• Purity

  >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When Recombinant Mouse R‑Spondin 3 (Catalog # ) is coated at 0.25 μg/mL, Recombinant Mouse RNF43 Fc Chimera binds with an ED    ₅₀ = 0.8-4.8 ng/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Mouse RNF43 (Ala34-Tyr197) Accession # Q5NCP0	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• N-terminal Sequence    
  Analysis

  Ala34 & Val36    
   

• Structure / Form

  Disulfide-linked homodimer    
   

• Predicted Molecular Mass

  45 kDa

• SDS-PAGE

  53-63 kDa, reducing conditions    
   

Background: RNF43

RING finger protein 43 (RNF43) is a 90 kDa member of the ZNRF3 family of ubiquitin ligase proteins (1, 2). Mouse RNF43 is synthesized as a 784 amino acid (aa) protein that contains a putative 23 aa signal sequence, a 174 aa extracellular domain (ECD), a transmembrane domain, and a cytoplasmic domain with an atypical RING-type zinc finger (1). RNF43 is expressed in stem cells at the bottom of colon crypts, where it limits the ability of Wnts to induce proliferation (3). RNF43 and ZNRF3, another transmembrane E3 ubiquitin ligase, ubiquitinate and promote the turnover of Frizzled Wnt receptors to antagonize Wnt signaling (3, 4). RNF43 has been shown to suppress both canonical and non-canonical Wnt signaling pathways by distinct mechanisms (5). RNF43/ZNRF3-mediated turnover of Frizzled receptors is inhibited by R-Spondin (4). Dishevelled, a positive regulator of Wnt signaling, interacts with RNF43/ZNRF3 to mediate turnover of Frizzled receptors (6). RNF43 may promote cell survival by binding to NEDL1 and by suppressing the transcriptional activity of p53 (7, 8). RNF43 has been shown both to inhibit and promote cancer. Deletion of RNF43, as well as mutations found in colorectal and other cancers, allows hypersensitivity to Wnts and promotes adenoma formation (3, 9). Furthermore, RNF43 down-regulation in gliomas is associated with poor prognosis (10). However, RNF43 is frequently over-expressed in cancers, correlating with growth-promoting activity and colorectal and hepatocellular cancer pathogenesis (1, 7, 11).

• References:

1. Yagyu, R. et al. (2004) Int. J. Oncol. 25:1343.

2. de Lau, W. et al. (2014) Genes Dev. 28:305.

3. Koo, B.K. et al. (2012) Nature 488:665.

4. Hao, H.X. et al. (2012) Nature 485:195.

5. Tsukiyama, T. et al. (2015) Mol. Cell. Biol. 35:2007.

6. Jiang, X. et al. (2015) Mol. Cell 58:522.

7. Xing, C. et al. (2013) Mol. Cancer Ther. 12:94.

8. Shinada, K. et al. (2011) Biochem. Biophys. Res. Commun. 404:143.

9. Giannakis, M. et al. (2014) Nat. Genet. 46:1264.

10. Xi, S. et al. (2015) Int. J. Clin. Exp. Pathol. 8:490.

11. Uchida, N. et al. (2004) Clin. Cancer Res. 10:8577.

• Long Name:

  Ring Finger Protein 43

• Entrez Gene IDs:

  54894 (Human); 207742 (Mouse); 303412 (Rat)

• Alternate Names:

  DKFZp781H02126; DKFZp781H0392; FLJ20315; FLJ77466; FLJ99338; MGC125630; ring finger protein 43; RNF124; RNF43; URCC