Recombinant Proteins
Recombinant Proteins — Active Enzymes for Proteinase Research
Triple Point Biologics' recombinant protein catalog comprises 308 active recombinant enzymes spanning ten proteinase and inhibitor families, each expressed in HEK293 cells for authentic post-translational processing and matched to a rabbit polyclonal antibody produced in the same…
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The TPB Recombinant Catalog at a Glance
Triple Point Biologics has specialized in proteinase and inhibitor research reagents since 1994. The recombinant protein catalog reflects that focus: every entry is a proteinase, proteinase inhibitor, or closely related regulatory protein — no fillers, no unrelated cytokines included simply to round out a general catalog. Researchers who need a recombinant proteinase can browse 308 characterized proteins across the following families:
- Matrix metalloproteinases (MMPs) — full-length and catalytic-domain constructs
- A disintegrin and metalloproteinases (ADAMs and ADAMTSs)
- Cysteine cathepsins (cathepsin B, C, D, K, L, S, V, X, and related)
- Serine proteases — kallikreins (KLK1–KLK15 and select tissue kallikreins)
- Granzymes A, B, H, K, and M
- Caspases (initiator and effector)
- Aspartyl proteases (BACE1, BACE2, pepsin, renin)
- Thrombins, plasminogen activators, and coagulation serine proteases
- Serpins and endogenous inhibitors (TIMP-1 through TIMP-4, α2-macroglobulin, cystatins)
- Furin and proprotein convertases
Browse the full catalog by family using the links in the Browse by Class section below, or go directly to a collection: Recombinant Metalloproteinases, Recombinant Cathepsins, Recombinant Kallikreins.
What Distinguishes TPB Recombinant Proteins
Several aspects of the production and QC pipeline are worth understanding before placing an order, because they affect how the protein behaves in downstream assays.
HEK293 Expression for Native-Like Glycosylation
All 308 recombinant proteins in this catalog are expressed in human HEK293 cells. For proteinases, expression host matters: many MMPs, ADAMs, and cathepsins carry N-linked glycans that influence folding, zymogen activation, and substrate access. Bacterial expression (E. coli) yields non-glycosylated protein that frequently requires refolding steps and can show altered kinetics compared to native enzyme. Baculovirus/insect-cell expression produces core glycans but not fully processed complex glycans. HEK293 expression provides human-type complex glycosylation without the refolding artifacts, which is why it is the preferred host for proteinase activity assays where kinetic fidelity matters.
Activity Validation on Every Lot
Each lot is tested for proteolytic activity before release using a fluorogenic substrate appropriate to the enzyme class — for example, Mca-PLGL-Dpa-AR-NH₂ for MMP activity or Z-FR-AMC for cathepsin B/L. The specific substrate, assay conditions (buffer, pH, activator where required), and measured specific activity are documented on the per-lot Certificate of Analysis (CoA). Lot-specific CoAs are available on each product page and on request; see Quality and Validation for the full testing matrix.
Purity is assessed by reducing SDS-PAGE with Coomassie staining, and endotoxin is measured by LAL assay. Proteins intended for cell-based assays carry an endotoxin specification of ≤1.0 EU/µg.
Matched Rabbit Polyclonal Antibody for Every Target
The defining feature of the TPB catalog is the matched-pair architecture: for each of the 308 recombinant proteins there is a corresponding rabbit polyclonal antibody raised against a recombinant fragment of the same target, produced in-house at the same facility. This is not incidental — it reflects a deliberate catalog design that has been maintained since the first product lines launched in 1994. The scientific rationale is addressed separately in the Matched-Pair Narrative section below.
Browse Recombinant Proteins by Class
The ten collection pages below each contain class-specific background, a full sortable table of available proteins, and direct links to individual product pages where you can download datasheets and lot-specific CoAs.
| Protein Class | Catalog Entries | Representative Targets | Collection Link |
|---|---|---|---|
| Matrix metalloproteinases | MMP-1 through MMP-28 (select isoforms) | MMP-2, MMP-9, MMP-14 (MT1-MMP) | Browse MMPs |
| ADAMs / ADAMTSs | ADAM10, 12, 17 (TACE), ADAMTS4, ADAMTS5 | ADAM17, ADAMTS5 | Browse ADAMs |
| Cysteine cathepsins | Cathepsins B, C, D, K, L, S, V, X | Cathepsin K, cathepsin S | Browse Cathepsins |
| Kallikreins | KLK1–KLK15 and tissue kallikreins | KLK3 (PSA), KLK5, KLK7 | Browse Kallikreins |
| Granzymes | Granzymes A, B, H, K, M | Granzyme B, Granzyme A | Browse Granzymes |
| Caspases | Caspases 1, 2, 3, 6, 7, 8, 9, 10 | Caspase-3, Caspase-8 | Browse Caspases |
| Aspartyl proteases | BACE1, BACE2, renin, pepsin | BACE1, renin | Browse Aspartyl Proteases |
| Coagulation / fibrinolysis serine proteases | Thrombin, uPA, tPA, plasmin, Factor Xa | Thrombin, uPA | Browse Coagulation Proteases |
| Serpins and TIMPs | TIMP-1–4, α2-macroglobulin, cystatins, PAI-1 | TIMP-2, PAI-1, cystatin C | Browse Inhibitors |
| Proprotein convertases | Furin, PCSK9, PC5/6 | Furin, PCSK9 | Browse Convertases |
Common Applications
The following applications account for the majority of how researchers use recombinant proteinases sourced from this catalog. Each section notes format preferences and relevant controls.
