Detection of EpCAM/TROP‑1 in 4T1 Mouse Cell Line by Flow Cytometry. 4T1 mouse breast cancer cell line was stained with Rat Anti-Mouse EpCAM/TROP‑1 Monoclonal Antibody (Catalog # MAB8998, filled histogram) or isotype control antibody (Catalog # MAB006, open histogram), followed by Phycoerythrin-conjugated Anti-Rat IgG Secondary Antibody (Catalog # F0105B).
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & 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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Epithelial Cellular Adhesion
Molecule (EpCAM), also known as EGP314 (Epithelial glycoprotein 314), TACSTD1
(tumor-associated calcium signal transducer 1) and CD326 is a 292 amino acid
(aa), 40 kDa transmembrane glycoprotein composed of a 243 aa extracellular
domain with two epidermal-growth-factor-like (EGF-like) repeats within the
cysteine-rich N-terminal region, a 23 aa transmembrane domain, and a 26 aa
cytoplasmic domain. Human and mouse EpCAM share 82% aa sequence identity.
During embryonic development, EpCAM is detected in fetal lung, kidney, liver,
pancreas, skin, and germ cells. EpCAM has been shown function as a homophilic
Ca2+ independent adhesion molecule (1). Homophilic adhesion via
EpCAM requires the interaction of both EGF-like repeats, with the first
EGF-like repeat mediating reciprocal interaction between EpCAM molecules on
opposing cells, while the second repeat is involved in lateral interaction of
EpCAM. Lateral interaction of EpCAM lead to the formation of dimers and
tetramers (2). During homophilic adhesion the cytoplasmic tail of EpCAM
interacts with the actin cytoskeleton via a direct association alpha -actinin (3).
Litvinow, S.V. et al. (1994) J. Cell Biol. 125:437.
Balzar, M. et al. (2001) Mol. Cell. Biol. 21:2570.
Balzar, M. et al. (1998) Mol. Cell. Biol. 18:4388.
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