Product Info

Source:
Mouse
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Monkey
Clonality:
Monoclonal [AFfirm06(AFB1836)]
Specificity:
CDH1 antibody detects endogenous levels of total CDH1.
RRID:
AB_2833860
Cite Format: Affinity Biosciences Cat# BF0219, RRID:AB_2833860.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

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;

Immunogens

Immunogen:

Purified recombinant fragment of human CDH1 expressed in E. Coli.

Uniprot:
Gene(ID):
Expression:
P12830 CADH1_HUMAN:

Non-neural epithelial tissues.

Description:
This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Mutations in this gene are correlated with gastric, breast, colorectal, thyroid and ovarian cancer. Loss of function is thought to contribute to progression in cancer by increasing proliferation, invasion, and/or metastasis. The ectodomain of this protein mediates bacterial adhesion to mammalian cells and the cytoplasmic domain is required for internalization. Identified transcript variants arise from mutation at consensus splice sites. [provided by RefSeq]
Sequence:
MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD

PTMs - P12830 As Substrate

Site PTM Type Enzyme
T66 Phosphorylation
Y68 Phosphorylation
S70 Phosphorylation
T211 Phosphorylation
T217 O-Glycosylation
T330 Phosphorylation
N558 N-Glycosylation
N570 N-Glycosylation
T576 Phosphorylation
T599 Phosphorylation
N622 N-Glycosylation
N637 N-Glycosylation
Y663 Phosphorylation
K738 Ubiquitination
T748 Phosphorylation
Y753 Phosphorylation
Y754 Phosphorylation
Y755 Phosphorylation
S770 Phosphorylation
T790 Phosphorylation Q05655 (PRKCD)
S793 Phosphorylation
Y797 Phosphorylation
S838 Phosphorylation
S840 Phosphorylation
S844 Phosphorylation P48729 (CSNK1A1) , P49674 (CSNK1E) , P48730 (CSNK1D)
S846 Phosphorylation
S847 Phosphorylation P68400 (CSNK2A1)
S850 Phosphorylation P68400 (CSNK2A1)
S851 Phosphorylation
S853 Phosphorylation P68400 (CSNK2A1)
K871 Ubiquitination
Y876 Phosphorylation

Research Backgrounds

Function:

Cadherins are calcium-dependent cell adhesion proteins. 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. 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.

PTMs:

During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3. Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm. The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway. Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions. 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.

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.

Subcellular Location:

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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Non-neural epithelial tissues.

Subunit Structure:

Homodimer; disulfide-linked. 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. Interacts with the TRPV4 and CTNNB1 complex (By similarity). Interacts with CTNND1. 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). Interacts with AJAP1 and DLGAP5. Interacts with TBC1D2. Interacts with LIMA1. Interacts with CAV1. Interacts with PIP5K1C. Interacts with RAB8B (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization. Interacts with KLRG1. 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. The formation of the complex between InlA and cadherin-1 is calcium-dependent.

Family&Domains:

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.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Apelin signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Hippo signaling pathway.   (View pathway)

· Environmental Information Processing > Signaling molecules and interaction > Cell adhesion molecules (CAMs).   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.

· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Endometrial cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Thyroid cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Melanoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Bladder cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Gastric cancer.   (View pathway)

References

1). Up-regulation of miR-20a by HPV16 E6 exerts growth-promoting effects by targeting PDCD6 in cervical carcinoma cells. Biomedicine & Pharmacotherapy (PubMed: 29710555) [IF=7.5]

2). Anthelmintics nitazoxanide protects against experimental pulmonary fibrosis. British Journal of Pharmacology (PubMed: 37428102) [IF=7.3]

3). N-2-(phenylamino) benzamide derivatives as novel anti-glioblastoma agents: Synthesis and biological evaluation. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY (PubMed: 34537445) [IF=6.7]

4). Tspan5 promotes epithelial–mesenchymal transition and tumour metastasis of hepatocellular carcinoma by activating Notch signalling. Molecular Oncology (PubMed: 33955149) [IF=6.6]

