Recombinant Mouse RGM-C/Hemojuvelin Protein, CF Summary
Product Specifications
Gln33-Asp393 (Ile379Val) (mature) & Pro166-Asp393 (Ile379Val) (C-terminus peptide), both with a C-terminal 6-His tag & Gln33-Asp165 (N-terminus peptide)
Analysis
Product Datasheets
Carrier Free
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.
3634-RG
| 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.
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Reconstitution Calculator
Background: RGM-C/Hemojuvelin
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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