Recombinant Human Claudin-1 (CLDN1) Protein (His)

Name: Recombinant Human Claudin-1 (CLDN1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02046P
Price: 2495.2 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Claudin-1 (CLDN1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O95832
Target Symbol	CLDN1
Species	Homo sapiens (Human)
Expression System	in vitro E.coli expression system
Tag	N-10His
Target Protein Sequence	MANAGLQLLGFILAFLGWIGAIVSTALPQWRIYSYAGDNIVTAQAMYEGLWMSCVSQSTGQIQCKVFDSLLNLSSTLQATRALMVVGILLGVIAIFVATVGMKCMKCLEDDEVQKMRMAVIGGAIFLLAGLAILVATAWYGNRIVQEFYDPMTPVNARYEFGQALFTGWAAASLCLLGGALLCCSCPRKTTSYPTPRPYPKPAPSSGKDYV
Expression Range	1-211aa
Protein Length	Full Length
Mol. Weight	24.2 kDa
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	Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions.; (Microbial infection) Acts as a co-receptor for hepatitis C virus (HCV) in hepatocytes. Associates with CD81 and the CLDN1-CD81 receptor complex is essential for HCV entry into host cell. Acts as a receptor for dengue virus.
Subcellular Location	Cell junction, tight junction. Cell membrane; Multi-pass membrane protein. Basolateral cell membrane.
Protein Families	Claudin family
Database References	HGNC: 2032 OMIM: 603718 KEGG: hsa:9076 STRING: 9606.ENSP00000295522 UniGene: Hs.439060
Associated Diseases	Ichthyosis-sclerosing cholangitis neonatal syndrome (NISCH)
Tissue Specificity	Strongly expressed in liver and kidney. Expressed in heart, brain, spleen, lung and testis.

