Background:  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.

Description: Rabbit polyclonal to BMPER

Immunogen: KLH conjugated synthetic peptide derived from BMPER

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 76 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.