epitope mapping within an internal region of Crossveinless-2 of human origin
recommended for detection of Crossveinless-2 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
Crossveinless-2 Background Information Crossveinless-2, also known as BMP-binding endothelial regulator protein, Cvl2 or Cv2, is a member of the Chordin family. It is an evolutionarily conserved protein that was first identifed in Drosophila where it is required for the formation of cross-veins in the wing. Crossveinless-2 is a developmentally secreted glycoprotein that contains a trypsin inhibitory-like (TIL) domain, five von Willebrand factor type C (VWFC) domains and one VWF type D (VWFD) domain. Crossveinless-2 regulates BMP homeostasis in early vertebrate embryonic tissues via its cysteine-rich BMP-binding domains. It is expressed during development at sites of high BMP signaling and its expression is responsive to this signaling thereby providing positive feedback. Crossveinless-2 directly interacts with BMP4 and BMP2 and can function either to enhance or inhibit BMP signaling. Crossveinless-2 may function to promote BMP signaling by aiding in ligand transport.
