Recombinant Human CDH1 Protein (C-6His)

Name: Recombinant Human CDH1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0963NP
Availability: InStock

BL-0963NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, Cluster of differentiation (cd) proteins, Featured cd protein molecules, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Cadherin-1/E-Cadherin/CDH1 is produced by our Mammalian expression system and the target gene encoding Asp155-Ile707 is expressed with a 6His tag at the C-terminus.
Accession	P12830
Synonym	Cadherin-1; CDH1;CAM 120/80;E-cadherin; CD324
Gene Background	E-Cadherin is a classical member of the cadherin superfamily. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein composed 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 cancers. 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. Also, E-Cadherin has a potent invasive suppressor role and it is a ligand for integrin alpha-E/beta-7.
Molecular Mass	61.2 KDa
Apmol Mass	80-90 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target 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.
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.
Database References	HGNC: 1748 OMIM: 119580 KEGG: hsa:999 STRING: 9606.ENSP00000261769 UniGene: PMID: 29805042 NEDD9, E-cadherin and gamma-catenin proteins have roles in pancreatic ductal adenocarcinoma PMID: 29924959 detection of Ezrin and E-cadherin expression in cervical smears, could be a potential prognostic marker for identifying cervical lesions with high-risk of progression to invasive cervical cancer, and may help on the selection of an appropriate therapy or avoid unnecessary treatment PMID: 29587669 CDH1 plays an essential role in epithelial cell adherence. Causative of blepharocheilodontic syndrome CDH1 mutations impair the cell adhesion function of the cadherin-catenin complex in a dominant-negative manner. PMID: 29348693 Together, these data suggest that the S18-2 protein induces epithelial to mesenchymal cell transition through the TWIST2/E-cadherin signalling and, consequently, CXCR4-mediated migration of prostate cancer cells. PMID: 29396484 In the present study, we demonstrated that miR711mediated downregulation of CD44 expression inhibited EMT of gastric cancer cells in vitro and in vivo by downregulating vimentin protein expression and upregulating Ecadherin protein expression through transfection, qRTPCR and western blotting PMID: 30226620 Soluble E-cadherin (sE-cad) (an 80-kDa soluble form), which is highly expressed in the malignant ascites of ovarian cancer patients, is a potent inducer of angiogenesis. In addition to ectodomain shedding, we provide further evidence that sE-cad is abundantly released in the form of exosomes. PMID: 29891938 In the former, p53 binds to the CDH1 (encoding E-cadherin) locus to antagonize EZH2-mediated H3K27 trimethylation (H3K27me3) to maintain high levels of acetylation of H3K27 (H3K27ac). PMID: 29371630 E-cadherin silencing relies on the formation of a complex between the paRNA and microRNA-guided Argonaute 1 that, together, recruit SUV39H1 and induce repressive chromatin modifications in the gene promoter PMID: 28555645 The results show how E-cadherin instructs the assembly of the LGN/NuMA complex at cell-cell contacts, and define a mechanism that couples cell division orientation to intercellular adhesion. PMID: 28045117 Low CDH1 expression is associated with pancreatic cancer. PMID: 29956814 the dysregulation of TET2/E-cadherin/beta-catenin regulatory loop is a critical oncogenic event in HCC progression PMID: 29331390 At the molecular level, transcription of the adherens junction protein E-cadherin is upregulated on nicotinic acid addition, leading to accumulation of E-cadherin protein at the cell-cell boundary. This can be attributed to nicotinic acid's ability to facilitate the ubiquitination and degradation of Snail1, a transcription factor that represses E-cadherin expression. PMID: 28256591 down-regulation of USP48 increases E-cadherin expression and epithelial barrier integrity through reducing TRAF2 stability PMID: 28874458 AnxA5 2D-network mediates E-cadherin mobility in the plasmalemma that triggers human trophoblasts aggregation and thereby cell fusion. PMID: 28176826 The disassociation of the beta-catenin/E-cadherin complex in the osteoblast membrane under stretch loading and the subsequent translocation of beta-catenin into the nucleus may be an intrinsic mechanical signal transduction mechanism. PMID: 29901167 The presence of E-cadherin decreases cortical contractility during mitosis through a signaling cascade leading to multipolar divisions, and its knockout promotes clustering and survival of cells with multiple centrosomes. PMID: 29133484 E-cadherin expression is not significantly linked to metastatic disease in pancreatic ductal adenocarcinoma. PMID: 29355490 High CDH1 expression is associated with the Pathogenesis of Adamantinomatous Craniopharyngiomas. PMID: 29625497 study provides evidence for genetic polymorphisms of the adherent junction component cadherin gene and the association of its haplotypes with leukoaraiosis PMID: 30017735 found that E-cadherin, N-cadherin and fibronetin are involved in CHD4-mediated epithelial-mesenchymal transition PMID: 29305962 Up-regulation of H19 in bladder cancer tissues is correlated with clinical stage or metastasis of cancer. By cell transfection to suppress H19 expression in bladder cancer cells, E-cadherin expression is up-regulated, thus weakening metastatic potency of cancer cells. PMID: 29614625 These findings suggested that PHF8 played an oncogenic role in facilitating FIP200-dependent autophagic degradation of E-cadherin, EMT and metastasis in hepatocellular carcinoma (HCC). PHF8 might be a promising target for prevention, treatment and prognostic prediction of HCC. PMID: 30180906 When ANXA5 expression increased, cell proliferation was inhibited by regulating the