Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Details of Functionality | Measured by its ability to bind rhBMP-4 in a functional ELISA. Immobilized rmDAN at 2 µg/mL (100 µL/well) can bind rhBMP-4 with a linear range of 0.1‑10 ng/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse DAN protein Ala17-Asp178, with a C-terminal Ile and 10-His tag |
Accession # | |
N-terminal Sequence | Ala17 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Nbl1 |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 18.9 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 | 27-30 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 BSA as a carrier protein. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
DAN (differential screening-selected gene aberrative in neuroblastoma) was initially identified as a gene whose expression is downregulated in src-transformed rat fibroblasts. DAN has now been shown to be a prototypical member of the DAN family of secreted glycoproteins that are putative BMP antagonists. DAN family members share a cysteine-rich domain that is structurally related to the cysteine-knot motif found in TGF-beta superfamily ligands. There are at least five mouse DAN family members, including DAN, Gremlin/DRM, Cer1 (Cerberus-related), Dante and PRDC (protein related to DAN and cerberus). Additional DAN family members include Xenopus Cerberus, chick Caronte, and C. elegans CeCan 1. Murine DAN binds BMP-2 in immunoprecipitation experiments and acts as a BMP antagonist in Xenopus animal cap explants. The DAN family of proteins are thought to act as antagonists by binding BMP ligands and preventing their interactions with signaling receptor complexes. Recombinant mouse DAN preparations from R&D Systems have been shown to bind BMP-4 in a functional ELISA. It is likely the various DAN family members and other TGF-beta BMP antagonists including Noggin, Chordin, Follistatin, and TSG can selectively antagonize the activities of different subsets of TGF-beta superfamily ligands. These antagonists represent one of the many elaborate regulatory mechanisms that have evolved to control the bioactivities of the TGF-beta superfamily ligands.
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