Recombinant Human CMG-2/ANTXR2 Fc Chimera Protein, CF Summary
|Human CMG-2/ANTXR2 |
Accession # P58335.5
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in 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.
When Anthrax Protective Antigen is immobilized at 1.5 μg/mL (100 μL/well), Recombinant Human CMG-2/ANTXR2 Fc Chimera (Catalog # 10360-AR) binds with an ED50 of 1-6 ng/mL.
2 μg/lane of Recombinant Human CMG-2/ANTXR2 Fc Chimera (Catalog # 10360-AR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 55-75 kDa and 110-150 kDa, respectively.
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.
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