expression of bcl-2 and bax while cell metastasis was suppressed by regulating E-cadherin and MMP-9 expression. PMID: 30010106 Six2 is negatively correlated with good prognosis and decreases 5-FU sensitivity via suppressing E-cadherin expression in HCC cells. PMID: 29772441 The - 73A > C CDH1 promoter variation may lead to differences in the overall survival of sporadic gastric carcinoma patients and allele-specific repressions of CDH1. PMID: 29168119 Overexpression of KLF6-SV1 is associated with young patients, and loss of E-cadherin suggests that this variant correlated with the aggressiveness of nasopharyngeal carcinoma. PMID: 29854578 Smad4 could be considered as a central component of EMT transition in human colorectal cancer that combines with transcriptional factors to reduce E-cadherin and alter the expression of the epithelial phenotype. PMID: 29468299 hnRNP H/F are important for maintenance and differentiation of embryonic stem cells and that this at least in part reflects a switch in TCF3 alternative splicing that leads to repression of CDH1/E-cadherin. PMID: 30115631 E-Cadherin and epithelial syndecan-1 were more highly expressed in intraluminal/luminal unicystic ameloblastoma than in mural unicystic ameloblastoma and solid/multicystic ameloblastoma, whereas the stromal expression of syndecan-1 was higher in mural unicystic ameloblastoma and solid/multicystic ameloblastoma. PMID: 29850393 miR-219-5p promotes tumor growth and metastasis of HCC by regulating CDH1 and can serve as a prognostic marker for HCC patients. PMID: 29862272 Plasma sE-cadherin levels and sE-cadherin/sVE-cadherin ratios are potential biomarkers for COPD. PMID: 29376431 the HDAC inhibitors augmented both Ecadherin and vimentin expression and their effects varied in different cholangiocarcinoma cell lines. Therefore, the clinical use of HDAC inhibitors in biliary cancer should be considered cautiously PMID: 29767267 E-cadherin expression was preserved in 10 (21.28%) of the 47 NSCLCs immunostained with anti-E-cadherin antibody and reduced/absent in 37 of the 47 (78.72%) NSCLCs studied. E-cadherin plays a major role in the intercellular adhesion. PMID: 29556623 CDH1 promoter methylation may be correlated with cervical cancer carcinogenesis, especially for Caucasians. It was associated with histological subtypes PMID: 29237293 High UTX expression is independently associated with a better prognosis in patients with esophageal squamous cell carcinoma (ESCC) and downregulation of UTX increases ESCC cell growth and decreases E-cadherin expression. Our results suggest that UTX may be a novel therapeutic target for patients with ESCC. PMID: 29351209 Data suggest that ECAD, STAT3, Bak, and Bcl-xL are expressed in affected endometrial tissues of women with endometrioid adenocarcinoma depending on neoplasm staging and cell differentiation. This study was conducted using immunohistochemistry of surgically resected tissues. (STAT3 = signal transducer and activator of transcription 3 protein; Bak = pro-apoptotic protein BAK; Bcl-xL = BCL2 associated agonist of cell death) PMID: 28937296 LncRNA RP11-789C1.1 inhibited EMT in GC through the RP11-789C1.1/miR-5003/E-cadherin axis, which could be a promising therapeutic target for Gastric Cancer. PMID: 29991048 Using single-molecule localization microscopy, we show that pAJs in these cells reach more than 1 mum in length and consist of several cadherin clusters with crystal-like density interspersed within sparser cadherin regions. Notably, extrajunctional cadherin appears to be monomeric, and its density is almost four orders of magnitude less than observed in the pAJ regions. PMID: 29691319 CDH1 methylation may play a role in the initiation and progression of salivary carcinoma ex pleomorphic adenoma PMID: 29207084 We illustrate the approach using immunohistochemical measurements of the epithelial-mesenchymal transition marker E-cadherin in a set of colorectal primary tumors from a population-based prospective cohort in North Carolina PMID: 29338703 The aim of our study was to analyze the immunohistochemical expression of beta-catenin, E-cadherin and Snail, depending on clinico-morphological aspects of the laryngeal squamous cell carcinomas. Results revealed variable E-cadherin, beta-catenin and Snail expression, depending on differentiation degree and tumor stage. PMID: 29250652 Twist, E-cadherin, and N-cadherin protein were differently expressed in endometrioid adenocarcinoma tissues and in normal endometrium which indicates their potential function for endometrioid adenocarcinoma development. PMID: 29237910 Findings uncover a new regulatory network in RCC involving metastasis-promoting miR-720 that directly targets expression of key metastasis-suppressing proteins E-cadherin and alphaE-catenin complex. PMID: 28802251 Results show that E-cadherin expression levels were negatively regulated by 90K via ubiquitination-mediated proteasomal degradation in a cell density-dependent manner. PMID: 29207493 these results indicate that increased alpha-actinin-1 expression destabilizes E-cadherin-based adhesions, which is likely to promote the migratory potential of breast cancer cells. Furthermore, our results identify a-actinin-1 as a candidate prognostic biomarker in basal-like breast cancer. PMID: 29742177 High glucose enhances the formation of EZH2/Snail/HDAC1 complex in the nucleus, which in turn causes E-cadherin repression. PMID: 29705809 TGF-beta1 induced epithelial-mesenchymal transition in non-small cell lung cancer cells by upregulating miR-9 and downregulating miR-9's target, E-cadherin. PMID: 29118814 Results show that E-cadherin/beta-catenin complex is disrupted by ICAT promoting epithelial-mesenchymal transition of cervical cancer cells. . PMID: 29048651 Studies categorize cadherin 1 (CDH1) variants, as neutral or deleterious. PMID: 29231860

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.