (2-12) to help characterise the structure of galanin. It shows the critical residues Tyr(9), Leu(10), and Leu(11) for interaction with the galR receptors. They cluster together as collapsed hydrophobic residues irrelevant to forming higher-order structures.

Galanin (2-12) acid

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