Downstream process development.

Configure and run DSP protocols in Seal, from load preparation to pooling and filtration. Connect execution records with ÄKTA runs and assays. Use neil to help configure the work, investigate recovery and plan the next study.

Configure your purification workflow
Illustration of a seal studying collected fractions beside a chromatography column, with a red peak below.

Run the purification protocol in Seal.

Configure load preparation, collection, pooling and filtration records. Keep quantities, calculations and sample identity with the execution, while ÄKTA and other instruments retain their acquisition data.

Reusable protocolv02

Chromatography study

  1. Identify the load, resin and method
  2. Record fractions and link their assays
  3. Assess the pool before recording pooling
Execution recordv02

DSP-019

Protein loaded
2,000 mg
Fractions collected
F01–F08
Pooling decision
Not recorded

Pool assessment pending

Collection recorded · Pool not approved. Fictional record.

Configure with neil. Test with your team. Reuse the protocol.
Each run keeps its own values, evidence and history.

See protocols in Seal

From the peak to the pooling decision.

Follow the collected fractions into their analytical results.

CHR-014 / elution

Illustrative UV trace and selected collection windowSynthetic elution trace from 0 to 160 mL. Eight equal 20 mL fractions. Selected F02 to F07. Protein recovery is calculated from separate fraction assays, not this trace.UV 280 nm / mAU8000F01F02F03F04F05F06F07F080Elution volume160 mL
F02–F07 selectedIllustrative trace
What changes if we widen the pool?
neil

82% recovered

1,640 mg in 120 mL

The wider pool adds 240 mg. It also brings in F02 and F07, which have higher host-cell protein results.

Test the candidate pool before choosing.

CHR-014 / pooling assessment

Fictional development records · Draft v01

Question: compare F03–F06 with F02–F07 before choosing a development pool.

Recovery comparison

Core pool / F03–F06

1,400 mg · 80 mL · 70% recovery

Wider pool / F02–F07

1,640 mg · 120 mL · 82% recovery

The wider option gains 240 mg, or 12 percentage points of recovery on the loaded-mass basis.

What comes with the extra recovery?

F02 and F07 report HCP at 70 and 95 ng/mg protein. The core fractions range from 9 to 22 ng/mg. No acceptance criterion is supplied. These individual results are not a measured result for either pool.

Proposed next study

  1. Downstream scientist: prepare representative candidate pools at the intended fraction proportions; record aliquots, actual volumes and sample handling.
  2. Analytical scientist: measure pooled protein and HCP, plus the quality attributes required by the study. Verify method suitability and any dilution or matrix effects.
  3. Process lead: compare the measured pool profiles, recovery and suitability for the next step against pre-agreed requirements. Record which option proceeds and why.

Decision remains open

This draft does not select or approve a production pool, establish impurity clearance or prove scale equivalence. The next study and the pooling decision require scientific review.

Sources: CHR-014 fraction records F01–F08, DSP-M07 v03, PROT-02 v04 and HCP-05 v02. Fixed example data; no live query or instrument command.

Develop the whole purification train.

Start with one decision. Keep the process knowledge as studies, methods and scale change.

Chromatography

Compare load, method version, column history and fraction results. Keep a pooling decision connected to the run that produced it.

What stays connected

Retain resin lot, column geometry, packing and cycle history, buffers, actual flow and pressure, collection events and sample methods. A proposed change to a collection rule remains a draft until the team reviews and tests it.

Filtration & concentration

Follow the material through membranes, concentration and buffer exchange. Compare recovery using the same calculation basis.

What stays connected

Connect membrane identity and area, feed and retentate quantities, permeate, process conditions, sample withdrawals and hold-up estimates. Keep measured losses separate from assumptions; do not equate a single step’s recovery with overall process yield.

Intermediate pools & holds

Know what entered each pool, where it went and which results support its next use.

What stays connected

Carry parent fractions, actual quantities, containers, transfers, storage and hold intervals into the pool record. Record sampling losses and the measured pool composition. Quality and downstream suitability require their own assessment.

Scale-up & transfer

Carry the chosen process forward with its limits, assumptions and development evidence.

What stays connected

Ask neil to compare receiving equipment, loading, residence time, flow, pressure and hold assumptions. Prepare a transfer work plan with the evidence needed to resolve differences. A matching setting does not prove scale equivalence.

Use the records your team already has.

Start with ÄKTA / UNICORN exports, your lab results and study records. Agree the files or permitted connection; keep the original run and method with the analysis.

Explore connections
Buffer preparationFormulation, preparation checks and the lots used in each runÄKTA / UNICORNRun, method, fraction collection and eventsAnalytical systems & LIMSFraction identity, method, units and reviewTransfer definitionChosen process, local differences and evidence

Questions from downstream teams.

Yes. Configure reusable protocols with instructions, fields, calculations, linked samples and review steps. Each execution retains the version used, recorded values, observations and results. neil can help prepare the configuration and analyse the resulting evidence; your team tests the workflow and defines the review and approval requirements for its intended use.
It sums recorded protein mass and volume for the selected fractions. Recovery is selected protein mass divided by the 2,000 mg loaded to this step. Core F03–F06 contains 1,400 mg in 80 mL (70%); wider F02–F07 contains 1,640 mg in 120 mL (82%). These are fictional development records, not live instrument results.
That is not established. The added fractions have HCP results of 70 and 95 ng/mg protein; core fractions range from 9 to 22. No acceptance criterion is supplied, and the example does not calculate or approve pooled quality. Prepare and test a candidate pool against the study’s requirements before making the pooling decision.
The run view is a synthetic UV trace illustrating eight 20 mL collection intervals, not an actual ÄKTA capture. Switch to fraction assays to see the fictional protein masses used for recovery. The calculation does not infer protein mass or impurity clearance from UV peak area. Actual chromatograms, method versions and instrument events can be linked to fraction records in a configured workflow.
Yes. Agree which method versions, instrument files, fractions, sample results and material records to connect or supply. Access depends on the source software, export or API and configured permissions. This page does not demonstrate a live instrument query or send commands to a chromatography system.
Connect capture and polishing studies with filtration, concentration, buffer exchange, intermediate holds and transfer work. Retain the material genealogy and calculation basis at each step. Scale-up, quality, clearance and process suitability need their own evidence rather than being inferred from recovery.
Ask for a run comparison, pooling assessment, mass-balance reconciliation, proposed study or transfer work plan. The output should retain source versions, calculations, missing evidence and open decisions. Your scientists review the interpretation and decide which process to take forward.

Put your purification protocol to work.

Bring a protocol and a representative study. Configure the steps, calculations and records, test the workflow with your team, then use neil to learn from the results.

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