E-cadherin Antibody | Affinity Biosciences

$Figure 2—figure supplement 1.Nuclear edging of the viral genomes upon entry suppressed HSV-1 infection. (A) HEp-2 cells were infected with HSV-1 at an MOI of 5. Cells were fixed at 0.5, 1, 1.5, and 2 hpi, and the intranuclear HSV-1 genomes were stained by FISH and scanned under a confocal microscope. Representative image of the 2 hpi sample and its 3D reconstruction are shown in the left panel. The percentage of the nuclear edge-located HSV-1 genomes vs total intranuclear stains at each time point was calculated, plotted and shown in the right panel. The total number of counted dots is shown as n on the top of the right panel. (B) The cross-section of a representative image from A is shown in the left panel. The while line measures the diameter of an HSV-1 FISH spot. The yellow line measures the center of an HSV-1 FISH spot to the edge of DAPI. The red arrow points to a nuclear edge-localized HSV-1 FISH spot. Scale bars, 2 μm. In the right panel, the distance of more than 100 nuclear edge-HSV-1 spots to the margin of the DAPI-stained area was measured and plotted. (C) Sequence, position, and number of targeting sites of 5 HSV-1 sgRNAs in the viral genome (GenBank accession number GU734771). Note that the figure is not drawn to scale as the sgRNA targeting site’s sequence is relatively short compared to the entire HSV-1 genome. (D) dCas9-emerin cells expressing a ctrl sgRNA or each of the 5 HSV-1 sgRNAs were infected with HSV-1 at an MOI of 1. Virus yield at 24 hpi was titrated by plaque assay. Data is shown as mean ± SD, n = 3, and P values are calculated using the Student's t-test. ‘***’ represents ≤0.001 and ‘****’ represents p≤0.0001. (E) GFP-expressing HEp-2 cells (GFP), dCas9-expressing cells or dCas9-emerin cells were transfected with plasmids expressing HSV-1 sgRNA2 or ctrl sgRNA for 24 hr and infected with HSV-1 at an MOI of 1. Cell-associated viruses at 24 hpi were titrated by plaque assay. Data is shown as mean ± SD, n = 3. (F) dCas9 and dCas9-emerin cells were transfected with plasmids expressing HSV-1 sgRNA1 or sgRNA2 for 24 hr and infected with HSV-1 at an MOI of 1. Cell-associated viruses at 24 hpi were titrated by plaque assay. Data is shown as mean ± SD, n = 3, and P values are calculated using the Student's t-test. ‘****’ represents p≤0.0001. (G) dCas9 and dCas9-emerin cells were transfected with plasmids expressing HSV-1 sgRNA2 and infected with R8515 (a GFP expressing recombinant HSV-1) at an MOI of 1. Cells were imaged at 24 hpi. (H) dCas9-emerin cells transfected with plasmids expressing ctrl sgRNA or HSV-1 sgRNA2 for 24 hr were infected with HSV-1 (2 hr on ice) at different MOIs. The mRNA level of ICP27 at the indicated time points was quantified by qPCR. Data is shown as mean ± SD, n = 3. (I) dCas9-emerin cells were transfected with plasmids expressing HSV-1 sgRNA2 or ctrl sgRNA for 24 hr and infected (2 hr on ice) with HSV-1 at an MOI of 1. Cells were collected at the indicated times and separated into cytosol (C), membranous organelles (M) and nuclear compartments (N). Successful separation of the subcellular compartments was confirmed by immunoblotting with marker antibodies (I upper panel). The viral DNA content in the nuclear compartment was quantified by qPCR targeting the ICP27 region of the HSV-1 genome and normalized to total cellular viral DNA load. Data is shown as mean ± SD, n = 3, and P values are calculated using the Student's t-test. n.s. represents not significant, p>0.05, ‘*’ represents p≤0.05 and ‘**’ represents p≤0.01. Two independent experimental results are shown at the bottom panel of I. (J–K) dCas9-emerin cells with (+DOX) or without DOX (-DOX) were transfected with plasmids expressing HSV-1 sgRNA or ctrl sgRNA for 24 hr and then infected with HSV-1 at an MOI of 5. At the indicated time point post infection, cells were fixed and stained with anti-ICP8 (green) and anti-Flag (red) antibodies. Two representative images at each time point are shown in J. White arrows indicate nuclei with diffuse ICP8 (inefficient replication compartment formation), and red arrows indicate nuclei with aggregated/condensed ICP8 (replication compartment formation). (K) More than 200 nuclei in each sampling group were counted, and the HSV-1 replication center formation efficiency (nuclei of aggregated/condensed ICP8 vs total ICP8-positive nuclei) was quantified and plotted. Data is shown as mean ± SD, n = 3. (L) The fraction of viral DNA (targeting the ICP27 region; top panel) or host genomic DNA (targeting GAPDH) (bottom panel) immunoprecipitated with the indicated antibodies was quantified by qPCR and compared to their respective levels immunoprecipitated by a nonspecific antibody (ab) (IgG) and plotted. Data is shown as mean ± SD, n = 3. (M) ChIP assay examining the histone packaging level on the promoters of ICP27, ICP8 and VP16 of HSV-1 in HSV-1 sgRNA- or ctrl sgRNA-expressing dCas9-emerin cells at the indicated time points post infection (2 hr on ice) was performed using anti-H3 antibody. The results were displayed as enrichment (fold) by comparing the fraction of viral promoters immunoprecipitated by anti-H3 to the fraction of GAPDH immunoprecipitated in the same reaction. Data is shown as mean ± SD, n = 3, and P values are calculated using the Student's t-test. n.s. represents not significant, p>0.05 and ‘**’ represents p≤0.01. (N) HSV-1 sgRNA- or ctrl sgRNA-expressing dCas9-emerin cells were treated with DMSO or different HDACi: valproic acid (VPA), trichostatin A (TSA), romidepsin (FK 228) or sodium butyrate (NaB) and infected with HSV-1 (2 hr on ice) at an MOI of 1 (drug treatment started 5 hr before the infection). The mRNA level of ICP27 at 3 hpi was quantified by qPCR, and the ICP27 level in ctrl sgRNA-expressing cells was set as 100%. Data is shown as mean ± SD, n = 3, and P values are calculated using the Student's t-test.$

