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Human Polyclonal CLDN3 Primary Antibody for IF, IHC - ABIN6711707
González-Mariscal, Garay, Quirós: Identification of claudins by western blot and immunofluorescence in different cell lines and tissues. in Methods in molecular biology (Clifton, N.J.) 2011
Show all 2 Pubmed References
Human Polyclonal CLDN3 Primary Antibody for ELISA, ICC - ABIN6260865
Ai, Zhang, Gao, Qin, Zhong, Gu, Li, Qiao, Tian, Cui, Yang, Bi, Xiao, Chen, Liu, Zhou, Sun, Yang: Sesquiterpene binding Gly-Leu-Ser/Lys-"co-adaptation pocket" to inhibit lung cancer cell epithelial-mesenchymal transition. in Oncotarget 2018
Human Monoclonal CLDN3 Primary Antibody for CyTOF, FACS - ABIN4898995
Im, Shao, Park, Peterson, Castro, Weissleder, Lee: Label-free detection and molecular profiling of exosomes with a nano-plasmonic sensor. in Nature biotechnology 2015
Atopic dermatitis lesional skin had decreased claudin-3 expression in sweat glands, which was accompanied by sweat leakage. Study results show the crucial role of claudin-3 in preventing sweat gland leakage and suggest that the pathogenesis of dermatoses accompanied by hypohidrosis involves abnormally decreased claudin-3.
Claudin3 promoter methylation status (HR: 5.67; 95% CI: 2.2714.17) but not claudin3 expression was an independent predictor of survival. Claudin3 promoter hypermethylation reduces claudin3 expression and independently predicts poor prognosis.
Immunohistochemical expression levels of cytoplasmic claudins 3 and 7 appear to be novel prognostic factors in triple-negative breast cancer.
CLDN3 could be further evaluated as a novel biomarker for predicting the prognosis of lung squamous cell carcinoma (SqCC) and as a target for the treatment of lung SqCC in the future.
We describe a novel workflow, completely covering the analysis of CLDN3 as an exemplary exosome-based biomarker for prostate cancer from in vitro profiling of cancer exosomes over in silico identification and in vitro retesting to clinical validation.
Data indicate that CDH11, ICAM1 and CLDN3 were overexpressed in tumors when compared to normal esophagus, normal gastric and non-dysplastic Barrett's.
Study provide first biochemically and clinically validated evidence to support a colorectal cancer-suppressive function of claudin-3 by serving as a conjoint rheostat for regulating Stat-3 and Wnt/beta-catenin-signaling.
These tumor samples express CD44 protein at low rather than high levels. There is no correlation between CLDN3 gene expression and protein expression in these CPTAC samples; hence, the claudin-low subtype defined by gene expression is not the same group of tumors as that defined by low expression of CLDN3 protein.
Increased expression of intestinal epithelial claudin-1 with downregulation of claudin-3 has been observed in intestinal inflammatory disorders.
Data show that the charge of Lys65 in claudin 1 (Cldn1) and Glu158 in claudin 3 (Cldn3), and of Gln57 in claudin 5 (Cldn5) are necessary for tight junction (TJ) strand formation.
Mislocalization claudin-3 to nucleus in colon cancer and mislocalization claudin-4 to nucleus in adenomas of the colon were detected for the first time. .
Reg I may play a role in the maintenance of mucosal barrier function by inducing tight junction proteins such as claudins 3 and 4.
Intracellular zinc has an essential role in the maintenance of the intestinal epithelial tight junction barrier through regulation of occludin proteolysis and claudin-3 transcription.
permeability barriers and affected cell morphology, proliferation, migration, AKT signaling, and gene expression. When claudins are exogenously expressed, ARPE-19 more closely model native RPE.
localization of Cldn3, Cldn7 and Cldn10 proteins in the different compartments of murine endometrium up to day 8.5 of pregnancy (dpc) as well as in human endometrium and first trimester decidua
Cln-3 plays a vital role in TNF-modulated paracellular permeability in submandibular epithelium.
Further in vitro studies suggested that the isolated MAbs possessed the desired binding properties for the detection or targeting of CLDN3.
that Claudin-3 expression was restricted to the apical pole of ependymocytes in the subcommissural organ
The expressions of MARVELD2, CLDN1 and CLDN3 mRNA were significantly lower in cholesteatoma tissue and may be involved in epithelium permeability.
increased claudin-3 and claudin-4 expression may play a postive role in the progression and metastasis of gastric cancer
Critical role of claudin-3 in water barrier function was confirmed in Cldn3-/- and Cldn3+/- mice and those with experimentally decreased claudin-3. Those results show the crucial role of claudin-3 in preventing sweat gland leakage and suggest that the pathogenesis of dermatoses accompanied by hypohidrosis involves abnormally decreased claudin-3.
Crystal structure of claudin-3 explains claudin-3 interaction with the tight junction strands.
Claudin-3 was present in the fila olfactoria from the epithelium to the olfactory nerve and in the main and accessory olfactory bulb.
claudin-3 and claudin-5 expression is increased by DHEAS and tight junction formation is stimulated via a Gnalpha11-coupled receptor in Sertoli cells
Cldn3(-/-) mice are fertile and show no Sertoli cell tight junction structural defects, even during the stages of Sertoli cell tight junction remodeling when preleptotene spermatocytes translocate from the basal to the adluminal compartment.
Study highlights a profound role for the choroid plexus in the pathogenesis of multiple sclerosis, and implies that CLDN3 may be regarded as a crucial and novel determinant of blood-cerebrospinal fluid barrier integrity
Seminiferous stage-specific expression and localization of claudin 3 during spermatogenesis regulate the progression of meiosis by promoting germ cell migration across the blood-testis barrier.
Claudin-3 expression in uterine luminal epithelium is stimulated by progesterone and suppressed by heparin-binding epidermal growth factor-like growth factor.
Claudin-3 and Clara cell 10 kDa protein were identified as possible markers of early tobacco smoke-induced epithelial injury along alveolar ducts.
the results indicate that Grhl2 regulates epithelial morphogenesis through transcriptional up-regulation of Cldn3 and Cldn4, as well as of Rab25, which increases the Cldn4 protein and its localization at TJs
Claudin-3 is expressed at the variety of epithelial tissues in inner ear including Organ of Corti, stria vascularis, Reissner's membrane, spiral limbus, vestibular sensory epithelia, dark cell area.
Mechanism of Clostridium perfringens enterotoxin interaction with claudin-3/-4 protein suggests structural modifications of the toxin to target specific claudins
Claudin-3 in the apical-most regions maintains the impermeable tight junctions during lactation, and claudin-4 contributes to the permeability changes of them immediately after parturition and weaning.
Cldn3 may therefore promote tubule formation and expansion of the ureteric bud epithelium
internalization of claudin 3 plays a crucial role in the remodeling of tight junctions
In the absence of follicle-stimulating hormone receptor signaling, claudin-3 is selectively upregulated in ovarian surface epithelium and tumors in comparison to wild type.
Claudin-3 and claudin-4 receptors are highly overexpressed in carcinosarcoma
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are comprised of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this intronless gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. It is also a low-affinity receptor for Clostridium perfringens enterotoxin, and shares aa sequence similarity with a putative apoptosis-related protein found in rat.
, CPE-R 2
, CPE-receptor 2
, Clostridium perfringens enterotoxin receptor 2
, ventral prostate.1 protein homolog
, ventral prostate.1-like protein
, clostridium perfringens enterotoxin receptor 2
, ventral prostate.1 protein
, integral membrane protein claudin-3
, tight junction-associated protein