EpCAM/TROP1 hFc Chimera, Human

EpCAM/TROP1 hFc Chimera, Human

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.
Z05246
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Product Introduction
Species Human
Protein Construction
EpCAM/TROP1 (Gln24-Lys265)
Accession # P16422		 hFc
N-term C-term
Purity > 95% as determined by Bis­Tris PAGE 
> 95% as determined by HPLC
Endotoxin Level Less than 1EU per μg by the LAL method.
Biological Activity Measured by its binding ability in a functional ELISA. Immobilized EpCAM/TROP1 hFc Chimera, Human at 2μg/ml (100μl/well) on the plate can bind Biotinylated Anti­EpCAM Antibody, hFc Tag. Test result was comparable to standard batch.
Expression System HEK293
Theoretical Molecular Weight 54.2 kDa
Apparent Molecular Weight Due to glycosylation, the protein migrates to 60-70 kDa based on Bis-Tris PAGE result.
Formulation Lyophilized from 0.22μm filtered solution in PBS (pH 7.4).
Reconstitution Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
Storage & Stability Upon receiving, the product remains stable up to 6 months at -20 °C or below. Upon reconstitution, the product should be stable for 3 months at -80 °C. Avoid repeated freeze-thaw cycles.

Background
Target 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.
Synonyms CD326; EGP; EGP-2; EGP314; EGP40; EpCAM; ACSTD1; DIAR5; gp40; HNPCC8; MOC31; TACST-1; TACSTD1; TROP1; ESA; KSA; MIC18; MK1

For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.