Recombinant Human E-cadherin protein (His Tag)
ED50
/
Species
Human
Purity
>90 %, SDS-PAGE
GeneID
999
Accession
P12830-1
验证数据展示
Technical Specifications
Purity | >90 %, SDS-PAGE |
Endotoxin Level | <1.0 EU/μg protein, LAL method |
Biological Activity |
Not tested |
Source | HEK293-derived Human E-cadherin protein Asp155-Ala709 (Accession# P12830-1) with a His tag at the C-terminus. |
Predicted Molecular Mass | 64.6 kDa |
SDS-PAGE | 65-80 kDa, reducing (R) condition |
Formulation | Lyophilized from sterile PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization. |
Reconstitution | Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water. |
Storage |
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
|
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature. |
Background
E-cadherin (epithelial cadherin), also known as CDH1 (cadherin 1) or CAM 120/80, is a classical member of the cadherin superfamily which also include N-, P-, R-, and B-cadherins. E-cadherin is expressed on the cell surface in most epithelial tissues. The extracellular region of E-cadherin establishes calcium-dependent homophilic trans binding, providing specific interaction with adjacent cells, while the cytoplasmic domain is connected to the actin cytoskeleton through the interaction with p120-, α-, β-, and γ-catenin (plakoglobin). E-cadherin is important in the maintenance of the epithelial integrity, and is involved in mechanisms regulating proliferation, differentiation, and survival of epithelial cell. E-cadherin may also play a role in tumorigenesis. It is considered to be an invasion suppressor protein and its loss is an indicator of high tumor aggressiveness. E-cadherin is sensitive to trypsin digestion in the absence of Ca2+.
References:
1.Braga V. et al. (2016) Curr Opin Cell Biol. 42:138-21. 2.Ishiyama N. et al. (2017) Cold Spring Harb Perspect Biol. 9(5):a028738. 3.Dongre A. et al. (2019) Nat Rev Mol Cell Biol. 20(2):69-84. 4.Yang, S. et al. (2013) Biomed res int. 2013:608728. 5.Harrison OJ. et al. (2010) Nat Struct Mol Biol. 17(3):348-357. 6.Biswas KH. et al. (2017) Exp Cell Res.358(1):14-19. 7.Buckley CD. et al. (2014) Science. 346(6209):1254211.