Relaxin 2 (B-29/A-24), Recombinant, Human (RLN2, bA12D24.1.1, bA12D24.1.2, H2, Prorelaxin H2, RLXH2)

Human Relaxin-2, also called H2 Relaxin, is a 6kD, 53aa 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 18kD in size and 185 aa in length. It contains a 24 aa signal sequence, a\n3.3kD, 31 aa B domain, a 106 aa C (or connecting) domain, and a C-terminal, 2.7kD, 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-a expression (8).\n\nSource:\nRecombinant corresponding to Asp25-Ser53 (B chain) and Gln162-Cys185 (A chain), expressed in E.coli.\n\nMolecular Weight: \n~2.7kD (A chain) 3.3kD (B chain)\n\nEndotoxin Level:\n(same/less than)1EU/1ug (LAL)\n\nBiological Activity:\nMeasured 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 typically 0.5-2.5ng/ml.\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with PBS. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

R1425-02M

Size

25ug

Form

Supplied as a lyophilized powder in sodium acetate. Reconstitute with PBS to 100ug/ml.

Purity

~97% (SDS-PAGE)

References

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.