Figure 2—figure supplement 1.

Fig.

Figure 9 TJP3 regulates GEM-induced cell apoptosis and EMT process.

Fig.

FIGURE 11.

FIGURE 2.

Product:	E-cadherin Antibody
Catalog:	AF0131
Description:	Rabbit polyclonal antibody to E-cadherin
Application:	WB IHC IF/ICC
Reactivity:	Human, Mouse, Rat, Monkey
Prediction:	Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.:	120kDa; 97kD(Calculated).
Uniprot:	P12830
RRID:	AB_2833315

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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. By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific.

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MSDS

Data Sheet

COA

Protocols

WB Handbook

IHC Protocol

IF/ICC Protocol

Product Info

Source:

Rabbit

Application:

WB 1:500-1:3000, 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,Rat,Monkey

Prediction:

Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(83%), Xenopus(83%)

Clonality:

Polyclonal

Specificity:

E-cadherin Antibody detects endogenous levels of total E-cadherin.

RRID:

AB_2833315
Cite Format: Affinity Biosciences Cat# AF0131, RRID:AB_2833315.

Conjugate:

Unconjugated.

Purification:

The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).

Storage:

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.

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:

Uniprot:

P12830(CADH1_HUMAN) >>Visit HPA database.

Gene(ID):

CDH1(999)

Expression:

P12830 CADH1_HUMAN:

Non-neural epithelial tissues.

Description:

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.

Sequence:

P12830 CADH1_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species

Results

Score

Pig

100

Horse

100

Bovine

100

Sheep

100

Dog

100

Zebrafish

100

Rabbit

100

Xenopus

Chicken

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P12830 As Substrate

P12830

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

Research Backgrounds

P12830_CADH1_HUMAN

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.

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). Genomic and Transcriptomic Characterization of Natural Killer T Cell Lymphoma. CANCER CELL, 2020 (PubMed: 32183952) [IF=50.3]

Application: IF/ICC Species: human Sample: NK-92 cells

Figure 6. Biological Function of MGA and BRDT. (D) Immunofluorescence images of E-cadherin (green), fibronectin (red), or vimentin (red) in NK-92 cells transfected with MGA shRNAs or scramble. Cells were counterstained with DAPI (blue). (G) Immunofluorescence images of E-cadherin (green), fibronectin (red), or vimentin (red) in NK-92 cells transfected with pCMV6-BRDT (upper panel) or vector control (lower panel). Cells were counterstained with DAPI (blue).

