Recombinant Mouse Dkk-1 C-Terminal Fragment Protein, CF

When Recombinant Mouse LRP-6 (C‑Terminal Fragment) FcChimera is immobilized onto a Goat anti-human IgG Fc coated plate, RecombinantMouse Dkk‑1 C-Terminal Fragment (Catalog # 9838-DK) binds with anED50 of 30-240 ng/mL.

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

Recombinant Mouse Dkk-1 C-Terminal Fragment Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse LRP-6 (C-Terminal Fragment) Fc Chimera is immobilized onto a Goat anti-human IgG Fc coated plate, Recombinant Mouse Dkk‑1 C-Terminal Fragment binds with an ED₅₀ of 30-240 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived mouse Dkk-1 protein
  Asp145-His272, with an N-terminal 6-His tag
• Accession #: O54908
• N-terminal Sequence: His
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, 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: 15 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: 19-38 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, 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 Mouse Dkk-1 C-Terminal Fragment Protein, CF

• dickkopf (Xenopus laevis) homolog 1
• dickkopf homolog 1 (Xenopus laevis)
• dickkopf related protein-1
• Dickkopf-1
• dickkopf-related protein 1
• Dkk1
• Dkk-1
• hDkk-1
• SKdickkopf-1 like

Background

Dickkopf related protein 1 (Dkk-1) is the founding member of the Dickkopf family of proteins that includes Dkk-1, -2, -3, -4, and a related protein, Soggy (1, 2). Mature mouse Dkk-1 is a 40 kDa secreted glycoprotein that consists of two conserved cysteine-rich domains (CRDs), CRD1 (N-terminal) and CRD2 (C-terminal), separated by a linker region (1, 3). Within the C-terminal fragment [amino acid (aa) 145 - 272] that includes the CRD2, mouse Dkk-1 shares 94% and 86% aa sequence identity with rat and human Dkk-1, respectively.  Dkk-1 antagonizes Wnt/beta-catenin signaling, an activity for which the C-terminal CRD2 is both necessary and sufficient (4, 5), and the C-terminal fragment has been shown to interact with LRP5 or LRP6 (6). However, crystallographic studies have shown that Dkk-1 interacts with LRP-6 as a bipartite inhibitor, with both CRDs binding the extracellular domain of LRP-6 simultaneously (4, 7-9). Mechanistically, Dkk-1 has been shown to promote the internalization and degradation of LRP-6, but mouse Dkk-1 may inhibit LRP-6 independently of this process (10, 11). Mice lacking Dkk-1 die at birth, lack anterior head structures, and have limb malformations (12). Accordingly, bone mass in mice has been found to be inversely proportional to Dkk-1 levels (13). Reduced Dkk-1 expression causes head, limb, and vertebrae defects in mice (14). Conversely, transgenic mice that overexpress Dkk-1 develop osteopenia (15). In addition to bone homeostasis, Dkk-1 expression may be required for neural differentiation of mouse embryonic stem (ES) cells (16, 17). Dkk-1 also likely has a complex role in cancer, as it has been shown to act as a tumor suppressor and also to promote metastasis (18).

1. Glinka, A. et al. (1998) Nature 391:357.
2. Niehrs, C. (2006) Oncogene 25:7469.
3. Ahn, V.E. et al. (2011) Dev. Cell 21:862.
4. Mao, B. et al. (2001) Nature 411:321.
5. Brott, B.K. and S.Y. Sokol (2002) Mol. Cell. Biol. 22:6100.
6. Kimura, H. et al. (2016) J Clin Invest. 126:7.
   
7. Chen, S. et al. (2011) Dev. Cell 21:848.
8. Bourhis, E. et al. (2011) Structure 19:1433.
9. Cheng, Z. et al. (2011) Nat. Struct. Mol. Biol. 18:1204.
10. Mao, B. et al. (2002) Nature 417:664.
11. Semënov, M.V. et al. (2008) J. Biol. Chem. 283:21427.
12. Mukhopadhyay, M. et al. (2001) Dev. Cell 1:423.
13. MacDonald, B.T. et al. (2007) Bone 41:331.
14. MacDonald, B.T. et al. (2004) Development 131:2543.
15. Li, J. et al. (2006) Bone 39:754.
16. Verani, R. et al. (2007) J. Neurochem. 100:242.
17. Cajánek, L. et al. (2009) Stem Cells 27:2917.
18. Menezes, M.E. et al. (2012) Int. J. Cancer 130:1477.

Bioinformatics

• Uniprot:
  • O54908()