Our Products
Our high quality proteins are produced from bacteria, insect cells (Baculovirus expression system) or biological fluids. The focus is
on human proteins which are of medical interest either as targets
to detect novel therapeutic drugs or as standards and substrates
in diagnostic assays.
One group of target proteins are matrix metalloproteinases (MMP). These proteolytic enzymes participate in many physiological pro-
cesses by digesting extracellular matrix proteins.
Their excessive or inappropriate expression contributes to the pathogenesis of a number of diseases such as cancer, arthritis, cardiovascular and neurological disorders, lung diseases and kidney diseases. Out of 20 human matrix metallproteinases, 9 enzymes are produced in highly purified form.
A second family of target proteins are metalloproteinases ADAMTS (a disintegrin and metalloprotei-nase with throm-
bospondin motif). Seven different ADAMTS-type enzymes digest the proteoglycan aggrecan, a major component of articular cartilage. Accelerated hydrolysis of aggrecan is an early step of cartilage destruction in osteoarthritis and inhibitors of aggrecanases are searched for to prevent and retard the degradation process. Recombinant ADAMTS1, ADAMTS4 and ADAMTS5 are offered for inhibitor screens and as standards in immunological and enzymatic assays.
A third group are human HtrA (High temperature requirement) proteases. These enzymes combine a trypsin-like serine protease domain with at least one PDZ domain and additional protein domains. As a first member of the HtrA-family HtrA1 is expressed in insect cells. The recombinant enzyme is useful for elucidating the inhibitory function of HtrA1 on TGFß-signaling and the tumor-suppressive activity of HtrA1.
Recombinant enzymes are used to generate antibodies, inhibitors , substrates and to develop diagnostic assays.
References
Proteolytic processing causes extensive heterogeneity of tissue matrilin forms. Ehlen HW, Sengle G, Klatt AR, Talke A, Müller S, Paulsson M, Wagener R. J Biol Chem. 2009 Aug 7;284(32):21545-56. Epub 2009 Jun 16.
A quantitative assay for aggrecanase activity. Will H, Dettloff M, Bendzkô P, Sveshnikov P. J Biomol Tech. 2005 Dec;16(4):459-72.
Truncation of the amino-terminus of the recombinant aggrecan rAgg1mut leads to reduced cleavage at the aggrecanase site. Efficient aggrecanase catabolism may depend on multiple substrate interactions. Hörber C, Büttner FH, Kern C, Schmiedeknecht G, Bartnik E. Matrix Biol. 2000 Nov;19(6):533-43.