Drug substance testing is an integral component in the manufacturing strategy for a biologic drug. Industry standard biologics (monoclonal antibodies [mAbs]) have, by now, well integrated drug substance testing-based control strategies to ensure that process parameters fall in-line and for the sake of product quality. However, the emergence of newer and more complex biologic modalities (e.g., cell therapies, gene therapies, protein fragments, and other constructs) challenges well-used testing methods.

The question is whether standard analytical methods for biologic drug substance testing can meet the requirements for quality assessment of these newer modalities. And if not, what innovations or adaptations are needed to address these analytical needs?

According to FDA’s industry guidance for mAb production, the antibody structure, integrity, specificity, and potency of a potential mAb therapeutic must first be precisely and thoroughly characterized before human studies can be conducted (1).

To characterize the structural integrity of the mAb, analytical methods such as sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), isoelectric focusing (IEF), high-performance liquid chromatography (HPLC), and mass spectrometry (MS) should be used, or other appropriate physicochemical methods, to show that the mAb, once purified, has not been fragmented, has not aggregated, or has otherwise not been modified as a result of the separation and purification process. FDA guidance also recommends that side-by-side comparisons should be conducted between each production lot and the in-house reference standard.

To test for the specificity of the mAb, direct binding assays should be used. The assays should show that the mAb binds to the specific target antigen for which it is intended (both positive and negative controls should be included here). FDA’s guidance also explains that “the protein, glycoprotein, glycolipid, or other molecule bearing the reactive epitope” must be biochemically defined. The antigenic epitope must also be determined. Fine specificity studies using inhibition or other techniques should also be conducted, when possible, to characterize the antibody specificity. Once antibody specificity is determined, antibody binding activity must then be quantified through affinity, avidity, or immunoreactivity assays, or combinations of these assays.

Potency assays are also important for characterizing the mAb product, monitoring consistency from lot to lot, and ensuring product stability. FDA’s guidance suggests using binding assays, serological assays, 

 functional assays, or animal model activity, to assess potency. A purified unmodified mAb must be fully characterized before it can enter human studies, with the mAb’s structural integrity, specificity, and potency described in the product’s investigational new drug (IND) filing (1).

With the evolution of biotherapeutic modalities from the traditional mAb format, however, drug substance analytical testing needs improved sensitivity. In addition, analytical methods used for small-molecule (i.e., chemical) drugs—such as solid phase extraction, gas chromatography, liquid chromatography, and/or mass spectrometry—are not the best suited for biologic drugs. For small-molecule drugs, these analytic methods remove biological matrix elements from the sample solution, leaving the chemical drug behind for subsequent analysis. Used for biologic drug analysis, however, the methods would remove the biologic drug itself from the sample solution. Testing of biologic drug sample for preclinical and clinical specimens would require specific binding techniques, such as immunological methods that quantify a desired biological target in the presence of a biological matrix (2).

There have been emerging analytical technologies, however, that allow for more sensitive scrutiny and more specific physiochemical detail. In the early development stages, more in-depth, orthogonal biochemical information can be gained from a target molecule to provide better understanding of its attributes. Having this in-depth information also allows for the

assessment of intrinsic product- or process-related impurities that could impact product safety in early clinical trials. The analysis of biological (i.e., protein) drugs can be done through methods such as HPLC, ultra-high performance liquid chromatography (UHPLC), gel electrophoresis, isoelectric focusing, gene sequencing, various other forms of mass spectrometry, amino acid analysis, carbohydrate analysis, peptide mapping, and capillary electrophoresis, among others (2).

Building test methods for measuring drug substance performance and quality of a new biologic modality can be guided by the appropriate regulatory authority, but harmonized standards can be most helpful, as these standards reflect a consensus of best practices among the major global regulatory authorities. The International Council for Harmonization of Technical Requirements for Pharmaceuticals for Human Use (ICH) provides such a set of standards.

ICH Q6 (3) is especially useful as it gives guidance on establishing specifications for drug substance testing for new chemical entities (as well as drug product testing). Recommended test and acceptance criteria guidelines follow a particular format:

Description—gives a qualitative statement describing the state (e.g., solid, liquid) and color of a new drug substance, and should any of these characteristics change while in storage, the change should be investigated and dealt with.

Identification—ideally, this testing should allow for discrimination between compounds of closely related structures that are likely to be present, and identification testing should be specific to the new drug substance. Use of two chromatographic procedures, in which separation is based on different principles or a combination of tests are used in a single procedure, is acceptable.

