Axl Extracellular Domain (human, recombinant)

Axl is a receptor tyrosine kinase and member of the TAM kinase family. It is composed of two immunoglobulin-like (Ig-like) domains, two fibronectin-like III domains, an extracellular cleavage site, a transmembrane region, and a C-terminal kinase domain. It is ubiquitously expressed and localizes to the cell membrane. After homodimerization, Axl is activated by growth arrest-specific protein 6 (GAS6) and is involved in promoting proliferation and hematopoietic lineage differentiation and negatively regulating antigen-presenting cell activation. The extracellular domain of Axl can be cleaved by metalloproteinases, releasing soluble Axl to bind and activate membrane-associated Axl. In cancer, Axl promotes metastasis, epithelial-to-mesenchymal transition (EMT), and survival. Increased expression of AXL is associated with shorter progression-free survival in patients with non-small cell lung cancer (NSCLC). Cayman's Axl Extracellular Domain (human, recombinant) protein can be used for binding assays. This protein consists of 428 amino acids, has a calculated molecular weight of 46. kDa, and a predicted N-terminus of Glu33 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 60-70 kDa due to glycosylation.