Recombinant Human CMG-2/ANTXR2 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Anthrax Protective Antigen
is
immobilized at 1.5 μg/mL
(100 μL/well), it binds Recombinant Human CMG‑2/ANTXR2 Fc Chimera (Catalog # 10360-AR) with an ED50 of 1-6 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human CMG-2/ANTXR2 protein Human CMG-2/ANTXR2 (Gln34-Asn317) Accession # P58335.5 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln34 inferred from enzymatic pyroglutamate treatment revealing Glu35 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
57 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 |
55-75 kDa, under 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 |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CMG-2/ANTXR2 Fc Chimera Protein, CF
Background
Capillary Morphogenesis Gene-2 (CMG-2) is a widely expressed anthrax toxin receptor (ATR) family protein (1 - 3). CMG-2 is a 55 kDa type I transmembrane (TM) protein that contains a 33 amino acid (aa) signal sequence, a 284 aa extracellular domain (ECD), a 24 aa TM segment, and a 147 aa cytoplasmic domain. There are three additional isoforms. Isoforms 4 shows a 12 aa insertion in the cytoplasmic region; isoform 2 shows a 103 aa deletion in the ECD; and isoform 3 is a truncated, 20 kDa, 289 aa soluble form. The main functional domain of CMG-2 is an extracellular integrin-like von Willebrand factor type A (VWA) domain with a metal ion dependent adhesion site (MIDAS). This domain adheres selectively to collagen type IV and laminin (1 - 5). CMG-2 isoform 2 is induced in HUVEC as they undergo capillary formation in collagen matrices
in vitro (3). CMG-2 is mutated in juvenile hyaline fibromatosis and infantile systemic hyalinosis disorders, and several of these mutations result in loss of laminin binding (6). CMG-2 and the related protein ATR/TEM8 serve as receptors for the protective antigen (PA) of
Bacillus Anthracis (1, 2). After binding the VWA domain, PA undergoes furin-type cleavage, forms a heptameric receptor/PA pre-pore and binds LF or EF toxin subunits (5, 7, 8). Transport to low pH endosomes, which requires CMG-2 ubiquitination and interaction with the LDL receptor related protein LRP6 (9, 10), allows PA pore formation and release of toxin to the cytoplasm (10, 11). Soluble CMG-2 VWA domain acts as a dummy receptor that can protect cultured cells from anthrax intoxication (2). Within the extracellular region, human CMG-2 shares 84%, 81%,89% and 93% amino acid sequence homology with mouse, rat, bovine, and canine CMG-2, respectively. CMG-2 VWA domain also shares 60% aa identity with ATR/TEM8.
- Scobie, H.M. and J.A.T. Young (2005) Curr. Opin. Microbiol. 8:106.
- Scobie, H.M. et al. (2003) Proc. Natl. Acad. Sci. USA 100:5170.
- Bell, S.E. et al. (2001) J. Cell Sci. 114:2755.
- Lacy, D.B. et al. (2004) Proc. Natl. Acad. Sci. USA 101:6367.
- Santelli, E. et al. (2004) Nature 430:905.
- Dowling, O. et al. (2003) Am. J. Hum. Genet. 73:957.
- Wigelsworth, D.J. et al. (2004) J. Biol. Chem. 279:23349.
- Go, M.Y. et al. (2006) J. Mol. Biol. 360:145.
- Abrami, L. et al. (2006) J. Cell Biol. 172:309.
- Wei, W. et al. (2006) Cell 124:1141.
- Lacy, D.B. et al. (2004) Proc. Natl. Acad. Sci. USA 101:13147.
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