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

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When Recombinant Mouse Dkk-1 N-Terminal Fragment (Catalog #9839-DK) is immobilized at 1 μg/mL, 100 μL/well, Recombinant Mouse CKAP4/p63 (Catalog # 9734-CK) binds with an ED50 of 15-90 ng/mL.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Dkk‑1 N-Terminal Fragment is coated at 1 μg/mL, Mouse CKAP4/p63 (Catalog # 9734-CK) binds with an ED50 of 15-90 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Dkk-1 protein
Met1-Ser144, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser30 & Thr32
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
13 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
13-22 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 PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 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 N-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 N-terminal fragment [amino acids (aa) 32-144] that includes the CRD1, mouse Dkk-1 shares 98% and 85% 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), while the N-terminal CRD1 was required for binding to CKAP4 (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 (3, 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.

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