Gene Functions References

the accumulation and toxicity of doxorubicin were rescued by CLDN1 siRNA in A549R cells. We suggest that CLDN1 is upregulated by CDDP resistance through activation of a PI3K/Akt/NF-kappaB pathway, resulting in the inhibition of penetration of anticancer drugs into the inner area of spheroids PMID: 29524521
Our data indicate that CLDN1 targeting with an anti-CLDN1 mAb results in decreased growth and survival of CRC cells. This suggests that CLDN1 could be a new potential therapeutic target. PMID: 28659146
Human Growth Hormone Inhibits CLAUDIN-1 Expression Through Activation of Signal Transducer and Activator of Transcription 3 (STAT3). PMID: 28617312
CLDN1 promotes invasion and metastasis in cervical cancer cells via the expression of EMT/invasion-related genes. PMID: 27974683
Cycling hypoxia could induce significant changes in CLDN1 and CLDN7 expression in nasopharyngeal cancer cells, indirectly regulation P18 expression and affecting cell invasion/proliferation. PMID: 28055967
Rab25 is amplified and enhances aggressiveness in luminal B cancers while in claudin-low tumors, Rab25 is lost indicating possible anti-tumor functions PMID: 27259233
association of genetic polymorphisms of claudin-1 with small vessel vascular dementia PMID: 28273404
Glutamine increased claudin-1 expression in the colonic mucosa of patients with irritable bowel syndrome. PMID: 25972430
CLDN-1 promoted the migration and EMT through the Notch signaling pathway. PMID: 28316062
In human lung tissue, Claudin-1 is higher in RBFOX3-positive cells than in RBFOX3-negative cells. Immunostaining and mRNA quantification revealed that protein levels, but not mRNA levels, of Claudin-1 are increased by RBFOX3. PMID: 28126724
Data show that miR-30a could bind to the 3'-untranslted region of Slug mRNA and increased expression of claudins, a family of tight junction transmembrane proteins. PMID: 26918943
These findings indicate a previously unrecognized mechanism that miR-142-5p, targeting CLDN1, plays an important role in Hashimoto's thyroiditis pathogenesis. PMID: 27277258
Here, the authors identified an interaction between claudin-1 and Sec24C, a cargo-sorting component of the coat protein complex II (COPII) vesicular transport system. PMID: 28679754
Aberrant expression of the tight junction molecules claudin-1 and zonula occludens-1 mediates cell growth and invasion in oral squamous cell carcinoma cells. PMID: 27436828
Increased expression of intestinal epithelial claudin-1 with downregulation of claudin-3 has been observed in intestinal inflammatory disorders. PMID: 28493289
Studies indicate claudin 1 (CLDN-1) as a target for improving epidermal drug absorption and preventing HCV infection and of claudin 4 (CLDN-4) as a target for anticancer therapeutics. PMID: 28415141
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
Studies indicate that claudin-1 accumulate in early endosomes in both epithelial and endothelial cells. PMID: 28415156
Claudin-low tumors were associated with young age of onset, higher tumor grade, larger tumor size, extensive lymphocytic infiltrate and a circumscribed tumor margin. Patients with claudin-low tumors had a worse overall survival when compared to patients with luminal A type breast cancer. PMID: 28045912
These results revealed that CLDN1 contributed to cancer stem cell features of hepatocellular carcinoma, which was altered by TMPRSS4 expression via ERK1/2 signaling pathway, providing promising targets for novel specific therapies. PMID: 28651932
Data suggest that epithelial-mesenchymal transition (EMT) is regulated by ZMYND8 (receptor for activated protein kinase C) which selectively activates gene promoters of CLDN1 (claudin 1) and CDH1 (E-cadherin) in breast cancer cells; thus, the presence of ZMYND8 could be implicated in maintaining epithelial phenotype of cells; ZMYND8 regulates invasion/migration of breast cancer cells. PMID: 28432260
The data suggested that miR-29a may regulate tumor growth and migration by targeting CLDN1. PMID: 28342862
TNF-alpha mediated regulation of claudin-1 and tumorigenic abilities of colon cancer cells. PMID: 27742576
CLDN1 is significantly hypomethylated in tumor samples and that the membrane staining intensity for claudin 1, 4, and 7 is significantly lower in colorectal cancer tissues than in adjacent nonneoplastic tissue. PMID: 28381183
CLDN1 rather than variants in FLG may be involved in the susceptibility of AD in the Ethiopian population PMID: 27581203
CLDN1 overexpression is a good prognostic factor in NSCLC. PMID: 27687058
Studies showthat CLDN1 is downregulated in lung adenocarcinoma and that low CLDN1 messenger ribonucleic acid (mRNA) expression leads to shorter overall survival. PMID: 27766775
The loss of claudin-1 appears to be involved in the pathogenesis of pterygium PMID: 26820697
autotypic tight junctions molecular composition, like claudin-1 and occludin expression could influence the demyelinating process by altering the permeability of the blood-nerve barrier. PMID: 26662145
High CLDN1 expression is associated with Cervical cancer. PMID: 26463354
Claudin-1 expression was correlated with lymphatic microvessel generation in hypopharyngeal squamous cell carcinoma and with patient survival. PMID: 26436506
High CLAUDIN-1 expression is associated with metastasis in follicular thyroid carcinoma. PMID: 26219679
The highest expression of claudin-1 was observed in well-differentiated oral squamous cell carcinomas, whereas poorly differentiated tumors exhibited mostly no expression of claudin-1. PMID: 25517868
Report genetic polymorphism of TJ component claudin-1 and their haplotypes are associated with leukoaraiosis. PMID: 25956626
Using a human liver-chimeric mouse model, we show that a monoclonal antibody specific for the TJ protein claudin-1 (ref. 7) eliminates chronic HCV infection without detectable toxicity PMID: 25798937
delocalization of claudin-1 induced by PKC phosphorylation contributes to metastatic capacity of osteosarcoma cells PMID: 26361141
The expressions of MARVELD2, CLDN1 and CLDN3 mRNA were significantly lower in cholesteatoma tissue and may be involved in epithelium permeability. PMID: 25319490
There was no difference in the frequency of fractures or renal lithiasis between the rs219780 genotype groups in PHPT patients. Nor was there any relationship between the T or C alleles and BMD or biochemical parameters. PMID: 26554238
CLD1-mediated hepatoma cell invasiveness occurs via heat shock factor 1 (HSF1) activation. PMID: 26157141
Findings suggest that CLDN1 is oncogenic in gastric cancer and its malignant potential may be attributed in part to regulation of anoikis, by mediating membrane beta-catenin-regulated cell-cell adhesion and cell survival. PMID: 25544763
reduction of claudin-1 expression may contribute to the progression of gastric tumors PMID: 25755790
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
Suggest that claudin 1 is an important messenger that regulates TNF-alpha-induced gene expression and migration in gastric cancer cells. PMID: 25548484
The findings suggest that down regulated CLDN1 and CLDN5 genes have potential relevance in relation to the progression of glioblastoma multiforme. PMID: 25345514
Positive expressions of Claudin-1 in retinoblastoma were fewer than those in retina; higher positive expressions were found in differentiated tissues than in undifferentiated tissues; Claudin-1 expressed more positively in optic nerves without invasion. PMID: 26122225
findings suggest that homozygous CD81 rs708564 TT may be a genetic modifier for avoiding HCV infection whether as a sole single nucleotide polymorphism or combined with the CLDN1 rs893051 GG genotype PMID: 25934191
Our results indicate that CLDN4 expression is correlated with poor prognosis, and CLDN1 expression may be an indicator of recurrence of oral squamous cell carcinoma. PMID: 25964581
CLDN1-negative phenotype predicts a high risk of recurrence and death in triple-negative breast cancer. PMID: 25393310
dystopic subcellular localizations of Snail-1 and claudin-1 may participate in changes of cellular morphology and behavior which might be associated with altered effectory pathways of proteins and thus substantially contribute to the cancer development. PMID: 22408413
Data show that C-terminal domain of Clostridium perfringens enterotoxin (cCPE)-binding to claudin 1 and claudin 5 is prevented by two residues in extracellular loop 2 of Cld1 (Asn(150) and Thr(153)) and Cld5 (Asp(149) and Thr(151)). PMID: 25342221

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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.

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