Assay—this requires that a specific, stability-indicating procedure be included to determine the content of a new drug substance.

Impurities—this category includes both organic and inorganic impurities and residual solvents.

Additional testing recommended for new biologic modalities can include the following, where appropriate (3):

Physicochemical properties—these properties include pH of an aqueous solution, melting point/melting range, and refractive index, and their measurements can be taken using methods such as capillary melting point and Abbé refractometry. Testing of physicochemical properties should be determined by the physical nature of the new drug substance and its intended use.

Water content—testing for water content is important when the new drug substance is known to be hygroscopic or degraded by moisture, or when it is knows that the drug substance is a stoichiometric hydrate.

Inorganic impurities—it is important to include tests and acceptance criteria for inorganic impurities (e.g., catalysts) during development, and the inclusion of such tests should be based on knowledge of the manufacturing process.

Microbial limits—it is possible that there may be a need to specify the total count of organisms (i.e., aerobic microorganisms, yeasts, molds, etc.) and the absence of specific objectionable bacteria (e.g., 

)—to be determined using pharmacopeial procedures. The type of microbial testing used and acceptance criteria for microbial limits should be based on several factors: the nature of the drug substance, the method of manufacture, and the intended use of the drug product.

Thus, establishing appropriate testing methods and acceptance criteria will help illuminate where the need is greatest for more specific and/or more sensitively tuned analytical methods.

Guidance for Industry, Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use

 (Rockville, MD, February 1997).
2. H. Shintani, “Development of Test Method for Pharmaceutical and BioPharmaceutical Products,” 

Specifications: Test Procedures and Acceptance Criteria for New Drug Substances And New Drug Products: Chemical Substances

Feliza Mirasol is the science editor for 


Vol. 45, No. 1
January 2021
Pages: 44–45

When referring to this article, please cite it as F. Mirasol, “Meeting Specificity Needs for Biologic Drug Substance Testing,” 

Articles

Features

Traditional biologic-based testing methods may need an upgrade to properly test newer therapeutic modalities.

Meeting Specific Requirements for Biologic Drug Substance Testing

Functional characterization of protein therapeutics is an expectation of regulatory agencies. The critical quality attributes (CQAs) that impact function and efficacy of the protein therapeutic should therefore be identified and characterized for a regulatory submission. Throughout the development process, notes Khanh Ngo Courtney, director of biologics for Avomeen, bioanalytical testing must be dynamic and tailored to both the protein and the manufacturing approach. “Given the speed of enzyme and protein therapy R&D, rapidly assessing biomolecule efficacy (or potency) and determining an accurate list of CQAs are key,” she states.

Before any biologic drug enters into the clinic, it is essential to have a clear understanding of what exactly the biomolecule entails, according to Vu Truong, CEO of Aridis Pharmaceuticals. That includes both structural and physicochemical characteristics.

General structural features that must be described for a protein therapeutic include the primary amino acid sequence, amino acid composition, and any available secondary and tertiary structures, Courtney notes. Peptide mapping can be used to determine the amino acid composition, protein sequence—including N- and C-termini status—post-translational modifications (PTMs), disulfide bridges, and sulfhydryl status, for instance, although additional methods are often needed to fully characterize all these structural elements, according to Andrew Hanneman, scientific advisor for biologics testing at Charles River Laboratories.

The molecular weight profile, isoform distribution patterns, and molar absorptivity are other physicochemical properties that must be determined to support clinical studies and product release.

The specific part of the biomolecule that mediates activity should be identified as well, adds Truong. Stability profile assays must also be conducted to demonstrate under what conditions that activity is preserved and lost due to fragmentation/cleavage, unfolding, and 

 immune responses, he says. Information on impurities and the acceptable levels at which they do not adversely impact activity and safety must also be developed.

It must be kept in mind, though, Courtney stresses, that structural and physicochemical properties vary depending on the CQAs for efficacy of each drug substance. For instance, if the drug requires higher-ordered structures, such as oligomerization or other protein binding partners, for activity, showing evidence of quaternary structure might be expected. If certain PTMs are required for a protein to be internalized, such as glycosylation, then elucidation of the glycan structure important for such activity might be helpful in a filing.

