Recombinant Human Cerberus 1 Protein, CF

When Recombinant Human Cerberus 1 (Catalog # 9515‑CB) iscoated at 2 µg/mL, Recombinant Human Nodal (Catalog # 3218‑ND) binds with an ED50 = 0.4-2.4 ng/mL.

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

Recombinant Human Cerberus 1 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Cerberus 1 (Catalog # 9515-CB) is coated at 2 µg/mL, Recombinant Human Nodal (Catalog # 3218-ND) binds with an ED₅₀ = 0.4-2.4 ng/mL.
• Source: Trichoplusia ni, T. ni (baculovirus)-derived human Cerberus 1 protein
  

  Human Cerberus 1 (Thr18-Ala267) Accession # O95813	HIEGR	GGGSGGGSGGGS	HHHHHHHHHH
  N-terminus			C-terminus

• Accession #: O95813
• N-terminal Sequence: Thr18
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 31 kDa.
  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: 36-41 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 HCl with Trehalose.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• 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 Human Cerberus 1 Protein, CF

• CER1
• cerberus 1 (Xenopus laevis) homolog (cysteine knot superfamily)
• Cerberus 1
• cerberus 1, cysteine knot superfamily, homolog (Xenopus laevis)
• cerberus
• cerberus-related 1
• Cerberus-related protein
• DAN domain family member 4
• DAND4
• MGC119894
• MGC119895
• MGC96951

Background

Cerberus 1, also called DAND4, is a member of the DAN domain family of BMP antagonists that includes DAN (DAND1), Gremlin/Drm (DAND2), PRDC (Protein Related to Dan and Cerberus; DAND3), and COCO/Dante (DAND5). DAN family members contain a cysteine-knot domain that is homologous to that found in other TGF-beta superfamily ligands (1, 2). Mature human Cerberus 1 shares 67% and 68% amino acid (aa) sequence identity with mouse and rat Cerberus 1, respectively. Within the cysteine-knot domain, it shares 24%-37% aa sequence identity with mouse DAN, Gremlin, PRDC, and COCO. Cerberus 1 is a secreted 38 kDa glycoprotein that forms homodimers (3). Cerberus-S, which is generated by proteolysis in Xenopus, is a short version of the molecule and includes the C-terminal cysteine-knot domain (4). At the onset of gastrulation, Cerberus 1 is transiently expressed in anterior endodermal structures in response to Nodal and Shh (3, 5-9). Cerberus 1 binds BMP-4 and Nodal and inhibits their activities. Xenopus Cerberus has also been shown to bind Xenopus Wnt8. These inhibitory functions of Cerberus favor mesodermal development in the anterior region of the gastrula and suppresses posterior mesodermal differentiation (3, 4, 6, 8, 10-12). In chick and Xenopus, Cerberus 1 also regulates, but is not required for embryonic left-right polarization, neurulation, and head and heart induction (4-8, 13).

1. Avsian-Kretchmer, O. and A.J.W. Hsueh (2004) Mol. Endocrinol. 18:1.
2. Kawano, Y. and R. Kypta (2003) J. Cell Sci. 116:2627.
3. Biben, C. et al. (1998) Dev. Biol. 194:135.
4. Piccolo, S. et al. (1999) Nature 397:707.
5. Zhu, L. et al. (1999) Curr. Biol. 9:931.
6. Tavares, A.T. et al. (2007) Development 134:2051.
7. Foley, A.C. et al. (2007) Dev. Biol. 303:57.
8. Bouwmeester, T. et al. (1996) Nature 382:595.
9. Bertocchini, F. and C.D. Stern (2002) Dev. Cell 3:735.
10. Glinka, A. et al. (1997) Nature 389:517.
11. Perea-Gomez, A. et al. (2002) Dev. Cell 3:745.
12. Takaoka, K. et al. (2007) Curr. Opin. Genet. Dev. 17:344
13. Simpson, E.H. et al. (1999) Dev. Biol. 213:202.

Bioinformatics

• Uniprot:
  • O95813()