Recombinant Mouse Epithelial Cell Adhesion Molecule (EPCAM) Protein (Myc)

Beta LifeScience SKU/CAT #: BLC-07570P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Epithelial Cell Adhesion Molecule (EPCAM) Protein (Myc)

Beta LifeScience SKU/CAT #: BLC-07570P
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Product Overview

Description Recombinant Mouse Epithelial Cell Adhesion Molecule (EPCAM) Protein (Myc) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q99JW5
Target Symbol EPCAM
Synonyms (Ep-CAM)(Epithelial glycoprotein 314)(EGP314)(mEGP314)(Protein 289A)(Tumor-associated calcium signal transducer 1)(CD antigen CD326)
Species Mus musculus (Mouse)
Expression System Mammalian cell
Tag C-Myc
Expression Range 24-266aa
Protein Length Partial
Mol. Weight 29.5 kDa
Research Area Cell-Cell Adhesion
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E.
Subcellular Location Lateral cell membrane; Single-pass type I membrane protein. Cell junction, tight junction.
Protein Families EPCAM family
Database References

Gene Functions References

  1. The expression of Epcam mRNA, which is a functional marker of potential hepatic stem-like cells, was controlled by LEF1, which was regulated by CLOCK. PMID: 29958886
  2. EpEX/EpCAM are sufficient to reprogram fibroblasts into iPSCs with only Oct4 or Klf4. PMID: 28157205
  3. extracellular vesicles tend to localize in the intestinal tract associated with epithelial cell adhesion molecule PMID: 27721471
  4. Data show that EpCAM-expressing proliferating ductal cells (PDC) could be a cellular origin of hepatocellular carcinoma (HCC), suggesting the existence of stem/progenitor-derived hepatocarcinogenesis. PMID: 28951464
  5. activation of hepatic H19RNA promoted cholestatic liver fibrosis through the ZEB1/EpCAM signaling pathway PMID: 28407375
  6. These results identify EpCAM as a substrate of matriptase and link HAI-2, matriptase, EpCAM, and claudin-7 in a functionally important pathway that causes disease when it is dysregulated. PMID: 28094766
  7. EpCAM appears to differentially regulate Langerhans cell mobility/migration in the setting of limited inflammation as compared with the intense inflammation triggered by contact sensitizers PMID: 27106675
  8. Knock-down EpCAM cell model of congenital tufting enteropathy was developed. In vivo inducible mouse model was developed resulting in mutant EpCAM protein. PMID: 25482158
  9. in addition to converting to cholangiocyte-like cells, Sox9(+)EpCAM(-) cells provide luminal space near expanded ductular structures to prevent deterioration of the injuries and potentially supply new hepatocytes to repair damaged tissues PMID: 24482234
  10. EpCAM is a highly conserved protein present in fishes, amphibians, reptiles, birds, marsupials, and placental mammals, and is subject to shedding, gamma-secretase-dependent regulated intramembrane proteolysis, and proteasome-mediated degradation. PMID: 24009667
  11. Suggest pivotal role of EpCAM in intestinal epithelial structure and integrity, with mutations resulting in congenital tufting enteropathy. PMID: 24337010
  12. mTrop1/Epcam knockout mice develop congenital tufting enteropathy through dysregulation of intestinal E-cadherin/beta-catenin. PMID: 23209569
  13. EpCAM contributes to formation of intestinal barrier by recruiting claudins to cell-cell junctions. PMID: 22819673
  14. These results conclusively link EpCAM expression to Langerhan cell (LC) motility/migration and LC migration to immune regulation. PMID: 22411813
  15. Results show that SSCs are the most concentrated in CD9(+)EPCAM(low/-) population and also suggest that EPCAM plays an important role in progenitor cell amplification in the mouse spermatogenic system. PMID: 21858196
  16. EpCAM could contribute substantially to the pathogenesis of lung cancer. PMID: 21535318
  17. EpCAM was required for differentiation or survival of parietal trophoblast giant cells, normal development of the placental labyrinth and establishment of a competent maternal-fetal circulation. PMID: 20046825
  18. analysis of EpCAM expression in normal, non-pathological tissues PMID: 17981779
  19. The spatiotemporal expression pattern of EpCAM changes during nephrogenesis PMID: 18025791
  20. These data suggest that EpCAM is involved in signal transduction triggering several intracellular signalling pathways using tumor cell lines in colorectal and lung cancer. PMID: 19002182
  21. EpCAM(+) cells isolated from injured liver proliferate to form colonies in vitro, and the clonally expanded cells differentiate into hepatocytes and cholangiocytes, suggesting that the oval cell fraction contains potential HSCs. PMID: 19429791
  22. expression of EpCAM and DLK1 suggests the developmental pathways of mouse liver progenitors PMID: 19527784


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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