Recombinant Human Claudin-3 (CLDN3) Protein (His-B2M)

Name: Recombinant Human Claudin-3 (CLDN3) Protein (His-B2M)
Brand: Beta LifeScience
SKU: BLC-02247P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Fc receptors, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Claudin-3 (CLDN3) Protein (His-B2M) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O15551
Target Symbol	CLDN3
Synonyms	CLDN3; C7orf1; CPETR2; Claudin-3; Clostridium perfringens enterotoxin receptor 2; CPE-R 2; CPE-receptor 2; Rat ventral prostate.1 protein homolog; hRVP1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-B2M
Target Protein Sequence	RVSAFIGSNIITSQNIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAAR
Expression Range	30-80aa
Protein Length	Partial
Mol. Weight	19.7kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location	Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Protein Families	Claudin family
Database References	HGNC: 2045 OMIM: 602910 KEGG: hsa:1365 STRING: 9606.ENSP00000378577 UniGene: Hs.647023
Associated Diseases	CLDN3 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.

Gene Functions References

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. PMID: 29749528
Immunohistochemical expression levels of cytoplasmic claudins 3 and 7 appear to be novel prognostic factors in triple-negative breast cancer. PMID: 29482498
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. PMID: 29511369
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. PMID: 28396511
Data indicate that CDH11, ICAM1 and CLDN3 were overexpressed in tumors when compared to normal esophagus, normal gastric and non-dysplastic Barrett's. PMID: 27363029
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. PMID: 28783170
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. PMID: 28287265
Increased expression of intestinal epithelial claudin-1 with downregulation of claudin-3 has been observed in intestinal inflammatory disorders. PMID: 28493289
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. PMID: 28415153
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. . PMID: 28295005
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. PMID: 27151944
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. PMID: 27593915
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 PMID: 26340953
Cln-3 plays a vital role in TNF-modulated paracellular permeability in submandibular epithelium. PMID: 26148935
Further in vitro studies suggested that the isolated MAbs possessed the desired binding properties for the detection or targeting of CLDN3. PMID: 25744656
that Claudin-3 expression was restricted to the apical pole of ependymocytes in the subcommissural organ PMID: 24974365
The expressions of MARVELD2, CLDN1 and CLDN3 mRNA were significantly lower in cholesteatoma tissue and may be involved in epithelium permeability. PMID: 25319490
Univariate analyses indicated that the T stage, lymph node metastasis, the TNM stage, and the expression of claudin-3, beta-catenin, and vimentin were significant predictors for overall survival (OS). PMID: 25820701
Data from live-cell imaging suggest at least two different cis-interaction interfaces within CLDN3 homopolymers as well as within CLDN1/CLDN3 heteropolymers. PMID: 25849148
our findings demonstrated that CLDN3 is an epigenetically silenced metastasis suppressor gene in Hepatocellular carcinoma PMID: 25277196
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 PMID: 24356983
Claudin 3 was expressed in all non-goblet columnar lined oesophagus, Barrett's oesophagus, high grade dysplasia and adenocarcinoma. PMID: 24290871
Claudin-3 overexpression increases the malignant potential of colorectal cancer cells. PMID: 24069372
folding and assembly of CLDN3 and CLDN5 into the tight junction are controlled by non-conserved residues in the transmembrane 3 and extracellular loop 2 segments PMID: 24478310
Our comparative analysis of CLDN3 profile in breast and ovarian cancer clearly indicates organ specificity. PMID: 23529315
Snail and Claudin-3 may play important roles in invasion and metastasis in NSCLC PMID: 23075682
Claudin-3 expression in uterine luminal epithelium is stimulated by progesterone and suppressed by heparin-binding epidermal growth factor-like growth factor. PMID: 23909989
High CLDN3 expression is associated with tumor growth and metastases. PMID: 23097631
Dow-regulation of Claudin-3 is associated with the progression of early gastric adenocarcinomas. PMID: 22290341
CLDN3 may have a role in ovarian cancer, and its inhibition by short hairpin RNA could be a treatment strategy. PMID: 21519794
Analysis of staining intensities of CLDN 1 and 3 is useful as an auxiliary diagnostic and prognostic tool in patients with salivary gland mucoepidermoid carcinoma. PMID: 21184237
demonstrate that claudin-3 alters the tight junction meshwork and seals the paracellular pathway against the passage of small ions of either charge and uncharged solutes PMID: 20655293
Claudin-3 expression in Epstein-Barr virus-associated nasopharyngeal carcinoma was variable PMID: 20204275
Increased expressions of CLDN 2 and 3 suggest structural changes of tight junction in coeliac disease which may be, at least in part, responsible for increased permeability and proliferation observed in coeliac disease. PMID: 20143085
Here we show for the first time in both an experimental and clinical setting a strong relation between intestinal tight junction loss and urinary claudin-3 levels PMID: 19525861
Airway tight junctions are regulated by claudin interactions that confer the selectivity of the junction. PMID: 12909588
up-regulation of DDR1, CLDN3, and epithelial cell adhesion molecule are early events in the development of epithelial ovarian cancer PMID: 15240533
in breast tissue, CLDN3 expression is similar in tumours and surrounding normal tissue, as demonstrated by immunohistochemistry and real-time PCR PMID: 15743508
claudin-3 phosphorylation by PKA may provide a mechanism for the disruption of tight junctions in ovarian cancer PMID: 15905176
The gene expression profile of hepatic stem cells throughout life consists of high levels of expression of claudin-3 (CLDN-3). PMID: 16627685
Claudin tight junction proteins in endoscopy biopsy samples showed Barrett's metaplasia contains more claudin-2 and claudin-3 than found in normal esophageal mucosa, but markedly lower claudins 1 and 5, indicating very different tight junction barriers. PMID: 17103306
Overexpression of claudin-3 is associated with uterine serous papillary carcinoma PMID: 17326053
When compared, small-cell-lung cancers, carcinoid tumors, and adenocarcinomas revealed significant differences re: CLDN3 expression. PMID: 17418912
CLDN3 overexpression can be used as a prognostic indicator in ovarian serous carcinomas and it may be a promising target for antibody-based therapy of ovarian carcinomas. PMID: 17647191
siRNA-mediated knockdown of Sp1 led to a significant decrease of CLDN3 expression at both the mRNA and protein levels, demonstrating a crucial role for this transcription factor in the regulation of CLDN3. PMID: 17986852
Claudin-3 and claudin-7 expression in effusions independently predicts poor survival in ovarian cancer. PMID: 18439941
claudins 1 and 3 had a significant effect on overall survival in patients with urothelial carcinoma of the upper urinary tract. PMID: 18550469
This is the first study to demonstrate that claudin-3 is involved in the barrier function of gastric epithelial cells and that rebamipide abolishes the H2O2-induced decrease in claudin-3 protein. PMID: 18774778
For the first time this study proves the presence of Claudin-1, Claudin-3 and Claudin-5 in ECV304 (obtained from ECACC) cell layers and the inducibility of their expression by glioma-conditioned media. PMID: 18817843
Using a panel of four genes (AHRR, p16INK4a, MT1G, and CLDN3) resulted in sensitivity and specificity of 50% and 68%, respectively and may have utility for early detection of esophageal squamous dysplasia and early ESCC. PMID: 19137073

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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.