Recombinant Human CEACAM-6/CD66c Fc Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human CEACAM-8/CD66b Protein (Catalog #
9639-CM) is immobilized at 0.5 µg/mL (100 µL/well), Biotinylated Recombinant Human CEACAM‑6/CD66c Fc Chimera Avi-tag (Catalog # AVI10928) binds with an ED 50 of 0.20-2.00 µg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human CEACAM-6/CD66c protein Human CEACAM‑6/CD66c (Lys35-Gly320) Accession # NP_002474.4 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Lys35 |
Structure / Form |
Disulfide-linked homodimer Biotinylated via Avi-tag |
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 |
60 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 |
85-100 kDa, under reducing conditions. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after opening.
- 3 months, -20 to -70 °C under sterile conditions after opening.
|
Buffer |
Supplied as a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CEACAM-6/CD66c Fc Avi-tag Protein, CF
Background
Carcinoembryonic antigen-related cell adhesion molecule 6
(CEACAM-6), previously called nonspecific cross-reacting antigen (NCA) or CD66c,
is a member of the
CEACAM subfamily of glycoproteins in the immunoglobulin (Ig) superfamily primarily found in mammals. CEACAMs are
transmembrane proteins used by several bacterial pathogens to bind and invade
host cells (1-3). Mature, human CEACAM-6 is a GPI-linked
membrane protein that contains an extracellular domain (ECD) with one
N-terminal V-type Ig-like domain and two C2-type Ig-like domains (1, 3). The
GPI membrane anchor is attached at the C-terminus following cleavage of the
propeptide (4). The mature ECD of human CEACAM-6 shares 46% amino acid sequence
identity to rat CEACAM-6 and is absent in mouse. CEACAM-6 is an intercellular
adhesion molecule and forms both homotypic and heterotypic bonds with CEACAM-1,
-5 and -8 through interaction of the V-type Ig-like domains (5, 6). CEACAM-6 is
expressed by granulocytes and their precursors and granulocyte activation
enhances surface expression by mobilizing CEACAM-6 from storage in azurophilic
granules (7). CEACAM-6 is also expressed in epithelia of various organs and is
upregulated in pancreatic and colon adenocarcinomas and hyperplastic polyps (7,
8). CEACAM-6 often shows aberrant expression in acute lymphocytic leukemias, and
over-expression confers resistance to adhesion-related apoptosis (anoikis) in tumor
cells (9‑11). CEACAM-6 expression is elevated in many solid tumors including breast, pancreatic,
colonic and non-small-cell lung carcinoma, and is a biomarker
or potential therapeutic for other carcinomas (12, 13). CEACAM-6 has been identified as the glycoprotein receptor for influenza
virus and plays a role in virus entry (14). Our Avi-tag Biotinylated CEACAM-6 features
biotinylation at a single site contained within the Avi-tag, a unique 15 amino
acid peptide. Protein orientation will
be uniform when bound to streptavidin-coated surface due to the precise control
of biotinylation and the rest of the protein is unchanged so there is no
interference in the protein's bioactivity.
- Tchoupa, A. et al. (2014) J Cell Commun Signal 12:27.
- Hauck, C.R. et al. (2006) Eur J Cell Biol. 85:235.
- Kuespert, K. et al. (2006) Curr Opin Cell Biol 18:565.
- Tawaragi, Y. et al. (1988) Biochem. Biophys. Res. Comm. 150:89.
- Bonsor, D.A. et al. (2015) PNAS 112:13561.
- Kuroki, M. et al. (2001) J. Leukoc. Biol. 70:543.
- Ducker, T.P. and K.M. Skubitz (1992) J. Leukoc. Biol. 52:11.
- Scholzel, S. et al. (2000) Am. J. Pathol. 156:595.
- Duxbury, M.S. et al. (2004) J. Biol. Chem. 279:23176.
- Ilantzis, C. et al. (2002) Neoplasia 4:151.
- Kalina, T. et al. (2005) BMC Cancer 5:38.
- Blumenthal, R.D. et al. (2007) BMC Cancer 7:2.
- Ru, G.Q. et al. (2017) Oncotarget. 8:83673.
- Rahman, S.K. et al. (2021) Viruses 13:726.
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