• Purity

  >97%, by SDS-PAGE under reducing conditions and visualized by silver stain.

• Endotoxin Level

  <0.01 EU per 1 μg of the protein by the LAL method.  

• Activity

  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 Asp25-Ser53 (B chain) & Gln162-Cys185 (A chain)

• Accession #

• N-terminal Sequence    
  Analysis

  Asp 25 (B chain)

  Gln 162 (A chain): not observed, predicted

• Structure / Form

  Disulfide-linked heterodimer    
   

• Predicted Molecular Mass

  2.7 kDa (A chain); 3.3 kDa (B chain)

   

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Relaxin-2

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).

• 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.

• Entrez Gene IDs:

  6019 (Human)

• Alternate Names:

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