CAM Ligands

Fibronectin is an adhesive glycoprotein with a molecular mass of 440 kDa. It is believed to be important for the formation of a provisional matrix that promotes cell adhesion and migration during wound healing. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases. It has also shown that several of its proteolytic breakdown products exhibit unexpected and mostly harmful biological activities. This antibody has specificity for human fibronectin.

C3 is a key component of the complement system since classical and alternative activation pathways merge at the C3 activation step when C3 is split into C3a and C3b. The molecular mass of C3 is 185 kDa and it consists of two chains (110 kDa and 75 kDa) held together by disulfide bonds. This antibody is specific for human C3.

C3 is a key component of the complement system since classical and alternative activation pathways merge at the C3 activation step when C3 is split into C3a and C3b. The molecular mass of C3 is 185 kDa and it consists of two chains (110 kDa and 75 kDa) held together by disulfide bonds. This antibody is specific for human C3d, a fragment of the alpha chain.

Complement C3a is an anaphylatoxin of 77 amino acid residues released by the action of the C3 convertases on the N-terminal of the alpha chain of C3. It is rapidly inactivated by serum carboxypeptidase N which removes the C-terminal arginine residue generating C3a (desArg). This antibody recognizes an epitope that is present on human C3, C3a and C3a (desArg) and does not react with C4a or C5a.

Type III collagen is present in the walls of arteries, intestines and the uterus, where it strenghtens the connective tissue. Patients with defects in the type III collagen (ex. Ehlers-Danlos syndrome) are at risk of rupture of major arteries or the intestine. This antibody is highly specific for type III collagen. It has been shown to have no cross-reactivity with type I and V collagens by ELISA and immunoblotting. There is no evidence for cross-reactivity with other connective tissue proteins (laminin, fibronectin, elastin.