There may also be varied requirements for different regulatory authorities, observes Hanneman. “Although drug development processes and submissions are increasingly harmonized among the major markets, there are some differences that need to be understood early in drug development. The characterization methods needed are developed and conducted or validated with knowledge of market-specific guidance and the expected level of oversight and data review,” he says.

A wide variety of analytical methods are needed to fully characterize therapeutic proteins. “Physiochemical properties are investigated via structural characterization and confirmation studies described in the International Council for Harmonization (ICH) Q6B Guidance (1) initiated in collaboration between FDA, the European Medicines Agency (EMA), and the Japan Pharmaceutical Manufacturers Association (JPMA),” states Hanneman.

In addition to peptide mapping, electrophoresis, high-performance liquid chromatography (HPLC), size-exclusion chromatography, and various forms of spectroscopy (e.g., Fourier transform infrared) are widely used. “The more methods that are employed, especially if they are truly orthogonal, the greater confidence the drug developer and regulators have in the nature and quality of the protein therapeutic,” Truong says. He also notes that by performing a very comprehensive set of analyses, companies set a standard that developers of biosimilars will have to meet, which raises the hurdles.

More recently, nucleic acid sequencing technologies, X-ray crystallography, cryomicroscopy, and mass spectrometry (MS) have attracted increasing attention. MS, says Hanneman, has proven highly flexible in biopharma applications because the soft ionization methods used to ionize large molecules provide a significant opportunity to manipulate large biomolecules like proteins, leading to direct and unambiguous readout of primary and, increasingly, higher order structural elements.

Protein MS, either intact or bottom-up, is commonly used in the characterization of protein therapeutics because it is a single method capable of characterizing many attributes at a time, according to Courtney. “Using high sensitivity instrumentation such as the Orbitrap, one can elucidate batch-to-batch primary sequence consistency, post-translational modifications, such as phosphorylation or glycosylation, and also damages to the protein upon stressed treatment, such as deamidation or oxidation,” she explains. A quadrupole time-of-flight (QTOF) MS system would be useful for verifying accurate intact mass of the biomolecule for use as an identity test, Courtney adds.

Quantitative peptide mapping conducted as a multi-attribute method (MAM), Hanneman agrees, holds significant promise to displace a variety of redundant HPLC and/or electrophoretic methodologies to speed up protein drug development.

Bottom up mass spectrometry is not new, but different ways to use this powerful tool are more frequently employed, Courtney says.

“MS continues to see increased applications, with newer and streamlined approaches used to manipulate large gas-phase ions. MS offers the significant advantage of precise mass measurement (ppm mass accuracy) as its output,” Hanneman agrees. He points to ion mobility and charge detection MS as two innovative methods.

Some aspects of therapeutic protein characterization still create challenges today. Truong points to demonstration of glycoform consistency and how changes in glycoform profiles can impact safety, efficacy, and immunogenicity as one area where improvements in speed and accuracy are needed.

Potency assays, such as an enzymatic activity assays and cell-based potency assays, also present difficulties, according to Courtney. She notes that both are necessary for characterization of potency and 

 cellular efficacy, but cells are intrinsically tricky “reagents” and can be difficult to control and troubleshoot, while, enzymatically, assays can be difficult to develop if the mechanism of the protein is not fully understood.

“These issues lead to higher variability for enzymatic and cellular potency assays than chromatographic methodologies,” Courtney says. The challenge, she adds, is to design such methods so they are fit-for-purpose. “Often these assays are over-designed, resulting in added complexity that leads to increased variability or being under-designed, and, thus, lack sufficient specificity. Achieving the right balance is challenging and the most difficult part of the process,” she explains.

The time it takes to complete cell-based assays is also an issue, according to Truong, but advances in nucleic-acid based methods (next-generation sequencing technologies) should ultimately overcome this difficulty. Similarly, the need to demonstrate genetic (cell-line) stability through numerous passages takes significant time.

Advances in analytical technologies are helping to increase the understanding of protein structure and function at the molecular level, providing greater insight into how proteins actually bind to targets and their detailed modes of action. “Elucidating structural and physicochemical properties of proteins and relating them to biologic activity is increasingly possible and at an ever-increasing pace,” Truong asserts.

Courtney refers again to MS as a powerful tool not only for understanding the molecular characteristics of proteins, but also as a read-out method for bioactivity and cellular potency. “If a protein therapeutic can elicit a cellular response, then perhaps a representative biomarker resulting from that response could be monitored by MS using selective ion monitoring or multiple-reaction monitoring,” she observes.

