Anti-LI Cadherin antibody [SP183] - C-terminal

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

LI Cadherin also known as Cadherin-17 is a protein that plays a significant role in cell adhesion specifically in epithelial cells. This protein belongs to the cadherin family and has a molecular mass of approximately 88 kDa. LI Cadherin is mainly expressed in the gastrointestinal tract including areas like the stomach and small intestine. It is found on the surfaces of cells where it facilitates cell-cell interaction by binding with other cadherin proteins on adjacent cells.

Biological function summary

This cadherin protein is important for maintaining the integrity of epithelial layers in the gastrointestinal tract. It contributes to the formation of adherens junctions which are necessary for the maintenance of tissue architecture and cellular communication. As part of a larger protein complex in adherens junctions it interacts with cytoskeletal elements to help stabilize cell structures. This mechanical support ensures that cells remain tightly adhered under various physiological conditions.

Pathways

LI Cadherin is involved in pathways that govern cell adhesion and signal transduction. It participates in the Wnt signaling pathway which is vital for cell proliferation and differentiation. Moreover it interacts with E-cadherin and β-catenin within the Wnt pathway aiding in the regulation of gene expression and cellular morphology. These interactions are important for maintaining normal cell behavior and preventing unwanted cell proliferation.

Associated diseases and disorders

LI Cadherin's expression has been linked to gastrointestinal cancers particularly gastric and colorectal cancers. Aberrations in cadherin-mediated cell adhesion can lead to tumorigenesis as disrupted cell adhesion can cause increased cell motility and invasion. LI Cadherin also engages with proteins such as α-catenin in tumor cells affecting cellular responses to cancerous transformations. By understanding these relationships researchers aim to develop targeted therapies to address malignancies associated with disrupted cadherin function.