Recombinant Mouse RGM-C/Hemojuvelin Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. Immobilized rhBMP-4 at 1 µg/mL (100 µL/well) can bind rmRGM-C with a linear range of 0.016‑1 µg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse RGM-C/Hemojuvelin protein Gln33-Asp393 (Ile379Val) (mature) & Pro166-Asp393 (Ile379Val) (C-terminus peptide), both with a C-terminal 6-His tag & Gln33-Asp165 (N-terminus peptide) |
Accession # |
|
N-terminal Sequence |
Gln33 (mature & N-terminus peptide) & Pro166 (C-terminus peptide)
|
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Hfe2 |
Purity |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
40 kDa (mature), 14 kDa (N-terminus peptide), 26 kDa (C-terminus peptide). 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 |
57 kDa, 20 kDa and 38 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 under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
Reconstitute at 100 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 RGM-C/Hemojuvelin Protein, CF
Background
RGM-C, also known as hemojuvelin, is a member of the repulsive guidance molecule (RGM) family of GPI-linked neuronal and muscle membrane glycoproteins (1). RGM-C is expressed in striated muscle and periportal hepatocytes (2-4). The protein undergoes partial cleavage intracellularly, resulting in a disulfide-linked dimer of the 14 kDa N-terminal and 33 kDa C-terminal portions (3, 5, 6). The N-terminal fragment contains an RGD motif, while the C-terminal fragment carries the GPI attachment site (3, 6). An alternatively spliced isoform lacks the N-terminal fragment. Full length RGM-C can also be released from the cell and circulates in the blood (5, 7). RGM-C is disrupted in type 2A juvenile hemochromatosis, a hereditary iron homeostasis disorder characterized by excessive iron accumulation (4). Loss of RGM-C function results in decreased expression of the iron regulatory hormone hepicidin and increased iron deposition in liver, pancreas, and heart (4, 8). Membrane associated RGM-C up-regulates hepicidin while soluble RGM-C down-regulates hepicidin expression (7). This appears to be an iron-responsive regulatory system, as high blood iron levels reduce the amount of soluble RGM-C produced (7). RGM-C, similar to RGM-A, associates with neogenin (6). Disease-related point mutations can prevent internal RGM-C cleavage or its ability to interact with neogenin (5, 6). Experimental inflammatory conditions result in decreased RGM-C expression and increased hepicidin expression, although the two effects occur independently (4, 9). RGM-C also functions as a BMP co-receptor and enhances BMP-2 and BMP-4 signaling (10). In this context, RGM-C enhances the BMP-2 up-regulation of hepatic hepicidin (10). Mature mouse RGM-C shares 89% and 97% amino acid (aa) sequence identity with human and rat RGM-C, respectively. It shares 51% and 44% aa sequence identity with mouse RGM-A and RGM-B, respectively.
- Schmidtmer, J. and D. Engelkamp (2004) Gene Exp. Patterns 4:105.
- Oldekamp, J. et al. (2004) Gene Exp. Patterns 4:283.
- Niederkofler, V. et al. (2004) J. Neurosci. 24:808.
- Niederkofler, V. et al. (2005) J. Clin. Invest. 115:2180.
- Kuninger, D. et al. (2006) J. Cell Sci. 119:3273.
- Zhang, A.S., et al. (2005) J. Biol. Chem. 280:33885.
- Lin, L. et al. (2005) Blood 106:2884.
- Huang, F.W. et al. (2005) J. Clin. Invest. 115:2187.
- Krijt, J. et al. (2004) Blood 104:4308.
- Babitt, J.L. et al. (2006) Nat. Genet. 38:531.
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