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Recombinant Human Relaxin-3 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Relaxin-3 Protein, CF Summary

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.

Applications/Dilutions

Dilutions
  • Bioactivity
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.

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Relaxin-3 Protein, CF

  • H3
  • INSL7
  • M3
  • relaxin 3
  • Relaxin3
  • Relaxin-3
  • RLN3
  • RXN3
  • ZINS4

Background

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).

  1. Kizawa, H. et al. (2003) Regul. Pept. 113:79.
  2. Wilkinson, T.N. et al. (2005) BMC Evol. Biol. 5:14.
  3. Bathgate, R.A. et al. (2006) Pharmacol. Rev. 58:7.
  4. Liu, C. et al. (2005) Ann. N.Y. Acad. Sci. 1041:47.
  5. Tanaka, M. et al. (2005) Eur. J. Neurosci. 21:1659.
  6. Liu, C. et al. (2003) J. Biol. Chem. 278:50754.
  7. Rosengren, K.J. et al. (2006) J. Biol. Chem. 281:5845.
  8. Liu, C. et al. (2003) J. Biol. Chem. 278:50765.

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Bioinformatics

Gene Symbol RLN3
Uniprot