Fluorogenic Activity Assays and Enzyme Kinetics
Fluorogenic peptide substrates (AMC- or MCA/Dpa-based) remain the standard method for measuring proteinase activity and determining Km, Vmax, and kcat/Km values. Because lot-specific activity data are included in every CoA, researchers can normalize enzyme input by specific activity rather than total protein mass, improving replicate consistency across experiments. Recombinant enzymes supplied as zymogens (e.g., most MMPs) include guidance on activation protocols — typically APMA treatment or furin pre-cleavage depending on the construct.
Inhibitor Screening and IC₅₀ Determination
Recombinant enzymes in defined-activity lots are suitable for compound library screening in 96- or 384-well fluorescence plate formats. The activity-validated, endotoxin-tested specification ensures that apparent inhibition is not confounded by variable enzyme input or endotoxin-mediated assay interference. For researchers building selectivity panels across multiple proteinase classes, the catalog depth across MMP, cathepsin, kallikrein, and granzyme families allows parallel screening without switching suppliers — a practical advantage when comparing inhibitor selectivity across structurally related enzymes.
Antibody Validation and Immunoassay Development
Recombinant proteins serve as positive controls and standard-curve antigens for ELISA, Western blot, and immunohistochemistry validation. When the recombinant and the detection antibody come from the same production lab — as is the case with every TPB matched pair — the immunogen sequence is fully traceable to the recombinant fragment used in the activity catalog. This traceability is directly useful when troubleshooting cross-reactivity: if the antibody does not recognize the recombinant on a Western blot, the problem is isolatable to either the detection conditions or the antibody lot, not to sequence mismatch between immunogen and test antigen.
Substrate Cleavage and Peptide Mapping
Identifying physiological or synthetic substrates often requires incubation of candidate peptides or proteins with purified recombinant enzyme followed by mass spectrometry or gel-based analysis. HEK293-expressed recombinants are appropriate for this application because their glycosylation state is closer to the native enzyme, reducing the risk of artifactual cleavage patterns caused by misfolded non-glycosylated protein.
Structural Biology and Biophysical Studies
Select catalog entries are available in larger quantities (≥500 µg) suitable for crystallography, cryo-EM, or surface plasmon resonance. Contact the technical team via the Custom Services page to discuss scale-up requirements for structural work, including tag removal and buffer exchange options.
How to Choose a Recombinant Protein for Your Experiment
Selecting between a full-length construct and a catalytic-domain-only variant, between an active enzyme and a zymogen, or between species orthologs depends on the specific assay format and biological question. The guide Introduction to Recombinant Proteins for Proteinase Research walks through these decisions systematically, covering:
- Construct design considerations — full-length vs. truncated, tagged vs. untagged
- Activation requirements for zymogen-form enzymes
- Buffer and storage conditions that affect enzyme stability
- Species ortholog selection for mouse, rat, and human comparisons
- How to use lot-specific specific-activity data to normalize enzyme input
Individual product pages link directly to the matching antibody (e.g., Anti-MMP-9 Rabbit Polyclonal Antibody from the Recombinant MMP-9 Protein page), making it straightforward to order both reagents in a single transaction and confirm that the antibody immunogen corresponds to the recombinant construct in use.
Custom Recombinant Protein Production
When a required proteinase or inhibitor is not in the standard catalog — for instance, a rare KLK isoform, a point mutant for structure-function studies, or a species ortholog not yet in the collection — the custom production service can produce it to the same HEK293-expression, activity-validated standard as catalog items. Custom projects also include the option of a matched polyclonal antibody raised against the same recombinant fragment, maintaining the paired architecture that characterizes the standard catalog.
Typical deliverables for a custom recombinant project include confirmed sequence, expression and purification report, SDS-PAGE, activity assay data where applicable, and a final CoA. Lead times and minimum quantities depend on the complexity of the construct. Details and a project inquiry form are available on the Custom Services page.
The Matched-Pair Principle: Why One-Lab Sourcing Matters
Most research workflows that characterize a proteinase involve at least two reagent types: the recombinant enzyme (or a cell lysate containing the target) and an antibody used to detect, quantify, or localize that enzyme. When those two reagents come from different suppliers, the immunogen sequence used to raise the antibody is often unknown or only partially described, and the recombinant's expressed sequence may differ from the antibody's epitope region — particularly if the antibody was raised against a bacterial fusion protein and the recombinant is a glycosylated HEK293 product.
At Triple Point Biologics, the antibody and recombinant for a given target are produced from the same construct. The rabbit polyclonal is raised against a recombinant fragment that is a defined segment of the same full-length sequence expressed in the activity catalog — for example, a polyclonal raised against residues 46–460 of the pro-mature MMP-2 sequence, where the matched recombinant expresses the same domain boundaries. The practical consequence is that the recombinant serves as a reliable positive control for the antibody, and the antibody can confirm the identity and integrity of the recombinant preparation.
This architecture also simplifies publication documentation: both reagents carry the same internal lot traceability, the same QC standards, and originate from a single specialist source with an uninterrupted production history dating to 1994. For details on the QC testing applied to both recombinants and antibodies, see Quality and Validation. For background on the laboratory and its history in proteinase research, see About Triple Point Biologics.