Recombinant Human CEACAM-3/CD66d His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human CEACAM‑3/CD66d is
immobilized at 2 µg/mL
(100 µL/well), the concentration of
Recombinant Human CEACAM-7
(Catalog #
9010-CM)
that
produces 50% of the optimal binding response is 0.6-3.6 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived human CEACAM-3/CD66d protein Lys35-Gly155, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Lys35 |
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 |
14 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 |
19-25 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 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-3/CD66d His-tag 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). Mature human CEACAM‑3 is approximately 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). CEACAM‑3 appears
to be primate specific, with no 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 ann adaptation of the innate immune system to handle specific host pathogens (9). The granulocyte-specific CEACAM epitope is present on
at least four CEA family members, CEACAM‑1
-3, -6 and -8, which upon engagement on the neutrophil surface triggers a
transient activation signal that requires extracellular calcium and regulates
the adhesive activity of the beta2 integrin, CD11/CD18 (10, 11). CEACAM‑3 is critical for opsonin‑independent
phagocytosis and bacterial clearance (3). 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 (3, 9).
- 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(6):1314.
- Gold P and Freedman SO, (1965) J Exp Med 122:467.
- Obrink, B. (1997) Curr Opin Cell Biol 9:616.
- Horst, AK. and Wagener, C. (2004) Handb Exp Pharmacol 283.
- Kuespert K et al. (2006) Curr Opin Cell Biol. 18(5):565.
- Pils S. et al. (2008) Int. J. of Med. Micro. 298, 7–8:553.
- Nagel G. et al. (1993) Eur J Biochem 214:27.
- Skubitz KM et al. (1996) J Leukoc Biol 60:106.
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