Galanin Family Related Drug Discovery Products
Creative Biolabs has the assays you can rely on for high throughput screening, lead optimization, characterizing and discovering targets, and uncovering the complexity of disease pathways. We can offer membrane protein in vitro assay kits that save valuable laboratory time and is ideal for high throughput screening.
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Creative Biolabs offers high-quality, innovative tools to help research groups accelerate membrane protein drug discovery. They can be found by targets. If there is no product that meets your needs, please contact us.
Galanin is a neuropeptide of 29–30 amino acids that is found in both the central and peripheral nervous systems. The peptide is distinct from other families of neuropeptides and exhibits strong N-terminal conservation across a number of mammalian species. With the activation of various receptor subtypes, galanin influences a number of physiological processes. Galanin modifies the release of many neurotransmitters in the CNS. The peptide also modulates how painful stimuli are perceived (nociception). Galanin affects pancreatic β-cells' ability to secrete insulin and either contracts or relaxes a number of gastrointestinal smooth muscles in the periphery.
Creative Biolabs offers a range of galanin family tools with our well-established high-efficient drug discovery strategy in a timely and cost-effective manner:
Overview of Galanin Family
GALR1 was isolated from the human melanoma Bowes cell line. The GALR1 gene, which in humans is translated into a protein with a length of 349 amino acids, is composed of three exons. The interspecies homology of GALR1 is significant; for instance, 93% of the amino acids in human and mouse GALR1 are identical. GALR1 mRNA was initially identified in the small intestine and embryonic brain tissues. Recent studies have also shown that GALR1 is only expressed in the peripheral nervous system and central nervous system. GALR1 mRNA is widely distributed throughout the olfactory regions, amygdala, thalamus, hypothalamus, pons, medulla, and spinal cord. GALR1 mRNA expression is not dynamic during development, in contrast to GALR2, and is regulated by cAMP through the transcription factor CREB.
The human GALR2 gene, which has two exons, is translated to create the 387 amino acid residue long protein. The human hGALR2 protein retains the C-terminal 15 amino acid expansion. Low levels of GALR2 mRNA were found in tissues taken from the large intestine, spleen, heart, and liver, whereas high levels were found in the hippocampus, hypothalamus, brain, amygdala, spinal cord, posterior root ganglion, anterior pituitary, lung, and kidney tissues.
Two exons make up the GALR3 gene, which in humans is translated into a 368 amino acid residue protein. The expression of GALR3 transcripts in the central nervous system is mostly restricted to the hypothalamus and regions of the mid- and hindbrain, while being relatively common in peripheral tissues.
Fig.1 Galanin receptors and their transduction mechanisms. (Liu & Hökfelt, 2002)
Galanin Family Drug Discovery
The identification of therapeutic targets related to disease states is a crucial phase in the drug development process. Studies on GALP pharmacology, genetics, and biochemistry have substantially benefited from the identification and molecular cloning of three GALP subtypes. High-throughput screening of small molecule compounds in search of galanin antagonists and agonists will be made possible by the expression of these receptors. The area of galanin has become more complex as a result of the discovery of GALP-like receptors and GALPs, but this complexity may also present new prospects for the discovery of medications that target GALPs.
Reference
- Liu, H.X., & Hökfelt, T. The participation of galanin in pain processing at the spinal level. Trends in pharmacological sciences. 2002, 23(10): 468-474.
