Recombinant Human RGM-B Protein, CF
Recombinant Human RGM-B Protein, CF Summary
Gly87-Asp209 (N-terminus chain) & Pro210-Ser452 (C-terminus chain), with a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
RGM-B, also known as DRAGON, is a 40 kDa member of the repulsive guidance molecule (RGM) family of GPI-linked neuronal and muscle membrane proteins (1, 2). It is synthesized as a preproprotein that consists of a 45 amino acid (aa) signal sequence, a 368 aa mature region, and a 24 aa C-terminal prosegment (3). RGM-B contains an RGD motif, two potential N-linked glycosylation sites, and an abbreviated von Willebrand factor domain. There is a potential proteolytic cleavage site within the VWF domain (4). Alternative splicing may generate isoforms of RGM-B with N-terminal extensions or truncation following the VWF domain. Mature human RGM-B shares 52% and 36% aa sequence identity with the comparable regions of RGM-A and RGM-C, respectively. It shares 98%, 92%, 92%, and 78% aa sequence identity with macaque, mouse, bovine, and chicken RGM-B, respectively. RGM-B is expressed in the developing and adult nervous system, particularly in the dorsal root ganglia and mantle layer of the spinal cord (3 - 5). In mouse, it shows a complementary, non-overlapping distribution with RGM-A (2 - 5). RGM-B is also expressed in fetal and adult enteric ganglia and in postnatal intestinal epithelium (6). RGM-B expression has been detected in neuronal cell bodies and proximal axonal segments (4) but is also present on the cell surface, where it interacts homophilically and mediates neuronal adhesion (3). RGM-B additionally functions as a BMP coreceptor. It directly binds BMP-2 and -4 but not other TGF-beta family proteins (7). RGM-B associates with BMP type I (ALK-2, -3, -6) and type II (Activin RIIA, Activin RIIB) receptors and enhances BMP signaling (7).
- Monnier, P.P. et al. (2002) Nature 419:392.
- Schmidtmer, J. and D. Engelkamp (2004) Gene Exp. Patterns 4:105.
- Samad, T.A. et al. (2004) J. Neurosci. 24:2027.
- Niederkofler, V. et al. (2004) J. Neurosci. 24:808.
- Oldekamp, J. et al. (2004) Gene Exp. Patterns 4:283.
- Metzger, M. et al. (2005) Dev. Dyn. 234:169.
- Samad, T.A. et al. (2005) J. Biol. Chem. 280:14122.
Citations for Recombinant Human RGM-B Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 2
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RGMb is a novel binding partner for PD-L2 and its engagement with PD-L2 promotes respiratory tolerance.
Authors: Xiao, Yanping, Yu, Sanhong, Zhu, Baogong, Bedoret, Denis, Bu, Xia, Francisco, Loise M, Hua, Ping, Duke-Cohan, Jonathan, Umetsu, Dale T, Sharpe, Arlene H, DeKruyff, Rosemari, Freeman, Gordon J
J Exp Med, 2014;211(5):943-59.
Sample Types: Antibody
Applications: ELISA (Capture)
Repulsive guidance molecule (RGM) family proteins exhibit differential binding kinetics for bone morphogenetic proteins (BMPs).
Authors: Wu, Qifang, Sun, Chia Chi, Lin, Herbert, Babitt, Jodie L
PLoS ONE, 2012;7(9):e46307.
Sample Types: Recombinant Protein
Applications: Surface Plasmon Resonance
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