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