Recombinant Human CEACAM-3/CD66d Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human CEACAM‑3/CD66d Fc Chimera is immobilized at 1 µg/mL (100
µL/well), Recombinant Human CEACAM-7 (Catalog # 9010-CM) binds with an ED50 of 0.05-0.4 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human CEACAM-3/CD66d protein Human CEACAM-3 (Lys35-Gly155) Accession # P40198 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Lys35 |
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 |
39.7 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 |
48-54 kDa, reducing conditions
|
Packaging, Storage & Formulations
Storage |
- 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. |
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-3/CD66d Fc Chimera Protein, CF
Background
Carcinoembryonic
Antigen-related Cell Adhesion Molecule 3 (CEACAM-3), or CD66d, 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). Human CEACAM-3 is ~35 kDa, consisting of an extracellular
domain (ECD) containing one IgV-like domain, a single transmembrane domain and a
cytoplasmic tail. The cytoplasmic tail of CEACAM-3 contains an immunoreceptor
tyrosine-based activation motif (ITAM), which recruits kinases to propagate
pro-inflammatory signaling cascades (3). Interestingly, CEACAM-3 appears to be
primate specific, with on non-primate orthologs currently identified (4). Originally discovered as a biomarker for
colorectal cancer (5), CEACAMs have now been associated with numerous
intracellular signaling processes including cell adhesion, cell growth,
recognition and differentiation, angiogenesis, and apoptosis (6-8). Unlike
other CEA family members, CEACAM-3 has not been shown to form cell–cell adhesion
interactions with other CEACAM family members (9). CEACAM-3 has been found to be
specifically expressed on human neutrophils and other granulocytes and appears
to be a specific adaptation of the innate immune system to cope with a small
set of host-specific pathogen (9). CEACAM-3
was identified as critical for opsonin-independent phagocytosis and bacterial
clearance (10). CEACAM-3 binds to the colony opacity-associated (Opa) outer
membrane proteins of bacteria, such as
Neisseria
gonorrhoeae, and triggers uptake of the pathogen and
subsequent elimination (9, 10).
- Beauchemin, N. et al. (1999) Exp. Cell Res. 252:243.
- Zebhauser R, et al. (2005) Genomics 86:566.
- Schmitter, T. et al. (2004) J. Exp. Med. 199:35.
- Pavlopoulou A. and Scorilas A. (2014) Genome Biol Evol. 6:1314.
- Gold P and Freedman, S.O. (1965) J Exp Med. 122:467.
- Obrink, B. (1997) Curr Opin Cell Biol. 9:616.
- Horst, AK. and Wagener, C. (2004) Handb Exp Pharmacol. 165:283.
- Kuespert K et al. (2006) Curr Opin Cell Biol. 18:565.
- Pils S. et al. (2008) Int J Med Microbiol. 298:553.
- Schmitter, T. et al. (2004) J. Exp. Med. 199:35.
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