Application: WB    Species: Human    Sample: HCC cells

Fig. 3 Tspan5 promotes EMT of HCC cells. (A) Tspan5 triggers the rearrangement of actin cytoskeleton. Stress fibres and actin filaments were visualized by Rhodamine-phalloidin staining (red) in HCC cells transduced with lentivirus containing Tspan5/shTspan5-encoding vector or empty/scramble RNA vector (Control/shControl). Nuclei were stained with DAPI (blue). Upregulation of Tspan5 significantly increased F-actin expression (red) and actin stress fibres throughout the Tspan5-upregulating cells compared with the control cells in which the actin bundles were predominantly localized underneath cell membranes. 400× magnification, scale bar: 10 μm. Mean ± SD, n = 3, Student's t-test; *P < 0.05, **P < 0.01. (B) Western blotting showing regulation of the expression of EMT markers, E-cadherin, N-cadherin, vimentin and Snail by Tspan5. GAPDH was used as a protein loading control. Numbers indicating relative protein ratio measured by Image J software and normalized to GAPDH. Vimentin was undetectable in MHCC97L cells. (C) Representative IF images showing regulation of the expressions of E-cadherin and vimentin by Tspan5. 630× magnifications, scale bar: 10 μm. Quantification of the protein expression was performed by Zeiss zen microscope software. Mean ± SD, n = 9, Student's t-test; **P < 0.01. (D) Representative IHC images of Tspan5, E-cadherin and vimentin expressions in xenograft sections of metastatic foci in mouse lungs. 600× magnifications, scale bar: 50 μm. Mean ± SD,

Application: IF/ICC    Species: Human    Sample: HCC cells

Fig. 3 Tspan5 promotes EMT of HCC cells. (A) Tspan5 triggers the rearrangement of actin cytoskeleton. Stress fibres and actin filaments were visualized by Rhodamine-phalloidin staining (red) in HCC cells transduced with lentivirus containing Tspan5/shTspan5-encoding vector or empty/scramble RNA vector (Control/shControl). Nuclei were stained with DAPI (blue). Upregulation of Tspan5 significantly increased F-actin expression (red) and actin stress fibres throughout the Tspan5-upregulating cells compared with the control cells in which the actin bundles were predominantly localized underneath cell membranes. 400× magnification, scale bar: 10 μm. Mean ± SD, n = 3, Student's t-test; *P < 0.05, **P < 0.01. (B) Western blotting showing regulation of the expression of EMT markers, E-cadherin, N-cadherin, vimentin and Snail by Tspan5. GAPDH was used as a protein loading control. Numbers indicating relative protein ratio measured by Image J software and normalized to GAPDH. Vimentin was undetectable in MHCC97L cells. (C) Representative IF images showing regulation of the expressions of E-cadherin and vimentin by Tspan5. 630× magnifications, scale bar: 10 μm. Quantification of the protein expression was performed by Zeiss zen microscope software. Mean ± SD, n = 9, Student's t-test; **P < 0.01. (D) Representative IHC images of Tspan5, E-cadherin and vimentin expressions in xenograft sections of metastatic foci in mouse lungs. 600× magnifications, scale bar: 50 μm. Mean ± SD,

5). Nogo-B inhibition restricts ulcerative colitis via inhibiting p68/miR-155 signaling pathway. International Immunopharmacology (PubMed: 37244119) [IF=5.6]

6). Upregulation of Translationally Controlled Tumor Protein Is Associated With Cervical Cancer Progression. Frontiers in Molecular Biosciences (PubMed: 34589516) [IF=5.0]

Application: WB    Species: Human    Sample:

FIGURE 5 Identification of key proteins involved in PI3K/AKT/mTOR pathway over-activation, apoptosis suppression, EMT, and p53 degradation in cancerous tissues of cervical cancer patients, in comparison with the paracancerous tissues. (A) WB images that are representative of all samples tested. (B) Densitometry quantification of the WB results from the experiment performed in A. The ratio of BAX:BCL2 is calculated to highlight the apoptosis activity.

7). Myelin Debris Impairs Tight Junctions and Promotes the Migration of Microvascular Endothelial Cells in the Injured Spinal Cord. CELLULAR AND MOLECULAR NEUROBIOLOGY (PubMed: 35147836) [IF=4.0]

8). Oxalate induces the ossification of RTECs by activating the JAK2/STAT3 signaling pathway and participates in the formation of kidney stones. Archives of Biochemistry and Biophysics (PubMed: 35749806) [IF=3.9]

9). LINC01060 knockdown inhibits osteosarcoma cell malignant behaviors in vitro and tumor growth and metastasis in vivo through the PI3K/Akt signaling. Cancer Biology & Therapy (PubMed: 37211864) [IF=3.6]

Application: WB    Species: Human    Sample: U2OS cells

Figure 3. Effects of LINC01060 knockdown on osteosarcoma cell invasion and migration. Note: U2OS cells were transfected with Lv-shLINC01060-1/2 and examined for cell migration using Wound healing assay (a-b), scale bar = 200 μm; cell invasion using Transwell pre-coated with Matrigel (c-d), scale bar = 100 μm; the protein levels of N-cadherin, MMP2, MMP9, Vimentin, and E-cadherin using Immunoblotting (e-f). All N = 3; * P 

10). Tumor necrosis factor-α coordinates with transforming growth factor-β1 to induce epithelial-mesenchymal transition and migration via the NF-κB/NOX4 pathway in bronchial epithelial cells. Molecular Biology Reports (PubMed: 35913579) [IF=2.8]

Load more

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.