epitope mapping at the C-terminus of Liprinβ1 of human origin
recommended for detection of Liprinβ1 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
Liprin β1 Background Information Liprins interact with members of the leukocyte common antigen-related (LAR) family of transmembrane protein tyrosine phosphatases, which are implicated in axon guidance and mammary gland development. Liprins are multivalent proteins that form complex structures and act as scaffolds for the recruitment and anchoring of LAR phosphatases. Based on sequence similarites and binding characteristics, liprins are subdivided into å-type and ∫-type liprins. Both å- and ∫-liprins homodimerize via their N-terminal, coiled coil regions. Liprin ∫1 interacts with S100A4, a calcium-binding protein related to tumor invasiveness and metastasis. The two proteins colocalize in the cytoplasm and at protrusion sites in the plasma membrane. The interaction of Liprin ∫1 and S100A4 inhibits the phosphorylation of Liprin ∫1 by PKC and protein kinase CK2 in vitro.
