Recombinant Human EpCAM/TROP1 Avi-tag His-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human EpCAM/TROP‑1 Avi-tag His-tag (Catalog # AVI9277) binds to Human EpCAM/TROP-1 Antibody (Catalog #
AF960) with a ED 50 of 0.750-7.50 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human EpCAM/TROP1 protein Human EpCAM (Gln24-Lys265) Accession # P16422.2 | Avi-tag | 6-His tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln24 |
Structure / Form |
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 |
31 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 |
35-42 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 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 EpCAM/TROP1 Avi-tag His-tag 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 that consists of a 242 amino acid (aa) extracellular domain with two EGF‑like repeats, a 23 aa transmembrane segment, and a 26 aa cytoplasmic domain (1). 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. 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). Our Avi-tag Biotinylated Recombinant Human EpCAM 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.
- 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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