Recombinant Human E Cadherin protein
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(3 Publications)
Recombinant Human E Cadherin protein is a Human Fragment protein, in the 155 to 707 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
CD324, CDHE, UVO, CDH1, Cadherin-1, CAM 120/80, Epithelial cadherin, Uvomorulin, E-cadherin
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human E Cadherin protein (AB235682)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab235682.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
E-Cadherin participates in establishing and maintaining adherens junctions which are vital for tissue structure. E-Cadherin operates as a core component of the cadherin-catenin complex which links the protein to the actin cytoskeleton. Through this linkage E-Cadherin plays an important role in signaling pathways that influence cellular growth and differentiation. The protein's ability to mediate intercellular connections also regulates cellular motility and supports basic aspects of cell behavior in epithelial tissues.
Pathways
E-Cadherin influences both the Wnt signaling pathway and the epithelial-to-mesenchymal transition (EMT). Within the Wnt signaling pathway E-Cadherin partners with β-catenin a significant player in transcription regulation and cell signaling. Disruption in E-Cadherin's adhesive functionality can lead to increased β-catenin availability affecting downstream transcriptional control. In the EMT process E-Cadherin loss characterizes an important step in which cells gain migratory and invasive properties typically seen during metastasis in cancer progression.
Specifications
Form
Liquid
General info
Function
CDH1 encodes a protein that is a calcium-dependent cell adhesion molecule, playing a role in cell-cell adhesion, mobility, and proliferation in epithelial cells. It acts as a potent invasive suppressor and serves as a ligand for integrin alpha-E/beta-7. The protein contributes to the sorting of heterogeneous cell types due to its homophilic interactions. E-Cad/CTF2, a product of CDH1, promotes the non-amyloidogenic degradation of Abeta precursors and strongly inhibits the production of APP C99 and C83. Additionally, in the context of microbial infection, it functions as a receptor for Listeria monocytogenes, with internalin A binding to it to promote bacterial uptake. This supplementary information is collated from multiple sources and compiled automatically.
Post-translational modifications
During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (PubMed:10597309, PubMed:11076937, PubMed:11953314). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (PubMed:10597309). The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway (PubMed:10597309). Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system (PubMed:11076937). The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions (PubMed:11953314). During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity).. N-glycosylation at Asn-637 is essential for expression, folding and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location (PubMed:19403558).. Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-754.. O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Thr-285 and Thr-509 are O-mannosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3.. (Microbial infection) Cleaved by S.pyogenes SpeB protease; leading to its degradation (PubMed:23532847). Degradation by SpeB promotes bacterial translocation across the host epithelial barrier (PubMed:23532847).
Subcellular localisation
Endosome
Target data
Publications (3)
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Oncology letters 29:245 PubMed40182609
2025
Applications
Unspecified application
Species
Unspecified reactive species
PeerJ 11:e15458 PubMed37273536
2023
Applications
Unspecified application
Species
Unspecified reactive species
Oxidative medicine and cellular longevity 2022:4509019 PubMed39282154
2022
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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