CAM Ligands

Type I collagen is present in connective tissue and bone where it makes up about 90% of the organic matrix. Type I collagen is produced from type-I procollagen by the proteolytic cleavage of N- and C-telopeptides, which are released into the circulation. The propeptides can be measured in serum as markers of the production of trype-I collagen. Elevated values of these propeptides are found in serum from patients with various metabolic or malignant bone diseases. Procollagen type I C-terminal propeptide (PICP) has a molecular mass of approximately 100 kDa.

Collagen type I is present in soft connective tissue and bone where it represents approximately 90% of the organic matrix. Collagen type I is produced from procollagen when two teloterminal propeptides are digested from the precursor and released into the circulation. The propeptide levels can be measured in serum as indicators of collagen production. Elevated values of these propeptides in serum are found in patients with various bone metabolism defects.

D-dimer is a fibrin degradation product present in the blood after a blood clot is degraded by fibrinolysis. D-dimer containd two crosslinked D fragments of fibrinogen. Determination of D-dimer concentration in blood is an important test for patients suspected of thrombotic disorders. Cat. No. 250227 binds human D-dimer, cross-reacts (<2%) with D-monomer directly coated on plate but does not react with directly coated fibrinogen.

The complement component C3 plays a central role in the activation of the complement system. C3 activation by the C3 convertase is the central reaction in both classical and alternative complement pathways. Cleaved C3 produces C3a anaphylatoxin, a mediator of local inflammatory process, and C3b, which binds to cell surface carbohydrates and immune aggregates. Genetic variation in C3 is associated with susceptibility to age-related macular degeneration 9 (ARMD9). This antibody recognizes the human complement C3 in ELISA.

Endostatin is a 20 kDa C-terminal peptide fragment derived from collagen XVIII. Endostatin is an angiogenesis inhibitor that can cause nearly complete suppression of tumor-induced angiogenesis and strong antitumor activity by preventing the endothelial cells to migrate. Endostatin competes with fibronectin at RGD binding sites on the receptor alpha-5 beta-1 integrin. This antibody recognizes human endostatin in ELISA.