Recombinant Mouse ROBO2 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When recombinant human Slit3 or Recombinant Mouse Slit3 (Catalog # 3629-SL) is coated at 0.25 μg/mL, Recombinant Mouse ROBO2 Fc Chimera binds with an apparent K d <2 nM. |
Source |
Mouse myeloma cell line, NS0-derived mouse ROBO2 protein
Mouse ROBO2 (Ser22-Ala863) Accession # NP_780758 |
IEGRMDP |
Mouse IgG2A (Glu98-Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Ser22 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Robo2 |
Purity |
>90%, by SDS-PAGE with silver staining |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
120 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 |
100-155 kDa, 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. |
Purity |
>90%, by SDS-PAGE with silver staining |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse ROBO2 Fc Chimera Protein, CF
Background
ROBO2 is a type I transmembrane glycoprotein that is part of the ROBO family of guidance molecules. Mouse ROBO2 is synthesized as a 1470 amino acid (aa) precursor and has a predicted molecular weight of approximately 160 kDa. Its extracellular domain contains five C2-type Ig-like domains and three fibronectin type III domains, and shares 98% aa sequence identity with the human and rat orthologs. Alternative splicing of mouse
Robo2 creates an 820 aa isoform that contains a 14 aa substitution for aa 807-946 and then terminates after this substitution. A 1527 aa isoform, termed ROBO2a, has also been identified (1). ROBO2a contains a longer signal peptide and is cleaved at a different position resulting in four extra aa in its N-terminus. It also contains an additional 42 aa that is inserted after aa 1049 (1). Mouse ROBO2 is ubiquitously expressed in embryonic and adult tissues, with the highest expression levels in the adult being seen in the brain, liver, and kidney (1-9). Mouse ROBO2a is also ubiquitously expressed during development; however, it is only expressed in the brain in adults (1). ROBO2 acts as a receptor for the Slit family of chemorepulsion molecules and facilitates Slit-mediated growth cone repulsion (5). It is highly expressed on axons that do not cross the ventral midline of the nervous system and on axons that have already crossed (9-11). As a result, Slit/ROBO2 signaling regulates guidance and midline crossing of growing axons (3, 5, 11-16). Slit/ROBO2 signaling has also been shown to mediate repulsion of neuronal cell bodies away from the floor plate during development (12). Furthermore, interactions between Slit and ROBO2 have also been shown to be critical for development of the foregut, lungs, kidney, and heart (6-8, 17, 18).
- Yue, Y. et al. (2006) Genomics 88:772.
- Piper, M. et al. (2000) Mech. Dev. 94:213.
- Erskine, L. et al. (2000) J. Neurosci. 20:4975.
- Vargesson, N. et al. (2001) Mech. Dev. 106:175.
- Guthrie, S. (2001) Curr. Biol. 11:R300.
- Greenberg, J.M. et al. (2004) Dev. Dyn. 230:350.
- Medioni, C. et al. (2010) Dev. Dyn. 239:3303.
- Domyan, E.T. et al. (2013) Dev. Cell 24:52.
- Sundaresan, V. et al. (2004) J. Comp. Neurol. 468:467.
- Rajagopalan, S. et al. (2000) Neuron 28:767.
- Mambetisaeva, E.T. et al. (2005) Dev. Dyn. 233:41.
- Kim, M. et al. (2011) Dev. Biol. 358:181.
- Fouquet, C. et al. (2007) J. Neurosci. 27:3037.
- López-Bendito, G. et al. (2007) J. Neurosci. 27:3395.
- Goldberg, D. et al. (2013) Dev. Dyn. 242:9.
- Wang, S. et al. (2013) J. Neurosci. 33:12242.
- Grieshammer, U. et al. (2004) Dev. Cell 6:709.
- Mommersteeg, M.T. et al. (2013) Circ. Res. 112:465.
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