Recombinant Mouse CEACAM-5/CD66e Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Mouse CEACAM-5/CD66e Fc Chimera (Catalog
# 10403-CM) is immobilized at 0.5 µg/mL (100 µL/well), Recombinant Mouse
Galectin-4
(Catalog #
2128-GA) binds with an ED50 of 0.1-0.8 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse CEACAM-5/CD66e protein Mouse CEACAM-5/CD66e (Gln35-Glu947) Accession # Q3UKK2.1 | IEGRMDP | Mouse IgG2a (Glu98-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
|
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>90%, 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 |
130 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 |
125-145 kDa and 185-195 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 |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 400 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 CEACAM-5/CD66e Fc Chimera Protein, CF
Background
CEACAM-5, also
known as CEA, CD66e and Psg30, belongs to the large family of CEACAM and
pregnancy specific glycoproteins. CEACAM family members are highly glycosylated
with varying arrangements of IgV-like and IgC-like regions in their
extracellular domains (ECD) and can be expressed as transmembrane,
glycophosphatidyl inositol (GPI) linked or soluble proteins (1-3). CEACAM-5 consists of an N-terminal Ig-like
V-set domain followed by six Ig-like C2-set domains and a GPI anchor (2, 4, 5).
While the mature ECD of mouse CEACAM-5 shares 26% amino acid identity with human
CEACAM-5, it remains unclear if these molecules are direct orthologs (6). CEACAM-5,
expressed primarily by epithelial cells, functions as a calcium-independent
adhesion molecule through homophilic and heterophilic interactions with CEACAM-1
(1, 7). CEACAM-5 is restricted to the apical face of intestinal epithelial cells
in the adult but is more diffuse during embryonic development and in tumors (8).
This is consistent with a role in the development and maintenance of epithelial
architecture. CEACAM-5 is up-regulated in a wide variety of human tumors,
promoting tumor cell migration, invasion, adhesion, and metastasis, and has
been used as a cancer marker (8, 9). It also contributes to tumor formation by
maintaining cellular proliferation in the presence of differentiation stimuli,
and by blocking apoptosis following loss of ECM anchorage (anoikis) (10, 11).
The GPI anchoring of CEACAM-5 can be released by GPI-PLD, resulting in a soluble
molecule that also promotes tumor metastasis (12). Cell surface expression of
CEACAM-5 on tumor cells prevents the adhesion of CEACAM-1 expressing
NK cells and provides protection from NK-mediated lysis (8). CEACAM-5 was shown to bind
galectin-4 and by surface plasmon resonance and coimmunoprecipitated with
galectin-4 in human colon adenocarcinoma LS174T cell lysates (13). CEACAM-5
also binds a subset of Neisseria opacity proteins (Opa) and E. coli
adhesion proteins (14, 15).
These interactions trigger clustering of the lipid raft-localized CEACAM-5 to
sites of pathogen contact (15,
16).
- Zebhauser, R. et al. (2005) Genomics 86:566.
- Hammarstrom, S. (1999) Semin. Cancer Biol. 9:67.
- Chan, et al. (2007) Curr Oncol. 14:70.
- Schrewe H. et al. (1990) Mol. Cell. Biol. 10:2738.
- Hefta, S.A. et al. (1988) Proc. Natl. Acad. Sci. 85:4648.
- Hance KW et al. Mutat Res. (2005) 576:132.
- Stern, N. et al. (2005) J. Immunol. 174:6692.
- Beauchemin N. et al. (2013) Cancer Metastasis Rev. 32:3.
- Blumenthal, R.D. et al. (2005) Cancer Res. 65:8809.
- Screaton, R.A. et al. (1997) J. Cell Biol. 137:939.
- Ordonez, C. et al. (2000) Cancer Res. 60:3419.
- Yamamoto, Y. et al. (2005) Biochem. Biophys. Res. Commun. 333:223.
- Ideo H. et al. (2005) J Biol Chem. 280:4730.
- Martin, J.N. et al. (2016) Biochemistry. 55:4286
- Berger, C.N. et al. (2004) Mol. Microbiol. 52:963.
- Tchoupa, A.K. et al. (2014) Cell Commun Signal. 12:27.
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