Significant effort has also been underway to use “native mass spectrometry” for direct MS measurement of proteins in their native conformation, including complexes of increasingly higher molecular weight. Improved separation modes allow for direct analysis of native proteins, including charge variant species, according to Hanneman.

There are hurdles to using MS for potency and routine testing, however, including the need for specialized equipment and personnel not usually found in a quality control (QC) laboratory. “I look forward to seeing how mass spectrometers can be simplified as bench-top instruments that aren’t so intimidating for routine use and could be run by non-specialized personnel,” Courtney comments.

Hanneman notes that instrument companies and software developers continue to work closely to provide advanced “push-button” MS data applications under 

 Part 11) (2)-compliant electronic data platforms for routine use in QC labs. For instance, MS tool kits include improved workflows and streamlined data analysis approaches for profiling and quantifying impurities, including host-cell proteins (HCP) and other process impurities, which will continue to grow in their implementation.

New formats and improved techniques for conducting 

 bioassays are also evolving, including new labeling and imaging approaches, such as innovative time-resolved fluorescence methods and reagents, Hanneman observes. “These tools for measuring target binding typically offer increased signal-to-noise ratio resulting in higher sensitivity and greater confidence in demonstrating specificity,” he says.

New and improved methodologies for aggregate and particle separation, including field flow fractionation (FFF), as well as instruments providing high-definition particle imaging and detection will see increased application, according to Hanneman. These new tools and approaches for detecting and measuring sub-visible particles and determining the size of protein aggregates (as well as viral particles) are undergoing innovation and developments to improve rate of throughput.

Regardless of what characterization methods are selected, they are targeted and tuned toward uncovering and reliably measuring drug product CQAs because they ultimately impact protein bioactivity 

 and safety, including potential immune reactions. The methods chosen, therefore, should provide overlapping and correlative information without “knowledge gaps”, Hanneman asserts.

“Comprehensive protein structure determination ranging from primary to tertiary/quaternary elements currently requires a wide variety of complementary techniques (some truly ‘orthogonal’), and each may fill a different piece of an overall large puzzle. The overlapping data sets then need to be synthesized into an overall description, which can be a complex process for large, heterogeneous, or multimeric protein drugs,” says Hanneman.

Truly comprehensive structural determination remains an elusive goal, however, according to Hanneman, due to protein higher order conformation as well as proteoform heterogeneity within a given sample. “[On a positive note], the development of computational bioinformatics tools and shared database resources go a long way toward simplifying the processing, visualization, and sharing of large protein characterization and comparability data sets among collaborating stakeholders,” he observes.

The advantages and disadvantages of various methods and approaches should, in addition, be weighed in terms of the “intended use” of each analytical method and whether each method needs to be validated, according to Hanneman. “Information-rich characterization methods need to be developed and applied as early as possible in a drug development program and used to direct best use of effort, then continually refined (or re-defined) all the way through to drug commercialization,” he says.

Furthermore, with cell and gene therapy programs gaining ground in the biologic marketplace, Hanneman believes the intended use and implementation of protein characterization methods will see changes and refinements in response to the need to detect the presence of genetic material and potentially characterize oligonucleotides as well as to analyze increasingly smaller sample aliquots produced using new and varied manufacturing processes.

Underlying the need to select the right set of methods for each given protein therapeutic is the critical importance of having the right talent working on a project. “People with the right skillsets and experience are needed to design studies that can overcome the various analytical challenges faced with respect to protein characterization,” Courtney states. “The right team,” she says, “will include someone with a fundamental understanding of protein biochemistry, enzyme kinetics, and/or cell biology to enable development of the right model system and a person who is QC-centric to help edit the method to ensure that it is fit-for-purpose.”

The team should also leverage best practices and, wherever possible, a set of analytical methods that have been successfully demonstrated in prior filings, according to Truong. “Evaluation of optimal sets of assays used in past applications can be very informative when selecting assays for a new protein candidate that will afford the best specificity and speed,” he says.

Going forward, adds Hanneman, cloud-based computing and “paperless” corporate infrastructure will greatly improve drug development timelines by supporting faster clearer data sharing. “These developments take significant time and resources to implement but once in place are highly advantageous,” he says.

Specifications: Test Procedures and Acceptance Criteria for Biotechnological/Biological Products

 Title 21, 11 (Government Printing Office, Washington, DC) pp. 110–114.

