Human Recombinant CLDN11 protein, Fc Tag (V2LY-0526-LY3196)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
Fc Tag
Protein Construction
This product is Human Recombinant CLDN11 protein, Fc Tag consist of Amino Acid: 23-82 and predicts a molecular mass of 33.2 kDa.
Molecule Mass
33.2 kDa
Sequence
Amino Acid: 23-82
Species
Human

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

Purity
>90% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Claudin 11
Function
Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Biological Process
Axon ensheathment Source: Ensembl
Bicellular tight junction assembly Source: GO_Central
Calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: UniProtKB
Cell adhesion Source: GO_Central
Spermatogenesis Source: Ensembl
Tight junction assembly Source: ARUK-UCL
Cellular Location
Cell membrane; Tight junction
Topology
Cytoplasmic: 1
Helical: 2-22
Extracellular: 23-82
Helical: 83-103
Cytoplasmic: 104-122
Helical: 123-143
Extracellular: 144-157
Helical: 158-178
Cytoplasmic: 179-207

Pörtner, C., Rode, K., Hollenbach, J., Thiemeyer, H., Beineke, A., Günzel-Apel, A. R., & Brehm, R. (2020). Expression of claudin-11 in canine prepubertal testes, and in canine adult testes showing normal spermatogenesis, impaired spermatogenesis, or testicular neoplasia. Theriogenology, 148, 122-131.

Kato, T., Mizuno, K., Nishio, H., Moritoki, Y., Kamisawa, H., Kurokawa, S., ... & Yasui, T. (2020). Disorganization of claudin‐11 and dysfunction of the blood‐testis barrier during puberty in a cryptorchid rat model. Andrology, 8(5), 1398-1408.

Li, C. F., Chen, J. Y., Ho, Y. H., Hsu, W. H., Wu, L. C., Lan, H. Y., ... & Yang, M. H. (2019). Snail-induced claudin-11 prompts collective migration for tumour progression. Nature cell biology, 21(2), 251-262.

Lindsey, R. C., Xing, W., Pourteymoor, S., Godwin, C., Gow, A., & Mohan, S. (2019). Novel role for Claudin‐11 in the regulation of osteoblasts via modulation of ADAM10‐mediated notch signaling. Journal of Bone and Mineral Research, 34(10), 1910-1922.

Horné, F., Dietze, R., Berkes, E., Oehmke, F., Tinneberg, H. R., Meinhold-Heerlein, I., & Konrad, L. (2019). Impaired localization of claudin-11 in endometriotic epithelial cells compared to endometrial cells. Reproductive Sciences, 26(9), 1181-1192.

Baek, J. M., Cheon, Y. H., Kwak, S. C., Jun, H. Y., Yoon, K. H., Lee, M. S., & Kim, J. Y. (2018). Claudin 11 regulates bone homeostasis via bidirectional EphB4-EphrinB2 signaling. Experimental & molecular medicine, 50(4), 1-18.

Shen, Z., Cao, B., Lin, L., Zhou, C., Ye, D., Qiu, S., ... & Cui, X. (2017). The clinical signification of claudin-11 promoter hypermethylation for laryngeal squamous cell carcinoma. Medical science monitor: international medical journal of experimental and clinical research, 23, 3635.

Li, J., Zhou, C., Ni, S., Wang, S., Ni, C., Yang, P., & Ye, M. (2017). Methylated claudin-11 associated with metastasis and poor survival of colorectal cancer. Oncotarget, 8(56), 96249.

Yang, P., Zhang, M., Liu, X., & Pu, H. (2017). MicroRNA-421 promotes the proliferation and metastasis of gastric cancer cells by targeting claudin-11. Experimental and therapeutic medicine, 14(3), 2625-2632.

Nissinen, L., Siljamäki, E., Riihilä, P., Piipponen, M., Farshchian, M., Kivisaari, A., ... & Kähäri, V. M. (2017). Expression of claudin‐11 by tumor cells in cutaneous squamous cell carcinoma is dependent on the activity of p38δ. Experimental dermatology, 26(9), 771-777.

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

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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