>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
31.4 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.
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 Human CMG-2 Protein, CF
anthrax toxin receptor 2
ANTXR2
Capillary morphogenesis gene 2 protein
capillary morphogenesis protein 2
cI-35
CMG2
CMG-2
CMG2MGC111533
CMG-2MGC45856
FLJ31074
ISH
JHF
JHS
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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