Recombinant Mouse Relaxin-1 Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Relaxin-1 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 2-8 ng/mL.
• Source: E. coli-derived mouse Relaxin-1 protein
  Arg23-Arg54, with an N-terminal Met (B chain) & Glu161-Cys185 (A chain)
• Accession #: P47932
• N-terminal Sequence: Met (B chain) & Glu161 (A chain)
• Structure / Form: Disulfide-linked heterodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Rln1
• 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: 3.7 kDa (B chain) & 2.7 kDa (A 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.
• SDS-PAGE: 4 & 3 kDa, reducing conditions

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 PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Mouse Relaxin-1 Protein, CF

• bA12D24.3.1
• bA12D24.3.2
• H1
• preprorelaxin H1
• prorelaxin H1
• relaxin 1 (H1)
• relaxin 1
• relaxin H1
• Relaxin1
• Relaxin-1
• RLN1
• RLXH1

Background

Mouse Relaxin-1 (RLN1 or M1 relaxin) is the counterpart of human relaxin-2 (H2 relaxin) within the structurally related insulin/relaxin superfamily, while orthologs of the human relaxin-1 are found only in higher primates (1, 2). As with other insulin/relaxin superfamily members, RLN1 is synthesized as a preprohormone (1 ‑ 3, 5). Processing of the 21 kDa preprorelaxin-1 includes removal of the signal sequence, formation of two disulfide bonds between A and B chains and removal of the intervening C‑chain by a prohormone convertase. The resulting mature protein is an unglycosylated 6 kDa dimer of disulfide-linked A and B chains that binds the leucine-rich G-protein coupled receptor RXFP1, previously called LGR7 (1 ‑ 4). Mouse RLN1 shares only 67%, 39%, 36% and 42% amino acid (aa) identity with rat, equine and feline RLN1 and human Relaxin-2, respectively, and its activity shows partial species specificity. For example, a unique amino acid near the end of the A chain in mice, Tyr184, lowers its affinity for RXFP1 compared to other species (5). Mouse RLN1 is prominently expressed in the prostate and ovary, with lower levels in the brain, heart and other organs (1 ‑ 3). In the prostate, RLN1 is anti-apoptotic and contributes to development and maintenance of male fertility (6). In the female mouse, circulating RLN1 produced by the corpus luteum during pregnancy is essential for growth and softening of the cervix and vagina in preparation for delivery. It also promotes development of the mouse mammary apparatus, regulates plasma osmolality, and increases cardiac output and glomerular filtration rate in pregnancy (1, 2). Many RLN1 effects on reproductive tissues are augmented by estrogen (1 ‑ 3, 7). In non‑reproductive tissues, RLN1 mediates collagen turnover (7). RLN1-deficient mice develop age‑related fibrosis and smooth muscle hypertrophy in organs such as lung, heart, kidney and liver (7 ‑ 10).

1. Kong, R.C.K. et al. (2010) Mol. Cell. Endocrinol. 320:1.
2. Sherwood, O.D. (2004) Endocr. Rev. 25:205.
3. Callander, G.E. and R.A.D. Bathgate (2010) Cell. Mol. Life Sci. 67:2327.
4. Hsu, S.Y. et al. (2002) Science 295:671.
5. Schwabe, C. and E. E. Bullesbach (1994) FASEB J. 8:1152.
6. Samuel, C.S. et al. (2003) Lab. Invest. 83:1055.
7. Lekgabe, E.D. et al. (2006) Endocrinology 147:5575.
8. Samuel, C.S. et al. (2003) FASEB J. 17:121.
9. Bennett, R.G. (2009) Transl. Res. 154:1.
10. Hewitson, T.D. et al. (2007) Endocrinology 148:660.

Bioinformatics

• Gene Symbol: Rln1
• Uniprot:
  • P47932()