Recombinant Mouse ROR2 mFc Chimera Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant
Mouse ROR2 mFc Chimera (Catalog # 11425-RO) binds Human ROR2 Antibody (Catalog #
AF2064) with an ED 50 of 0.600‑7.20 ng/mL. |
| Source |
Mouse myeloma cell line, NS0-derived mouse ROR2 protein Mouse ROR2 (Glu34-Gly403) Accession # NP_038874.3 | IEGRMDP | Mouse IgG2A (Glu98-Lys330) | | N-terminus | | C-terminus | |
|
| Accession # |
|
| N-terminal Sequence |
Glu34 |
| Structure / Form |
Disulfide-linked homodimer |
| 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. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
68 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 |
80-88 kDa, under reducing conditions. |
Packaging, Storage & Formulations
| Storage |
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 with Trehalose. See Certificate of Analysis for details. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse ROR2 mFc Chimera Protein, CF
Background
ROR2 (Receptor Tyrosine Kinase-like Orphan Receptor 2) is a member of the ROR family of receptor tyrosine kinases and is important for skeletal development, including bone and cartilage formation, as well as for the development of the central nervous system (1-5). Mature mouse ROR2 contains a 370 amino acid (aa) extracellular domain (ECD) and a 520 aa cytoplasmic tail containing an tyrosine kinase domain. The ROR2 ECD features an immunoglobulin domain, a cysteine-rich domain that resembles the Wnt-binding sites of Frizzled proteins, and a kringle domain. The ECD of mouse ROR2 shares 94% and 99% aa sequence identity with the ECD of human and rat ROR2, respectively. ROR2 binds the Wnt family ligand, Wnt-5a, to activate non-canonical Wnt signaling pathways (6-8). ROR2 is broadly expressed during embryonic development and can be found in cells of all three germ layers as well as in most organ tissues (9, 10). Activation of ROR2 signaling promotes cellular proliferation, differentiation, cell-polarization, and migration. ROR2 is important for osteogenic and chondrogenic differentiation of mesenchymal stem cells (11, 12). Mutations in ROR2 are associated with the skeletal disorders, brachydactyly type B and Robinow syndrome (6). ROR2 is also involved in neurite outgrowth and synapse development in the brain (4). A variety of tumors have been found to over-express ROR2. Depending upon the cellular context, ROR2 can act as a tumor suppressor or promoter (13). Expression of ROR2 within carcinomas is correlated with a poor prognosis of survival and increased rates of recurrence (14-16).
- DeChiara, T.M. et al. (2000) Nat. Genet. 24:271.
- Petrova, I.M. et al. (2014) Mol. Neurobiol. 49:303.
- Takeuchi, S. et al. (2000) Genes Cells 5:71.
- Paganoni, S. and A. Ferreira (2003) J. Neurosci. Res. 73:429.
- Endo, M. et al. (2012) J. Cell. Sci. 125:2017.
- Minami, Y. et al. (2010) Dev. Dyn. 239:1.
- Oishi, I. et al. (2003) Genes Cells 8:645.
- Wallkamm, V. et al. (2014) PLoS ONE 9:e109428.
- Al-Shawi, R. et al. (2001) Dev. Genes. Evol. 211:161.
- Matsuda, T. et al. (2001) Mech. Dev. 105:153.
- Cai, S.X. et al. (2014) J. Cell. Physiol. 229:791.
- Xin, H. et al. (2013) Int. J. Mol. Med. 31:583.
- Ford, C.E. et al. (2013) Int. J. Cancer 133:779.
- Rasmussen, N.R. et al. (2014) PLoS ONE 9:e116101.
- Mei, H. et al. (2014) Biochem. Biophys. Res. Commun. 453:703.
- Lu, B.J. et al. (2012) Mol. Med. Rep. 5:1033.
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