2). CircGPR137B/miR-4739/FTO feedback loop suppresses tumorigenesis and metastasis of hepatocellular carcinoma. Molecular Cancer, 2022 (PubMed: 35858900) [IF=37.3]

Application: WB Species: Human Sample: HepG2 and Hep3B cells

Fig. 6 FTO is regulated by circGPR137B/miR-4739 axis in HCC. A Schematic representation of the binding sites between miR-4739 and FTO 3’UTR. B Comparison of the luciferase activity of WT or Mut FTO 3’UTR after treatment with miR-4739 mimics in HepG2 and Hep3B cells. C, D RT-qPCR and western blot analysis of the expression of FTO, p21, p27, cleaved caspase-3/− 9, N-cadherin, E-cadherin and vimentin after the transfection with circGPR137B lentiviruses and (or) miR-4739 mimics in HepG2 and Hep3B cells. E, F, G MTT, colony formation and transwell analysis of the cell proliferation, colony number and cell invasion after the transfection with FTO plasmids and (or) miR-4739 mimics in HepG2 and Hep3B cells. Data are the means ± SEM of three experiments. *P < 0.05, **P < 0.01, ***P < 0.001

3). METTL13 Mediates the Translation of Snail in Head and Neck Squamous Cell Carcinoma. International Journal of Oral Science, 2020 (PubMed: 34381012) [IF=14.9]

4). Engineering supramolecular dynamics of self-assembly and turnover of oncogenic microRNAs to drive their synergistic destruction in tumor models. Biomaterials, 2024 (PubMed: 38733658) [IF=14.0]

Application: WB Species: Human Sample: MCF-7 cells

Fig. 6. Biological activity of “Crab” aRNases in tumor cells. (A, B) Kinetics of miR-21 downregulation in MCF-7 cells by Crab-p-21, Crab-α-21 and Crab-β-21 aRNases and ON-21 oligonucleotide (A), and miR-17 downregulation in MCF-7 cells by Crab-α-17 aRNase and ON-17 oligonucleotide (B). Stem-loop PCR data of miR-21 and miR-17 levels are shown. The inhibitory effect of specific “Crab” aRNases was compared to the control non-targeted Crab-α-Scr conjugate. The expression of miRNAs was normalized to U6. Data represent the mean ± s.e. of three independent experiments. *, ** and *** statistically significant differences from control Crab-α-Scr conjugate with p≤0.05, p≤0.01 and p≤0.001. (C-E) Western-blot analysis of PDCD4 (C), E2F1 (D) and E-cadherin (E) protein level 72 h after transfection of MCF-7 cells by Crab-α-21, Crab-p-21 (C) and Crab-α-17 (D, E). Protein levels were normalized to the level of GAPDH. Data represent the mean ± s.e. of three independent experiments. *, ** and *** statistically significant differences with p≤0.05, p≤0.01 and p≤0.001. (F-H) Real-time analysis of the growth rate of MCF-7 cells after transfection with Crab-α-21 (F), Crab-β-21, Crab-p-21 (G) and Crab-α-17 (H) aRNases. (I) Real-time analysis of the growth rate of A-549 cells after transfection with Crab-α-21 and Crab-β-21. Control − tumor cells without treatment. LF – tumor cells treated with Lipofectamine™ 2000 only. Cell transfection was performed using Lipofectamine™ 2000 with aRNase concentration of 1 μM.

5). Gut Akkermansia muciniphila ameliorates metabolic dysfunction-associated fatty liver disease by regulating the metabolism of L-aspartate via gut-liver axis. Gut Microbes, 2021 (PubMed: 34030573) [IF=12.2]

Application: IHC Species: Mice Sample: ileum

Figure 2. A. muciniphila increased markers related to lipid metabolism in liver and gut of HFC mice. HFC induced obese MAFLD (11 weeks of feeding) were administered with saline as the control or A. muciniphila (6 weeks of treatment) to assess liver and ileum parameters: a-c for parameters in the liver and d-f for parameters in the ileum. e-g, representative images of the ileum (Scale bar, for 100 µm). (a) Hepatic mitochondrial copy number determination. (b) Gene expression related to lipid uptake and oxidation in the liver of mice. (c) Protein levels of metabolic regulators mitochondrial complexes, and the LKB1-AMPK axis in the liver of mice. The protein levels were quantified and normalized to the loading control actin (d) Gene expression of lipid uptake and oxidation in the ileum of mice. The gene level or protein level in the HFC group was set as 1, and the relative fold increases were determined by comparison with the HFC control group. (e) Immunohistochemistry analysis of PGC-1α in the ileum of mice. The brown dot indicates the examined protein. Representative images were captured. Scale bar, 100 µm. (f) TG level quantification (indicated by oil red O staining) and oxidative stress-induced cell apoptosis determination (indicated by CHOP examination) in the ileum. Representative images were captured. Scale bar, 100 µm. (g) Immunohistochemistry analysis of E-cadherin and H

6). Stearoyl-CoA desaturase-1 promotes colorectal cancer metastasis in response to glucose by suppressing PTEN. JOURNAL OF EXPERIMENTAL & CLINICAL CANCER RESEARCH, 2018 (PubMed: 29530061) [IF=11.3]

Application: WB Species: human Sample: CRC

Fig. 1| SCD1 is upregulated in human CRC tissues and associated with CRC prognosis. a SCD1 mRNA level in colorectal cancer tissues (CRC) and matched adjacent non-tumor tissues (Control) detected by Real Time-PCR. b Representative Western blot and quantification data of SCD1 and EMT markers (E-cadherin and vimentin) in colorectal cancer tissue and matched adjacent non-tumor tissue.

