Triple Point Biologics' Other Enzymes antibody catalog covers specialty catalytic proteins outside the four classical proteinase families — serine, cysteine, aspartic, and metallo — including ADAM (a disintegrin and metalloprotease) family members, caspases, and structurally related enzymes implicated in proteinase-adjacent biology. ADAMs are type I transmembrane metalloproteases responsible for ectodomain shedding of growth factors, cytokines, and adhesion molecules, with individual family members (e.g., ADAM10, ADAM17/TACE) acting on discrete substrate sets regulated by protein–protein interaction domains distinct from the catalytic cleft. Caspases are cysteine-dependent aspartate-directed proteases organized into initiator (caspase-8, -9) and executioner (caspase-3, -6, -7) subclasses, with zymogen processing and active-site accessibility representing key measurable endpoints in apoptosis research. Together, these enzyme classes represent high-priority research targets in cell death signaling, inflammatory mediator release, and substrate-cleavage biology.

TPB has produced rabbit polyclonal antibodies against proteinases and their regulatory proteins since 1994. Antibodies in this collection are raised against recombinant protein immunogens spanning functional domains — prodomain, catalytic domain, or disintegrin/cysteine-rich regions — to maximize epitope specificity and reduce cross-reactivity within paralogous families. Each antibody is validated by Western blot and immunohistochemistry (IHC); select clones have also been characterized for immunofluorescence (IF) using endogenous expression controls. Species cross-reactivity is designated as validated or predicted based on sequence homology analysis and is documented per-product. Critically, every antibody target in this collection has a matched recombinant protein produced in the same laboratory, providing a structurally defined positive control for assay calibration. Matched recombinants are available through our recombinant protein catalog.

These antibodies are routinely used in ectodomain shedding assays to detect membrane-anchored versus soluble substrate forms, in caspase cleavage studies to resolve zymogen and processed species by molecular weight, and in protease inhibitor screening workflows where target occupancy or activity-state detection is required. For guidance on designing activity-based experiments, see our protease activity assay guide. Researchers using recombinant proteins as assay standards are referred to our recombinant protein positive controls guide. Full documentation of lot-to-lot consistency testing, immunogen sequences, and validation data is available on our quality and validation page.