Osteopontin (N-terminal region) Antibody

Osteopontin (OPN) is a 34 kDa sialic acid rich member of small integrin-binding ligand N-linked glycoproteins. It is expressed in many different tissues and is post-translationally modified at multiple sites with both glycosylation and phosphorylation. The mature post-translationally modified protein is 60 kDa. OPN is involved with cell survival, proliferation, invasion, and stem like behavior. OPN can interact with CD44, bind hydroxyapatite, and activates many integrins. These interactions are important for OPN function in cell matrix formation. A higher presence of OPN has been found in a variety of cancers, leading to increased tumor growth and metastasis. In addition, OPN is involved in type I immunity through its function as a cytokine where it can enhance production of interferon-gamma and interleukin-12 and reduce production of interleukin-10.

Clone M574 was generated from a recombinant protein containing amino acid residues in the N-terminal region of human osteopontin. This sequence has high homology with rat and mouse osteopontin.

Clone M574 was purified using Protein G chromatography. The antibody detects a 60 kDa* protein corresponding to the molecular mass of Osteopontin on SDS-PAGE immunoblots of human MDA-MB-231 cells and human full length recombinant Osteopontin protein.