Measured by its ability to inhibit proliferation of HeLa human cervical epithelial carcinoma cells. Hsieh, S.Y. et al. (2004) Oncogene 23:9183. The ED50 for this effect is 3-12 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human Dkk-3 protein Ala22-Ile350, with a C-terminal 10-His tag
>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
37.5 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
64-74 kDa, reducing conditions
Publications
Read Publications using 1118-DK in the following applications:
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 250 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Dkk-3 Protein, CF
dickkopf (Xenopus laevis) homolog 3
dickkopf 3
dickkopf homolog 3 (Xenopus laevis)
Dickkopf-3
dickkopf-related protein 3
Dkk3
Dkk-3
hDkk-3
regulated in glioma
REIC
REICdkk-3
RIG
RIG-like 5-6
RIG-like 7-1
Background
Dkk-3, also known as REIC (Reduced Expansion in Immortalized Cells), is one of four numbered members of the Dickkopf family of Wnt antagonists (1). Dkk-3 is a secreted monomer expressed in many normal human tissues, most strongly in heart, brain and spinal cord (1, 2), and during early embryonic development in the mouse (3). N-glycosylation at up to four sites preceding or between two conserved cysteine-rich motifs results in expression of a 45 - 65 kDa glycoprotein (1, 4). The cysteine-rich motifs contain 10 cysteines each, with prokineticin and colipase families containing sequences similar to those of the second motif (1, 5). Human Dkk-3 shows 82%, 88%, 85% and 53% amino acid (aa) identity with mouse, bovine, canine and chick Dkk-3, respectively, and 37 - 45% aa identity with other human Dkk family members. Several lines of evidence implicate Dkk-3 as a negative growth regulator. Dkk-3 is downregulated in many tumors as compared to normal cells, sometimes by loss of heterozygosity (4, 6). Downregulation by CpG hypermethylation in acute lymphoblastic leukemia is correlated with faster progression and shorter survival (7). Release of cultured cells from serum starvation results in downregulation of Dkk-3 in late G1 phase of the cell cycle (6). Overexpression of Dkk-3 results in tumor cell-line-specific growth inhibition, induction of apoptosis, and decreased tumorigenicity in nude mice (2, 4, 6). The prototype Dickkopf member, Dkk-1, antagonizes Wnt family signaling by binding to Wnt receptors LRP5 and LRP6 (low-density lipoprotein receptor-related proteins) and promoting their internalization (1, 9, 10). Results are less straightforward for Dkk-3, where some studies show binding to LRP5/6 while others do not. These effects appear to be dependent on the cells and conditions used (1, 6 - 10).
Krupnik, V.E. et al. (1999) Gene 238:301.
Tsuji, T. et al. (2000) Biochem. Biophys. Res. Comm. 268:20.
Kemp, C. et al. (2005) Dev. Dyn. 233:1064.
Hsieh, S.-Y. et al. (2004) Oncogene 23:9183.
Bullock, C.M. et al. (2004) Mol. Pharmacol. 65:582.
Tsuji, T. et al. (2001) Biochem. Biophys. Res. Comm. 289:257.
Roman-Gomez, J. et al. (2004) Br. J. Cancer 91:707.
Hoang, B.H. et al. (2004) Cancer Res. 64:2734.
Caricasole, A. et al. (2003) J. Biol. Chem. 278:37024.
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