As part of our integrated Pharmaceutical Development & Manufacturing capabilities leading into Drug Substance Development, we provide end-to-end programs for complex blood protein factors. We translate well-characterized concepts into robust, compliant, and manufacturable drug-substance processes with phase-appropriate documentation and analytical packages tailored to coagulation biology.
Overview of Blood Factor Development
Blood factors are structurally intricate glycoproteins and serine proteases whose performance depends on sequence integrity, post-translational modifications, and controlled activation states. Development therefore, hinges on upstream expression control, orthogonal purification trains, and stability-minded formulations, all anchored by fit-for-purpose bioassays. We design processes that preserve native folding and domain architecture; manage labile disulfides and metal-binding motifs; and maintain glycan profiles within scientifically justified ranges. Our analytical strategy spans identity, purity, potency, and comparability, pairing chromatography and mass spectrometry with functional readouts (e.g., chromogenic activity, assembly/activation kinetics).
Our Services
We deliver four coordinated drug substance development service tracks—recombinant coagulation blood factor development, plasma-derived single blood factor development, plasma-derived complex blood factor development, and activated blood protease factor development—each ending with a scalable process, control strategy, and rigorous analytics.
We deliver coherent drug-substance development programs for blood factors—recombinant, plasma-derived single or complex, and activated proteases. Engage our team to convert complex protein concepts into scalable, well-controlled substance processes.
Frequently Asked Questions
Q1: What distinguishes development of activated proteases from zymogens?
Activated proteases require timed conversion, immediate capture, and formulations that suppress autolysis. We fix activation kinetics, quantify active-site concentration, and confirm stability with activity-retention curves under temperature, agitation, and freeze–thaw stress.
Q2: How is complex integrity verified for multi-component assemblies?
We combine SEC-MALS, native MS, and binding kinetics (BLI/SPR) with functional co-factor assays. Acceptance criteria cover subunit ratio, oligomeric state, and activity. In-process controls (conductivity, pH, residence time) maintain assembly fidelity during purification.
Q3: How do you design stability-indicating methods for these proteins?
We align chromatographic purity with biophysical and functional endpoints: RP/IEC/SEC for degradants and aggregates, DSC/DSF for conformational stability, DLS for size changes, and calibrated activity assays. Forced-degradation studies ensure each method tracks relevant failure modes.
Our products and services are for research use only.
