Recombinant Cynomolgus Monkey EpCAM/TROP1 Fc Protein, CF Summary
Additional Information |
Cynomolgus Monkey/Rhesus Macaque |
Details of Functionality |
Measured by the ability of the immobilized protein to support the adhesion of the L Cells mouse fibroblast cell line. The ED50 for this effect is 0.3-1.8 μg/mL.
|
Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey EpCAM/TROP1 protein Cynomolgus Monkey EpCAM/TROP-1 (Gln24-Lys265) Accession # NP_001035118.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln24, blocked, deduced from Lys25 upon deblocking
|
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 |
54 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 |
60-66 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 |
>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 Cynomolgus Monkey EpCAM/TROP1 Fc Protein, CF
Background
Epithelial Cellular Adhesion Molecule (EpCAM), also known as
KS1/4, gp40, GA733-2, 17-1A, and TROP-1, is a 40 kDa transmembrane glycoprotein.
Based on its similarity with human EpCAM, Cynomolgus EpCAM is predicted to
consist of a 242 amino acid (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. Cynomolgus and human EpCAM share 93% aa sequence identity (1). During
embryonic development, EpCAM is detected in fetal lung, kidney, liver,
pancreas, skin, and germ cells. In adults, human EpCAM is expressed on
basolateral cell membranes of all simple, pseudo-stratified, and transitional
epithelia but not on normal squamous stratified epithelia, mesenchymal tissue,
muscular tissue, neuro-endocrine tissue, or lymphoid tissue (2). It is
additionally expressed on undifferentiated embryonic stem cells, thymocytes,
and dendritic cells (3-5). It is up-regulated on actively proliferating
epithelial tissues, during adult liver regeneration, and on many epithelial
cell-derived carcinomas (2, 6). EpCAM functions as a homophilic cell adhesion molecule
(7). It associates into tetramers and forms complexes
in cis with Claudin-7,
CD44v6, TSPAN8, CD9, Integrin alpha 3, and Annexin A1 (8-11) that can interfere
with cell adhesion (12, 13). Proteolytic cleavage of EpCAM releases multiple
fragments from the ECD as well as a cytoplasmic fragment that can regulate gene
transcription (14-16).
- Strnad, J. et al. (1989) Cancer Res. 49:314.
- Schnell, U. et al. (2013) Biochim. Biophys. Acta 1828:1989.
- Ng, V.Y. et al. (2010) Stem Cells 28:29.
- Nelson, A.J. et al. (1996) Eur. J. Immunol. 26:401.
- Borkowski, T.A. et al. (1996) Eur. J. Immunol. 26:110.
- de Boer, C.J. et al. (1999) J. Pathol. 188:201.
- Litvinov, S.V. et al. (1994) J. Cell Biol. 125:437.
- Balzar, M. et al. (2001) Mol. Cell. Biol. 21:2570.
- Nubel, T. et al. (2009) Mol. Cancer Res. 7:285.
- Kuhn, S. et al. (2007) Mol. Cancer Res. 5:553.
- Schmidt, D.S. et al. (2004) Exp. Cell Res. 297:329.
- Litvinov, S.V. et al. (1997) J. Cell Biol. 139:1337.
- Gaiser, M.R. et al. (2012) Proc. Natl. Acad. Sci. USA 109:E889.
- Schnell, U. et al. (2013) Biosci. Rep. 33:e00030.
- Schon, M.P. et al. (1993) Int. J. Cancer 55:988.
- Maetzel, D. et al. (2009) Nat. Cell Biol. 11:162.
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