Arc 1; CADH1_HUMAN; Cadherin 1; cadherin 1 type 1 E-cadherin; Cadherin1; CAM 120/80; CD 324; CD324; CD324 antigen; cdh1; CDHE; E-Cad/CTF3; E-cadherin; ECAD; Epithelial cadherin; epithelial calcium dependant adhesion protein; LCAM; Liver cell adhesion molecule; UVO; Uvomorulin;
WB: 1:500-1:3000, IHC: 1:50-1:200, IF/ICC: 1:100-1:500, ELISA(peptide) 1:20000-1:40000
Human, Mouse, Rat
Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(83%), Xenopus(83%)
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
E-cadherin Antibody detects endogenous levels of total E-cadherin.
Please cite this product as: Affinity Biosciences Cat# AF0131, RRID:AB_2833315.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
A synthesized peptide derived from human E-cadherin, corresponding to a region within C-terminal amino acids.
Observed Mol.Wt.: (Observed)120kD.
Predicted Mol.Wt.: (Calculated)97kDa.
Cell junction. Cell membrane. Endosome. Golgi apparatus > trans-Golgi network. 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.
Non-neural epithelial tissues.
CDH1 a single-pass type I membrane protein, and calcium dependent cell adhesion proteins. It is a ligand for integrin alpha-E/beta-7, and it colocalizes with DLG7 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. Involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Defects in CDH1 are involved in dysfunction of the cell-cell adhesion system, triggering cancer invasion (gastric, breast, ovary, endometrium and thyroid) and metastasis.
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.
E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.
(Microbial infection) Serves as a receptor for Listeria monocytogenes; internalin A (InlA) binds to this protein and promotes uptake of the bacteria.
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).
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.
Cell junction>Adherens junction. Cell membrane>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.
Non-neural epithelial tissues.
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).
(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).
Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.
· Cellular Processes > Cellular community - eukaryotes > Adherens junction.(View pathway)
· Environmental Information Processing > Signal transduction > Hippo signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Apelin signaling pathway.(View pathway)
· Environmental Information Processing > Signaling molecules and interaction > Cell adhesion molecules (CAMs).(View pathway)
· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.(View pathway)
· Human Diseases > Cancers: Specific types > Thyroid cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Bladder cancer.(View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Gastric cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Endometrial cancer.(View pathway)
· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.
· Human Diseases > Cancers: Specific types > Melanoma.(View pathway)
· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.
Application: IF/ICC Species:mouse; Sample:Not available
Lenalidomide (1μM) inhibited JAM-A-transfected cell invasion (B) and EMT (C).
Application: WB Species:human; Sample:A549 cells
Figure 3. A549/DDP and A549/PTX cells showed molecular and morphological changes that were consistent with EMT. (A) microscopy at x200 magnification was used to assess cell morphology. The A549 cells (parental cells) had an epithelioid, rounded cobblestone appearance and there was limited formation of pseudopodia. A549/PTX and A549/DDP cells exhibited a spindle-shaped morphology and an increased formation of pseudopodia, indicating a loss of cell polarity. (B) E-cadherin, β-catenin, vimentin, MMP-2 and MMP-9 which are EMT-related proteins, were assessed in terms of expression levels. EMT-related transcription factors (Snail, Slug, Twist and ZEB1) were measured in A549/PTX and A549/DDP cells using western blot analysis. (C) The expression changes were confirmed at the mRNA level by qRT-PCR. Expression was standardized to the expression of GAPDH and normalized to 1.0 in the parental cells (compared with the parental A549 cells, means ± SEM, n=3, * P<0.05)
Application: WB Species:human; Sample:HepG2
Figure 6. Effect of BCL2L10 on its downstream gene expression profiles of human cancer pathway in HepG2 cells. (A) By human cancer pathway PCR array, ectopic expression of BCL2L10 up- or down-regulated several genes related to tumor proliferation, apoptosis, metastasis and angiogenesis. (B) Western blot was performed to confirm the downstream gene expression regulated by BCL2L10 in HepG2 cells. GAPDH was used as an internal control. (C) Schematic diagram of the molecular events for BCL2L10 function as a tumor suppressor through regulating cell cycle, proliferation, apoptosis metastasis and angiogenesis effectors.
Application: WB Species:human; Sample:Not available
(C) miR-93-5p overexpression suppressed and increased E-cadherin and N-cadherin expression, respectively. The opposite result was observed in response to miR-93-5p downregulation.
Application: WB Species:human; Sample:BGC-823 cell
Figure 4. Overexpression of FOXQ1 in BGC-823 cell line resulted in EMT and increased invasiveness. To determine whether FOXQ1 promotes the EMT to increase cell invasion, the expression levels of FOXQ1, E-cadherin and vimentin were detected via western blotting and qRT-PCR. The results revealed that FOXQ1 could increase EMT, which decreased E-cadherin expression and increased vimentin expression (* P
Application: WB Species:human; Sample:Not available
Figure 2. Co-culture with TAMs induces EMT in GC cells. (A) The EMT markers in MKN45 and MKN74 cells were analyzed using western blotting after being co-cultured with THP-1 cells. (B and C) The EMT markers in MKN45 and MKN74 cells were analyzed by RT-PCR after being co-cultured with THP-1 cells; * P
Application: WB Species:human; Sample:Not available
Fig. 3. Knockdown of NS inhibited tumor migration and invasion in vitro. (A) Crystal violet staining of the shNS and control group cells that crossed the polycarbonate membrane of the Transwell chamber to detect cell migration. (B) The number of cells that crossed the Transwell migration chamber in different groups. (C) Crystal violet staining of the shNS and control group cells that crossed the Matrigel-coated polycarbonate membrane of the Transwell chamber to detect cell invasion. (D) The number of cells that crossed the Transwell invasion chamber in different groups. (E) Representative Western blotting results indicate the EMT marker expressions in the different groups. The results are presented as the means ± SD, as based on three independent experiments. Statistical significance was determined using Student's t-test. *P < 0.05. Scale: 100 mm.
Application: WB Species:human; Sample:human gastric cancer
Fig. 6. MiR-1271 inhibited gastric cancer cell migration, invasion, and epithelial-mesenchymal transition. (A) Overexpression of miR-1271 could inhibit MGC-803 cell migration and invasion, whereas its downregulation in SGC-7901 cells increased the cell migration and invasion processes. (B) Western blots showed that overexpression of miR-1271 could upregulate E-cadherin and downregulate N-cadherin and vimentin expression in MGC-803 cells, whereas its downregulation had the opposite effect in SGC- 7901 cells. Three independent experiments were conducted. *P < 0.05, **P < 0.01.
Application: WB Species:rat; Sample:Not available
Effects of null-MVs and miR-200b-MVs administration on protein expression in TGFb-Indeced EMT.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
|S844||Phosphorylation||P48729 (CSNK1A1) , P49674 (CSNK1E) , P48730 (CSNK1D)||Uniprot|