Recombinant Human RGM-B Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human RGM-B Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immoblized rhBMP-4 at 1 µg/mL (100 µL/well) can bind rhRGM-B with a linear range of 10-500 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human RGM-B protein
Gly87-Asp209 (N-terminus chain) & Pro210-Ser452 (C-terminus chain), with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Gly87 & Pro210
Protein/Peptide Type
Recombinant Proteins
Gene
RGMB
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
13.4 kDa (N-terminus chain), 27.7 kDa (C-terminus chain).
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
20 kDa and 35 kDa, reducing conditions
Publications
Read Publications using
3630-RG in the following applications:

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 opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human RGM-B Protein, CF

  • DKFZp434P228
  • Dragon
  • DRG11-responsive axonal guidance and outgrowth of neurite
  • RGM domain family, member B
  • RGMB
  • RGM-B

Background

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).

  1. Monnier, P.P. et al. (2002) Nature 419:392.
  2. Schmidtmer, J. and D. Engelkamp (2004) Gene Exp. Patterns 4:105.
  3. Samad, T.A. et al. (2004) J. Neurosci. 24:2027.
  4. Niederkofler, V. et al. (2004) J. Neurosci. 24:808.
  5. Oldekamp, J. et al. (2004) Gene Exp. Patterns 4:283.
  6. Metzger, M. et al. (2005) Dev. Dyn. 234:169.
  7. Samad, T.A. et al. (2005) J. Biol. Chem. 280:14122.

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Publications for RGM-B (3630-RG)(2)

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Bioinformatics

Gene Symbol RGMB
Uniprot