Recombinant Human EpCAM/TROP1 Fc Chimera Avi-tag Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Human EpCAM/TROP1 Affinity Purified Polyclonal Ab (Catalog # AF960) is immobilized at 0.25 μg/mL (100 μg/well), Biotinylated Recombinant Human EpCAM/TROP-1 Fc Chimera Avi-tag (Catalog # AVI960) binds with an ED50 of 1‑6 ng/mL.
2 μg/lane of Biotinylated Recombinant Human EpCAM/TROP-1 Fc Chimera Avi-tag (Catalog # AVI960) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 55-75 kDa and 110-150 kDa, respectively.
Epithelial Cellular Adhesion Molecule (EpCAM), also known as KS1/4, gp40, GA733-2, 17-1A, and TROP‑1, is a transmembrane glycoprotein originally identified as a tumor-associated antigen due to its high expression level in rapidly growing epithelial tumors (1). EpCAM is one of several cell adhesion molecules (CAMs) that does not share the structural patterns found in the four major CAM families. Human EpCAM is composed of an extracellular domain (ECD) with two epidermal-growth-factor-like (EGF‑like) repeats, a single transmembrane domain, and a highly charged, short cytoplasmic domain. Within the mature ECD, human EpCAM shares 81% and 82% amino acid sequence identity with mouse and rat EpCAM respectively. During embryonic development, EpCAM is detected in fetal lung, kidney, liver, pancreas, skin, and germ cells (2). In adults, human EpCAM is detected in basolateral cell membranes of all simple, pseudo-stratified, and transitional epithelia, but is not detected in normal squamous stratified epithelia, mesenchymal tissue, muscular tissue, neuro-endocrine tissue, or lymphoid tissue (2). EpCAM expression has been found to increase in actively proliferating epithelia tissues and in human malignant neoplasias arising from squamousal epithelia (2, 3). It has been found that EpCAM is present on normal hepatic stem cells and is increased on cells with advanced cirrhosis due to the cells' proliferation through autocrine activation of Wnt signaling (4). Additionally, EpCAM may be beneficial in the early diagnosis of hepatocellular carcinoma (HCC) since HCC typically originates from a cirrhotic background (4). EpCAM has been shown function as a homophilic Ca2+ independent adhesion molecule (3). Homophilic adhesion via EpCAM requires the interaction of both EGFlike repeats, with the first EGFlike 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 (5). During homophilic adhesion the cytoplasmic tail of EpCAM interacts with the actin cytoskeleton via a direct association alpha actinin (6).
- Kloudova, K. et al. (2016) Oncotarget. 7:46120.
- Huang, L. et al. (2018) Int. J. Mol. Med. 42:1771.
- Munz, M. et al. (2009). J. Cancer Res. 69:5627.
- Khosla, R. et al. (2017). Stem Cells Trans. Med. 6:807.
- Balzar, M. et al. (2001) Mol. Cell. Biol. 21:2570.
- Balzar, M. et al. (1998) Mol. Cell. Biol. 18:4388.
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