| Reactivity | HuSpecies Glossary |
| Applications | Inhibition Activity |
| Format | Carrier-Free |
| Details of Functionality | Measured by its ability to inhibit the activity of Recombinant Human BMP‑1/PCP (Catalog # 1927-ZN) on the cleavage of a fluorogenic peptide substrate Mca-YVADAPK(Dnp)-OH (Catalog # ES007). Recombinant human MFRP at 30 µg/mL will reduce rhBMP-1 activity by 30‑60% when measured with 1 µg of BMP-1 and 10 µM ES007 in 100 µL of 10 mM HEPES, 0.01% Brij-35, pH 7.5 at room temperature. |
| Source | Mouse myeloma cell line, NS0-derived human MFRP protein Ser101-Pro579, with an N-Terminal 10-His tag |
| Accession # | |
| N-terminal Sequence | His |
| Protein/Peptide Type | Recombinant Proteins |
| Gene | MFRP |
| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 52.7 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 | 90-105 kDa, reducing conditions |
| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions | Reconstitute at 250 μg/mL in sterile PBS. |
MFRP (membrane-type frizzled-related protein) is a 65 kDa, type II transmembrane protein related to both Tolloid proteases and frizzled-domain containing Wnt pathway proteins (1 - 4). Human MFRP is 579 amino acids (aa) in length (3, 5, 6). It contains a 69 aa cytoplasmic region, a 21 aa transmembrane segment, and a 489 aa extracellular domain (ECD). The ECD is characterized by the presence of two LDLR class A repeats, two CUB domains, and a C-terminal cysteine-rich/frizzled domain. The mRNA for MFRP is highly unusual in that it is dicistronic; that is, it contains two independent ORFs, one for MFRP and one for a functionally-related protein termed CTRP5/C1qTNF5 (4, 7). CTRP5 is a secreted, 25 kDa short-chain collagen that contains a C1q-type domain (6, 8). In prokaryotes, polycistronic transcripts exist that contain functionally-interactive molecules. This would also appear to be the case for MFRP and CTRP5. CTRP5 is suggested to bind to membrane MFRP via the C1q and CUB domains, respectively. This is positioned to generate a receptor-coreceptor complex that binds select Wnts such as Wnt-1 and/or Wnt-10b (4, 6, 7). MFRP has multiple documented mutations. In human, these are associated with hyperopia (severe farsightedness). The mutations result in premature truncations (3, 9). MFRP is expressed in retinal pigment epithelium, ciliary epithelium, and keratinocytes (4, 7, 10, 11). Human MFRP ECD is 70% aa identical to mouse ECD.
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