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Recombinant Human Relaxin-2 (B-33/A-24) Protein, CF

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Relaxin-2 (B-33/A-24) Protein, CF Summary

Additional Information
Replaces 2804-RN/CF
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 0.5‑2.5 ng/mL.
Source
E. coli-derived human Relaxin-2 protein
Val23-Arg55 (B chain), with an N-terminal Met & Gln162-Cys185 (A chain)
Accession #
N-terminal Sequence
Met (B chain), Gln162 (A chain)
Structure / Form
Disulfide-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
Gene
RLN2
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
2.7 kDa (A chain), 3.9 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.
Publications
Read Publications using
3596-RN/CF in the following applications:

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
>97%, 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-2 (B-33/A-24) Protein, CF

  • bA12D24.1.1
  • bA12D24.1.2
  • H2
  • relaxin 2
  • Relaxin2
  • Relaxin-2
  • RLN2
  • RLXH2

Background

Human Relaxin-2, also called H2 Relaxin, is a 6 kDa, 53 amino acid (aa) nonglycosylated, heterodimeric polypeptide that plays an important role in female reproduction (1, 2). Relaxin belongs to a structurally related insulin/relaxin superfamily that currently contains 10 members in human (2). To date, three human relaxin genes have been identified (1, 2). Among these, Relaxin-2 is best studied and the only known Relaxin to circulate in the blood (2, 3). As with other insulin/relaxin superfamily members, human Relaxin-2 is synthesized as a preprohormone (4). It is 18 kDa in size and 185 aa in length. It contains a 24 aa signal sequence, a 3.3 kDa, 31 aa B domain, a 106 aa C (or connecting) domain, and a C-terminal, 2.7 kDa, 24 aa A domain (2, 4, 5). Upon removal of the signal peptide, two intrachain disulfide bonds are created between the B and A chains. This is followed by prohormone convertase removal of the intervening C chain, creating a disulfide-linked heterodimer. Initially, the B chain is 31 aa in length and terminates with a Lys‑Arg dipeptide. This is subsequently cleaved by a carboxypeptidase to generate a 29 aa mature chain (5). The mature human Relaxin-2 heterodimer is 48%, 44% and 43% aa identical to rat, canine and porcine Relaxin-2, respectively. Human Relaxin-2 is 35% and 75% aa identical to human Relaxin-3 and 1, respectively. An alternate splice form for human Relaxin-2 has been reported (6). It is identical to the standard form through the first 70 aa of the preproprecursor. At this point, a 47 aa substitution occurs that appears to be absent in typical cleavage motifs. Relaxin confers its activity by binding to leucine-rich guanine nucleotide-binding (G-protein) coupled receptors, LGR7 and LGR8 (2, 7). Relaxin is best known as a hormone of parturition that promotes growth and softening of the cervix, and development of the mammary gland (2, 3). It also has a marked impact on the uterus. In particular, it promotes angiogenesis, inhibits MMP production and activity, and down‑regulates estrogen receptor-alpha expression (8).

  1. Hayes, E.S. (2004) Reprod Biol Endocrinol. 2:36.
  2. Sherwood, O.D. (2004) Endocr. Rev. 25:205.
  3. Wilkinson, T.N. et al. (2005) BMC Evol. Biol. 5:14.
  4. Hudson, P. et al. (1984) EMBO J. 3:2333.
  5. Marriott, D. et al. (1992) Mol. Endocrinol. 6:1441.
  6. Gunnersen, J.M. et al. (1996) Mol. Cell. Endocrinol. 118:85.
  7. Hsu, S.Y. et al. (2002) Science. 295:671.
  8. Goldsmith, L.T. et al. (2004) Proc. Natl. Acad. Sci. USA 101:4685.

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Publications for Relaxin-2 (3596-RN/CF)(4)

We have publications tested in 4 confirmed species: Human, Mouse, Rat, Hamster.

We have publications tested in 2 applications: Bioassay, In Vivo.


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Bioassay
(2)
In Vivo
(2)
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Human
(1)
Mouse
(2)
Rat
(1)
Hamster
(1)
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Bioinformatics

Gene Symbol RLN2
Uniprot