7). Psychologic Stress Drives Progression of Malignant Tumors via DRD2/HIF1α Signaling. CANCER RESEARCH, 2021 (PubMed: 34321238) [IF=11.2]

Application: IF/ICC Species: mouse Sample: tumor cells

Fig. 2. |DRD2 overexpression promotes the metastasis, invasion, tube formation, and cloning formation of tumor cells.K and L, Effect of DRD2 on the expression of E-cadherin and vimentin detected by IF. Each experiment was performed in triplicate. Results are shown as means ± SD, *, P < 0.05; **, P < 0.01.

Application: IHC Species: mouse Sample: tumor cells

Fig. 6. |TFP inhibits EMT of melanoma cells.D–F, IHC analysis of E-cadherin, vimentin, HIF1α, VEGFA, and Twist1 in melanoma tumor tissues of mice under stress stimulation. Representative images and staining scores are shown. Scale bar, 100 μm.

Application: WB Species: mouse Sample: dopamine-treated melanoma cells

Fig. 6. |TFP inhibits EMT of melanoma cells.C, Effect of TFP on the EMT markers (E-cadherin and vimentin) in dopamine-treated melanoma cells.

8). Water-extracted Lonicera japonica polysaccharide attenuates allergic rhinitis by regulating NLRP3-IL-17 signaling axis. Carbohydrate Polymers, 2022 (PubMed: 36184153) [IF=11.2]

9). YY1 complex promotes Quaking expression via super-enhancer binding during EMT of hepatocellular carcinoma. CANCER RESEARCH, 2019 (PubMed: 30760518) [IF=11.2]

Application: WB Species: human Sample: PLC-PRF-5 cells

Fig. 3 | YY1 and p65 promote EMT, migration, and invasion by targeting QKI. (a) Expression of E-cadherin and Vimentin transfected with YY1, p65, and QKI or co-transfected with QKI siRNA. (b) Morphological changes in PLC-PRF-5 cells transfected with YY1, p65, and QKI or co-transfected with QKI siRNA observed with SEM. (c) Representative immunofluorescence images of E-cadherin and Vimentin of PLC-PRF-5 cells treated in the same manner as in the wound-healing assay.

Application: IHC Species: mouse Sample: tumor tissues

Fig. 5| QKI expression is required for the YY1 complex to promote the metastasis and malignancy of HCC. (a) Comparison of PLC-PRF-5 and Hep3B tumor growth in mice were measured starting 6 days after implantation. All of the groups were euthanized on day 24. (b) Metastatic lung nodules were counted in each group. (c) QKI, p65, YY1, E-cadherin, and Vimentin expression levels in the tumor tissues of p65, YY1, p65+YY1, QKI and p65+YY1+siQKI groups analyzed through IHC staining.

Application: IF/ICC Species: human Sample: PLC-PRF-5 cells

Fig. 3| YY1 and p65 promote EMT, migration, and invasion by targeting QKI. (a) Expression of E-cadherin and Vimentin transfected with YY1, p65, and QKI or co-transfected with QKI siRNA. (b) Morphological changes in PLC-PRF-5 cells transfected with YY1, p65, and QKI or co-transfected with QKI siRNA observed with SEM. (c) Representative immunofluorescence images of E-cadherin and Vimentin of PLC-PRF-5 cells treated in the same manner as in the wound-healing assay.

10). Twist1 Regulates Vimentin through Cul2 Circular RNA to Promote EMT in Hepatocellular Carcinoma. CANCER RESEARCH, 2018 (PubMed: 29844124) [IF=11.2]

Application: IF/ICC Species: human Sample: PLC cells

Figure 3. |Twist1 up-regulates Vimentin expression through increased circ-10720,which adsorbs miRNA.(F) Representative immunofluorescence images of Ecadherin and Vimentin in PLC cells transfected with Twist1 alone or co-transfected with circ-10720 siRNA.

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E-cadherin Antibody - #AF0131