DKK2 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | Q9QYZ8 |
Other Accession | NP_064661.2 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 28432 Da |
Gene ID | 56811 |
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Application & Usage | Western blotting (0.5-4 µg/ml). However, the optimal conditions should be determined individually. The antibody recognizes 30-35 kDa Dkk2 in samples from human, mouse and rat origins. A ~25 kDa band can also be detected, presumably to be the cleavage fragment of Dkk2. |
Other Names | DKK-2, DKK 2, dkk2, dkk-2, dkk 2, dickkopf homolog-2, dickkopf homolog2, dickkopf homolog 2 |
Target/Specificity | DKK2 |
Antibody Form | Liquid |
Appearance | Colorless liquid |
Formulation | 100 µg (0.5 mg/ml) purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 30% glycerol, 0.5% BSA and 0.01% thimerosal. |
Handling | The antibody solution should be gently mixed before use. |
Reconstitution & Storage | -20 °C |
Background Descriptions | |
Precautions | DKK2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | Dkk2 {ECO:0000312|MGI:MGI:1890663} |
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Function | Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. |
Cellular Location | Secreted. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Xenopus Dickkopf (Dkk)-1 was initially discovered as a Wnt antagonist that plays an important role in head formation. By far, four members of Dkk have been identified in mammals. Each Dkk molecule contains two conserved cysteine-rich domains. Recent studies showed that the second Cys-rich domains of Dkk1 and Dkk2 inhibited Wnt-3a-activated signaling, whereas the first Cys-rich domains had no effects. In addition, the second Cys-rich domain of Dkk-2, but not that of Dkk-1, was able to activate the canonical pathway in the presence of LRP6, and this LRP-dependent signaling does not require Dvl.
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