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Claudin18.2 ICC ER1902-86
Claudin18.2 ICC ER1902-86

Claudin Antibodies

What are Claudins?

Claudins are a family of proteins which, along with occludin, are the most important components of the tight junctions. Tight junctions establish the paracellular barrier that controls the flow of molecules in the intercellular space between the cells of an epithelium.

Claudin 5

At theblood–brain barrier, Claudin-5 is the most enrichedtight junction protein and its dysfunction has been implicated in neurodegenerative disorders such as Alzheimer's disease, neuroinflammatory disorders such as multiple sclerosis as well as psychiatric disorders including depression and schizophrenia.

Claudin 7

Claudin-7 plays a significant role in maintaining the physiological functions and pathological conditions of the TJ barrier. The dysregulation of claudin-7 plays a tumor suppressor role or conversely has carcinogenic effects in different target tissues or cells, but the exact underlying mechanism is still unclear. In this review, we will summarize the expression pattern of claudin-7 in tumors, focusing on the expression and regulation of claudin-7 in colorectal cancer and discussing the correlation between claudin-7 and invasion, metastasis and epithelial–mesenchymal transition (EMT) in colorectal cancer.

Claudin 18

Claudin-18 is a tight-junction protein uniquely expressed in gastric epithelial cellsand has been shown to be expressed in gastric and pancreatic adenocarcinoma. There are two isotypes:

Claudin 18.2 is reported only limitedly expressed in differentiated epithelial cells of the gastric mucosa whereas significantly expressed in a variety of malignant tumor tissues such as gastric cancer, pancreatic cancer, cholangiocarcinoma, ovarian cancer and lung cancer etc. Thus Claudin 18.2 has emerged as an ideal target for immunotherapy including monoclonal antibody, bispecific antibody, ADC and CAR-T therapy.

Claudin 18. is highly homologous to Claudin 18.2. Taking the human Claudin 18 protein as an example, the two isoforms only differ by 7 amino acids in the first extracellular domain (the mouse origin contains 8 amino acid differences).


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