Triple Point Biologics' Other Proteins recombinant catalog covers non-enzymatic proteins that serve as physiologically relevant substrates, structural scaffolds, and binding partners in proteinase research — including targets such as von Willebrand factor (vWF), myocilin, and hemicentin. These proteins do not themselves carry proteinase or inhibitor activity, but they occupy central roles in the extracellular matrix, cytoskeletal organization, and cell-surface signaling networks. Their susceptibility to specific proteinases makes them indispensable reference materials for defining cleavage site specificity, reaction kinetics, and proteolytic processing events characterized in published studies of vascular biology, glaucoma, and basement membrane remodeling.

Each recombinant protein in this collection is expressed in HEK293 cells to preserve mammalian post-translational modifications relevant to native protein behavior, and is produced alongside a matched rabbit polyclonal antibody raised in-house — the same approach Triple Point Biologics has applied to proteinase and inhibitor targets since 1994. The paired antibody is validated for Western blot and IHC, allowing researchers to detect both the intact substrate and proteolytic fragments within the same experimental system without switching between reagent sources. Predicted cross-reactivity to non-human orthologues is noted per target where sequence homology data support it.

Primary applications for proteins in this collection include substrate cleavage assays — where a defined recombinant substrate is incubated with a candidate proteinase to establish cleavage efficiency, site preference, or inhibitor sensitivity — as well as structural biology co-crystallization studies and matched-pair experiments pairing the substrate directly with a TPB recombinant proteinase. For guidance on experimental design, see the Triple Point Biologics Protease Activity Assays guide and the Recombinant Protein Positive Controls guide, which cover substrate titration, buffer selection, and appropriate positive control configurations for these formats.