The inter-α-trypsin inhibitor (ITI, IαI) family, a typical and classical example for protein-glycosaminoglycan-protein (PGP) complexes, occurs constitutively in plasma at relatively high concentrations and is a result of alternate combinations of three kinds of heavy chains with a common light chain, the bikunin proteoglycan. Bikunin has two proteinase inhibitor domains and belongs to the Kunitz-type protease inhibitor family; it displays an inhibitory activity against trypsin, leukocyte elastase and plasmin. The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid and this binding promotes the stability of the extra-cellular matrix. The ITI protein family is suspected of playing a key role in the extra-cellular matrix biology.

Western Blot: 1:500~1,000; Immunohistochemistry: Paraffin-embedded sections;

Type: Primary
Antigen: ITI (inter-alpha-trypsin inhibitor)
Clonality: Monoclonal
Clone: 40B10
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG1 Kappa
Reactivity: Human