Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Details of Functionality | Measured by its ability to induce cAMP accumulation in THP‑1 human acute monocytic leukemia cells. Parsell, D.A. et al. (1996) J. Biol. Chem. 271:27936. The ED50 for this effect is 3.5‑17.5 ng/mL. |
Source | E. coli-derived human Relaxin-3 protein Asp119-Cys142 (A chain) & Ala27-Arg53 (B chain) |
Accession # | |
N-terminal Sequence | Asp119 (A chain) & Ala27 (B chain) |
Structure / Form | Disulfide-linked heterodimer |
Protein/Peptide Type | Recombinant Proteins |
Gene | RLN3 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 2.46 kDa (A chain), 3.04 kDa (B chain). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Human Relaxin-3 (H3 relaxin, INSL7) is one of seven relaxin-like peptides belonging to the insulin superfamily (1 - 4). Unlike human relaxins 1 and 2, it does not play a role in reproduction but appears to be a neuropeptide involved in stress response in the brain stem (3 - 5). The 142 amino acid (aa) Relaxin-3 pre-proprotein is processed to remove a 25 aa signal peptide and a connecting peptide (aa 53 - 118). The resulting mature Relaxin-3 is a 5.5 kDa, 51 aa secreted heterodimer of A (aa 119 - 142) and B (aa 26 - 52) peptides connected by two intermolecular disulfide bonds (1). Mature human Relaxin-3 is 96%, 94%, and 92% aa identical to porcine, canine, and mouse Relaxin-3, respectively. This is much higher identity between species than that seen for other relaxins. Relaxin-3 is thus suggested to be the ancestral relaxin family member (2). Relaxin-3 is the only known ligand for the G-protein-coupled receptor GPCR135, designated RXFP3 (4, 6). In rodents, GPCR135 is expressed primarily in the supraoptic and paraventricular nucleus (6). This region has connections to the dorsal tegmental region of the pons (also called the nucleus incertus), where expression of Relaxin-3 is highest (5). Relaxin-3 also binds the more widely-expressed LGR7 (RXFP1) receptor, but with lower affinity than that of Relaxin-2 (1, 7). Although binding of Relaxin-3 to LGR7 increases intracellular cAMP, binding to GPCR135 inhibits cAMP accumulation, indicating coupling to Gi, Go or Gz by this receptor (1, 5). Relaxin-3 expression does not overlap well with its other receptor, GPCR142, which instead appears to be the primary receptor for INSL5 (3, 8).
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