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mouse anti-Human E-cadherin monoclonal antibody (SHE78-7) 8192


Antibody summary

  • Mouse monoclonal to Human E-cadherin
  • Suitable for: WB,ELISA,IHC,IF,FACS
  • Isotype: IgG2a
  • 100 µg
SKU: 8192parent Category: Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in







1 mg/mL





available sizes

100 µg

Available product – mouse anti-Human E-cadherin monoclonal antibody (SHE78-7) 8192

Tested applications
Recommended dilutions
ELISA: 2ug/ml

Western Blotting

Flow : 2ug/ml, reducing and non-reducing conditions

Flow Cytometry: 1ug/ml.

Immunohistochemistry: 2ug/ml, paraffin- embedded and frozen tissue sections.

Immunofluorescence: 1ug/ml.Cell-Cell Contact Inhibition Assays: 1ug/ml.
Human placenta E-Cadherin
Size and concentration
100µg and
Storage Instructions
Lyophilized antibody is stable at 4°C for 2 years. Store the reconstituted solution in aliquots at -20°C for one year or at 4°C for 6 months after addition of 0.1% sodium azide by th
Storage buffer
PBS, pH 7.4, lyophilized.
immunogen affinty purifcation
Compatible secondaries
goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody 5486
goat anti-mouse IgG, H&L chain specific, biotin conjugated, Conjugate polyclonal antibody 2685
goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody 7854
goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1706
goat anti-mouse IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1716
goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1721
Isotype control
Mouse monocolonal IgG2a - Isotype Control
target relevance
Protein names
Cadherin-1 (CAM 120/80) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]
Gene names
FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000269|PubMed:11976333, ECO:0000269|PubMed:16417575}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. {ECO:0000269|PubMed:16417575}.; FUNCTION: (Microbial infection) Serves as a receptor for Listeria monocytogenes; internalin A (InlA) binds to this protein and promotes uptake of the bacteria. {ECO:0000269|PubMed:10406800, ECO:0000269|PubMed:17540170, ECO:0000269|PubMed:8601315}.
Subellular location
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:28169360}. Cell membrane {ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:28301459}; Single-pass type I membrane protein. Endosome. Golgi apparatus, trans-Golgi network. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane.
TISSUE SPECIFICITY: Non-neural epithelial tissues.
SUBUNIT: Homodimer; disulfide-linked (PubMed:11856755). Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions (PubMed:16126725, PubMed:7982500). Interacts with the TRPV4 and CTNNB1 complex (By similarity). Interacts with CTNND1 (PubMed:15240885). The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex (By similarity). Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (By similarity). Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs) (PubMed:11226248, PubMed:16126725). Interacts with AJAP1 and DLGAP5 (PubMed:14699157, PubMed:14595118). Interacts with TBC1D2 (PubMed:20116244). Interacts with LIMA1 (PubMed:18093941). Interacts with CAV1. Interacts with PIP5K1C (PubMed:17261850). Interacts with RAB8B (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization (PubMed:20432435). Interacts with KLRG1 (PubMed:19604491). Forms a ternary complex composed of ADAM10, CADH1 and EPHA4; within the complex, CADH1 is cleaved by ADAM10 which disrupts adherens junctions (By similarity). Interacts with SPEF1 (PubMed:31473225). Interacts with CTNNB1 and PKP2 (PubMed:11790773). {ECO:0000250, ECO:0000250|UniProtKB:P09803, ECO:0000250|UniProtKB:Q9R0T4, ECO:0000269|PubMed:11226248, ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:11856755, ECO:0000269|PubMed:12526809, ECO:0000269|PubMed:14595118, ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:16126725, ECO:0000269|PubMed:17261850, ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:19604491, ECO:0000269|PubMed:20116244, ECO:0000269|PubMed:20432435, ECO:0000269|PubMed:31473225, ECO:0000269|PubMed:7982500}.; SUBUNIT: (Microbial infection) Interacts with L.monocytogenes InlA (PubMed:12526809, PubMed:17540170, PubMed:17715295). The formation of the complex between InlA and cadherin-1 is calcium-dependent (PubMed:12526809). {ECO:0000269|PubMed:12526809, ECO:0000269|PubMed:17540170, ECO:0000269|PubMed:17715295}.
Post-translational modification
PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (PubMed:11076937, PubMed:11953314, PubMed:10597309). 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). {ECO:0000250|UniProtKB:P09803, ECO:0000269|PubMed:10597309, ECO:0000269|PubMed:11076937, ECO:0000269|PubMed:11953314}.; PTM: 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). {ECO:0000269|PubMed:18491227, ECO:0000269|PubMed:19403558}.; PTM: Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-754. {ECO:0000269|PubMed:21283129, ECO:0000269|PubMed:22252131, ECO:0000269|PubMed:22770219}.; PTM: 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. {ECO:0000250|UniProtKB:P09803}.; PTM: (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). {ECO:0000269|PubMed:23532847}.
Target Relevance information above includes information from UniProt accession : P12830
The UniProt Consortium


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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.



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