Recombinant Human CEACAM-18 Fc Chimera Protein, CF

When Recombinant Human Galectin-3 (Human Cell-expressed) (Catalog # 8259-GA) is coated at 1 μg/mL, 100 μL/well, Recombinant HumanCEACAM-18 Fc Chimera (Catalog # 9869-CM) binds with an ED50 of0.5-5 μg/mL.

2 μg/lane of Recombinant Human CEACAM-18 was resolved with SDS-PAGEunder reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 93 -105 kDa and 190- 200 kDa,respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human CEACAM-18 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Galectin-3 (Catalog # 8259-GA) is immobilized at 1 μg/mL, 100 μL/well, it binds Recombinant Human CEACAM-18 Fc Chimera. The concentration of Recombinant Human CEACAM-18 Fc Chimera that produces 50% of the optimal binding response is
  0.5-5 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human CEACAM-18 protein
  

  Human CEACAM-18 (Gln31-His317) Accession # A8MTB9	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: A8MTB9
• N-terminal Sequence: No results obtained. Gln31 inferred from enzymatic pyroglutamate treatment revealing Ile32.
• 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:
  • Bioactivity
• Theoretical MW: 59 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: 93-105 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• 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 CEACAM-18 Fc Chimera Protein, CF

• Carcinoembryonic Antigen-Related Cell Adhesion Molecule 18
• CEACAM-18

Background

Carcinoembryonic Antigen-related Cell Adhesion Molecule 18 (CEACAM-18) is part of the CEA protein family consisting of CEACAMs and the pregnancy-specific glycoproteins (PSGs). Both CEACAM and PSG molecules have been identified in humans and belong to the much larger glycosylphosphatidylinositol (GPI)-linked immunoglobulin (Ig) superfamily (1, 2). Mature human CEACAM-18 has a 298 amino acid (aa) extracellular domain containing 2 IgC2-like and 1 IgV-like domains, a single transmembrane domain and a short cytoplasmic tail (2). CEACAM-18 is one of only five conserved CEACAMs among mouse, rat, and human (2), but mature human CEACAM-18 has low aa sequence identify with mouse and rat at 60% and 58%, respectively. Originally discovered as a biomarker for colorectal cancer (3), CEACAMs have now been associated with numerous intracellular signaling processes including cell adhesion, cell growth, recognition and differentiation, angiogenesis, and apoptosis (4-6). While the exact function of CEACAM-18 has been yet to be elucidated, it may bind pathogen receptors or other immunoregulatory members (6). CEACAM family members were identified as the major Galectin-3 receptor candidates on human neutrophils (7). Binding of carbohydrate ligands to CEACAMs may be important in the release of proinflammatory mediators (8, 9).

1. Beauchemin, N. et al. (1999) Exp. Cell Res. 252:243.
2. Zebhauser R. et al. (2005) Genomics 86:566.
3. Gold P and Freedman SO, 1965) J Exp Med 122:467.
4. Obrink, B. (1997) Curr Opin Cell Biol 9:616.
5. Horst, A.K. and Wagener, C. (2004) Handb Exp Pharmacol 283.
6. Kuespert K. et al. (2006) Curr Opin Cell Biol. 18(5):565.
7. Feuk-Lagerstedt E. et al. (1999) J. Immunol. 163:5592.
8. Yoon, J. et al. (2007) J. Immunol. 179:8454.
9. Schröder, A.K. et al. (2006) Hum Immunol. 67:676.

Bioinformatics

• Uniprot:
  • A8MTB9()