Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to inhibit Wnt induced TCF reporter activity in HEK293 human embryonic kidney cells.
Recombinant
Mouse Wnt‑3a (Catalog # 1324-WN)
induces a dose responsive increase in Wnt
reporter activity in HEK293 cells. Recombinant Mouse Dkk-2 (Catalog # 2435-DKB/CF) inhibits a constant dose of 100 ng/mL of Recombinant Mouse Wnt-3a (Catalog # 1324-WN). The ED50 for this effect is 100-600 ng/mL. |
Source | Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse Dkk-2 protein Ser26-Ile259, with Leu35Pro substitution and a C-terminal 10-His tag |
Accession # | |
N-terminal Sequence | Ser26 |
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. |
Dilutions |
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Theoretical MW | 27 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. |
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SDS-PAGE | 29-35 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
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. |
Dickkopf related protein 2 (Dkk-2) is a member of the Dickkopf family of secreted Wnt modulators (1-3). Dkk proteins contain a signal peptide and two conserved cysteine-rich domains that are separated by a linker region. The second cysteine-rich domain mediates Dkk-2 binding activities, and its interaction with LRP beta propellers has been mapped (2-4, 7). The 226 aa, ~35 kDa mature mouse Dkk-2 shares 99%, 96%, 96%, 96% and 94% aa identity with rat, human, dog, horse and cow Dkk-2, respectively, and can activate the canonical Wnt signaling pathway in Xenopus embryos (5). Dkk proteins modify Wnt engagement of a receptor complex composed of a Frizzled protein and a low-density lipoprotein receptor-related protein, either LRP5 or LRP6 (3). When LRP6 is over-expressed, direct high-affinity binding of Dkk-2 to LRP can enhance canonical Wnt signaling (6-8). However, when Dkk-2 and LRP6 form a ternary complex with Kremen2, Wnt signaling is inhibited due to internalization of Dkk-2/LRP6/Krm2 complexes (9, 10). Thus, depending on the cellular context, Dkk-2 can either activate or inhibit canonical Wnt signaling (3). In contrast, binding of Dkk-1 or Dkk-4 to LRP is consistently antagonistic (3). Dkk proteins are expressed in mesenchymal tissues and control epithelial transformations. Dkk-2 expression has been studied most in bone and eye, although it is expressed as early as periimplantation in mice (11). Mouse Dkk-1 or Dkk-2 deficiencies have opposite effects on bone homeostasis, despite down-regulating Wnt antagonism in both cases (12, 13). Dkk-2 expression is induced by Wnts in bone, and is thought to enhance bone density by promoting terminal differentiation of osteoblasts and mineral deposition (12). In contrast, Dkk-1 negatively regulates late osteoblast proliferation, which limits bone density (13). Dkk-2-deficient mice are blind, exhibiting faulty differentiation of corneal epithelium and ectopic blood vessels in the periocular mesenchyme (14, 15).
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