Human Recombinant CLDN3-VLP protein (V2LY-0526-LY3203)

Name: Human Recombinant CLDN3-VLP protein
SKU: V2LY-0526-LY3203
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

HEK293 Cells

Protein Species

Human

Protein Construction

This product is Human Recombinant CLDN3-VLP protein consist of Amino Acid: 1-220 and predicts a molecular mass of 23.32 kDa.

Molecule Mass

23.32 kDa

Sequence

Amino Acid: 1-220

Species

Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Endotoxin

Please contact us for more information.

Format

Liquid

Buffer

Tirs, NaCl, Glycine, Arginine

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -70°C. Store it under sterile conditions at -70°C or lower. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

Claudin 3

Function

Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.

Biological Process

Actin cytoskeleton reorganization Source: ARUK-UCL
Bicellular tight junction assembly Source: UniProtKB
Calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: Ensembl
Cell adhesion Source: GO_Central
Cell junction maintenance Source: ARUK-UCL
Epithelial cell morphogenesis Source: UniProtKB
Establishment of endothelial blood-brain barrier Source: ARUK-UCL
Maintenance of blood-brain barrier Source: ARUK-UCL
Negative regulation of cell migration Source: ARUK-UCL
Negative regulation of cell population proliferation Source: ARUK-UCL
Negative regulation of gene expression Source: ARUK-UCL
Negative regulation of wound healing Source: ARUK-UCL
Positive regulation of bicellular tight junction assembly Source: ARUK-UCL
Positive regulation of cell junction assembly Source: ARUK-UCL
Positive regulation of cell migration Source: ARUK-UCL
Positive regulation of gene expression Source: ARUK-UCL
Positive regulation of metallopeptidase activity Source: ARUK-UCL
Positive regulation of protein phosphorylation Source: ARUK-UCL
Positive regulation of wound healing Source: ARUK-UCL
Regulation of cell morphogenesis Source: ARUK-UCL
Regulation of membrane permeability Source: ARUK-UCL
Regulation of transepithelial transport Source: ARUK-UCL
Response to ethanol Source: Ensembl
Response to hypoxia Source: UniProtKB

Cellular Location

Cell membrane; Tight junction

Involvement in disease

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.

Topology

Cytoplasmic: 1-8
Helical: 9-29
Extracellular: 30-80
Helical: 81-101
Cytoplasmic: 102-115
Helical: 116-136
Extracellular: 137-159
Helical: 160-180
Cytoplasmic: 181-220

Feng, J., Xu, Y., Wei, Z., Xia, Y., Zhang, H., Shen, C., ... & Fang, Y. (2022). Capsaicin inhibits migration and invasion via inhibiting epithelial-mesenchymal transition in esophageal squamous cell carcinoma by up-regulation of claudin-3 expression. Journal of Functional Foods, 89, 104934.

Anwer, S., Branchard, E., Dan, Q., Dan, A., & Szaszi, K. (2021). Tumor necrosis factor-α induces claudin-3 upregulation in kidney tubular epithelial cells through NF-κB and CREB1. American Journal of Physiology-Cell Physiology, 320(4), C495-C508.

Hempel, C., Protze, J., Altun, E., Riebe, B., Piontek, A., Fromm, A., ... & Piontek, J. (2020). Assembly of tight junction strands: Claudin-10b and claudin-3 form homo-tetrameric building blocks that polymerise in a channel-independent manner. Journal of molecular biology, 432(7), 2405-2427.

Yang, H., Park, H., Lee, Y. J., Choi, J. Y., Kim, T., Rajasekaran, N., ... & Shin, Y. K. (2020). Development of human monoclonal antibody for claudin-3 overexpressing carcinoma targeting. Biomolecules, 10(1), 51.

Yuan, M., Chen, X., Sun, Y., Jiang, L., Xia, Z., Ye, K., ... & He, Q. (2020). ZDHHC12-mediated claudin-3 S-palmitoylation determines ovarian cancer progression. Acta Pharmaceutica Sinica B, 10(8), 1426-1439.

Danzinger, S., Tan, Y. Y., Rudas, M., Kastner, M. T., Weingartshofer, S., Muhr, D., ... & kConFab Investigators. (2018). Differential claudin 3 and EGFR expression predicts BRCA1 mutation in triple-negative breast cancer. Cancer investigation, 36(7), 378-388.

Che, J., Yue, D., Zhang, B., Zhang, H., Huo, Y., Gao, L., ... & Cao, B. (2018). Claudin-3 inhibits lung squamous cell carcinoma cell epithelial-mesenchymal transition and invasion via suppression of the Wnt/β-catenin signaling pathway. International journal of medical sciences, 15(4), 339.

Yamaga, K., Murota, H., Tamura, A., Miyata, H., Ohmi, M., Kikuta, J., ... & Katayama, I. (2018). Claudin-3 loss causes leakage of sweat from the sweat gland to contribute to the pathogenesis of atopic dermatitis. Journal of Investigative Dermatology, 138(6), 1279-1287.

Zhang, L., Wang, Y., Zhang, B., Zhang, H., Zhou, M., Wei, M., ... & Wang, C. (2017). Claudin-3 expression increases the malignant potential of lung adenocarcinoma cells: role of epidermal growth factor receptor activation. Oncotarget, 8(14), 23033.

Worst, T. S., Von Hardenberg, J., Gross, J. C., Erben, P., Schnölzer, M., Hausser, I., ... & Boutros, M. (2017). Database-augmented mass spectrometry analysis of exosomes identifies claudin 3 as a putative prostate cancer biomarker. Molecular & Cellular Proteomics, 16(6), 998-1008.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

For research use only. Not intended for any clinical use.

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