Recombinant Mouse 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 Mouse CMG‑2/ANTXR2 Fc Chimera (Catalog # 10418-AR) with an ED50 of 1-5 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse CMG-2/ANTXR2 protein Mouse CMG-2/ANTXR2 (Gln32-Gly318) Accession # Q6DFX2.1 | IEGRMDP | Mouse IgG2A (Glu98-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
No results obtained. Gln32 inferred from enzymatic pyroglutamate treatment revealing Ala33. |
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 |
58 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 |
55-70 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 Mouse CMG-2/ANTXR2 Fc Chimera Protein, CF
Background
Capillary Morphogenesis Gene-2 (CMG-2), also known as ANTXR2,
is a widely expressed anthrax toxin receptor (ATR) family protein (1‑3). Mature,
full-length CMG‑2/ANTXR2 is a type I transmembrane protein containing a von
Willebrand A (vWA) domain in the extracellular domain (ECD) (1-5). In addition
to the full-length protein, 3 additional isoforms exist: Isoform 2 shows a 103 amino
acid (aa) deletion in the ECD; isoform 3 is a truncated, 289 aa soluble form;
and isoforms 4 shows a 12 aa insertion in the cytoplasmic region (6). The ECD
of mature, full-length mouse CMG‑2/ANTXR2 shares 84% and 89% aa sequence
identity with human and rat CMG‑2/ANTXR2, respectively. The vWA domain in the
ECD of CMG‑2/ANTXR2 adheres selectively to collagen type IV and laminin (1‑5). CMG-2/ANTXR2
isoform 2 is induced in HUVEC as they undergo capillary formation in collagen
matrices in vitro (3). CMG‑2/ANTXR2 is mutated in juvenile hyaline fibromatosis
and infantile systemic hyalinosis disorders, and several of these mutations
result in loss of laminin binding (7). CMG‑2/ANTXR2 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, 8, 9). Transport to low pH endosomes, which requires CMG‑2/ANTXR2
ubiquitination and interaction with the LDL receptor related protein LRP6 (10,
11), allows PA pore formation and release of toxin to the cytoplasm (11, 12).
Soluble CMG‑2/ANTXR2 VWA domain acts as a dummy receptor that can protect
cultured cells from anthrax intoxication (2). CMG‑2/ANTXR2 has been shown to interact with LRP6 and activate
Wnt/ beta -catenin pathway in gastric cancer, which leads to maintenance of
stem-like cells in GC (13).
- 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.
- Cryan, L. et al. (2011) Front Biosci. 16:1574.
- 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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