LAR Mouse, Unlabeled, Clone: 7, BD

Descripción

The Leukocyte common Antigen-Related (LAR) receptor protein tyrosine phosphatase (RPTP) is one of approximately 20 known, distinct transmembrane RPTPs. LAR consists of an extracellular region with three Ig-like and eight fibronectin type III-like (FNIII) domains and a cytoplasmic region containing two tyrosine phosphatase domains typical of RPTPs. The Ig and FNIII domains of LAR show some sequence similarity to domains in the neural cell adhesion molecule N-CAM, a neural surface glycoprotein which mediates cell adhesion and neurite outgrowth. Studies suggest that LAR regulates neurite outgrowth and pathfinding during neural development. N-CAM and other cell adhesion molecules that affect neurite outgrowth, such as L1, TAG-1, and fasciculin II, lack intrinsic kinase or phosphatase activity. Thus, LAR is part of a distinct class of proteins with both cell adhesion and tyrosine phosphatase functions. LAR transcripts are alternatively spliced and that splicing is regulated during development. It is postulated that the various spliced forms of LAR each have specialized functions in the nervous system and play a role in neural development and regeneration.