Cynthia A. Challener, PhD, is a contributing editor to 


Vol. 34, No. 1
January 2021
Pages: 34–37

When referring to this article, please cite is as C. Challener, “Using Protein Characterization to Support Regulatory Submissions,” 

Having a clear and detailed understanding of exactly what a biomolecule entails is essential for therapeutics development.

Protein Characterization Can Support Regulatory Submission

SPT Labtech, an automated instrumentation and consumables designer and developer, has acquired Apricot Designs, a US-based laboratory equipment supplier, in the latter half of January 2021.

Through the acquisition, SPT will have the ability to expand its portfolio of liquid handling technologies as part of its larger portfolio of automation solutions for drug discovery, structural biology, genomics, cryo-electron microscopy, sample management, and biobanking, SPT said in a Jan. 21, 2021 company press release. The agreement will also increase SPT’s global footprint through Apricot’s US and Asia locations.

"We are delighted to welcome Apricot Designs to the SPT Labtech group,” said Patrick Bennett, group CEO at SPT Labtech, in the press release. “The company's liquid handling technology products seamlessly complement our existing portfolio of high-performance positive displacement instruments. The addition reflects our continued commitment to accelerating scientific research by maximizing our customers' productivity. The powerful combination of technologies and application know-how will enable us to streamline end-to-end workflows and serve a wider range of research applications."

"We are delighted to join SPT Labtech, a company with an impressive reputation for creating innovative, automated solutions for life sciences,” added Felix H. Yiu, CEO of Apricot Designs, in the press release. “We are confident that customers will benefit from the partnership's combined product capabilities, industry-leading applications and technical support, and enhanced infrastructure."

News

Through the acquisition, SPT will have the ability to expand its portfolio of liquid handling technologies as part of its larger portfolio of automation solutions for drug discovery, structural biology, genomics, cryo-EM, sample management, and biobanking. 

SPT Labtech’s Acquisition of Apricot Designs Expands Liquid Handling Technologies Portfolio

Leukocare, a German biotechnology company, announced on Jan. 11, 2021 that it has officially launched its development laboratories and offices in Milford, MA.

According to a company press release, the new US offices will give the company the ability to support its US-based customers on site while continuing to collaborate with its global team. The offices and laboratories are located on Rentschler Biopharma´s Milford premises, where the companies will continue to carry out their global strategic alliance that was established in 2017.

“I am delighted to announce the opening of Leukocare´s US site today,” said Michael Scholl, CEO at Leukocare, in the press release. “The company´s outstanding development over the last few years led to our desire of establishing a presence in the largest pharmaceuticals market worldwide. This strategic step enables us to be even closer to both our US and global customers and to better understand and serve their needs. Furthermore, the existing infrastructure of Rentschler in Milford—that we will partially make use of—allows us to start operations without any delay and, thus, makes Milford the perfect choice for our newly established US site. We therefore will continue to pursue our strategy of pushing boundaries of biopharmaceutical product development by combining innovative biostatistics, artificial intelligence, and vast formulation expertise with first-class analytics.”

The new US offices will give the company the ability to support its US-based customers on site while continuing to collaborate with its global team.

Leukocare Opens Development Laboratories and Offices in Massachusetts 

Nexelis, a portfolio company of Ampersand Capital Partners and a provider of advanced assay development and laboratory testing services, has signed an asset purchase agreement with GlaxoSmithKline (GSK) to acquire GSK’s good clinical laboratory practices (GCLP)-certified clinical bioanalytical laboratory located in Marburg, Germany.

The transaction is effective at the end of January 2021, Nexelis stated in a Jan. 20, 2021 press release. Nexelis intends to quickly expand the Marburg site, initiating collaborations with other vaccine development companies as well as with its other North American and European sites. The company expects to add new clinical testing platforms in Marburg that will be fully bridged with Laval platforms, develop synergies with its early development-stage ImmunXperts branch in Belgium, and leverage existing talents in fields such as biostatistics to form a broad-based, end-to-end service offering in bacteriology, virology, and oncology.

The clinical laboratory science team in Marburg, consisting of approximately 80 scientists and analysts, will be transferred to Nexelis and will continue to keep a strong relationship with GSK. The team will support the development of future GSK vaccine candidates through a five-year strategic collaborative agreement, Nexelis said in the press release.

“We are thrilled to welcome on board new colleagues with a legacy of over 20 years under Novartis and GSK leadership in clinical laboratory activities supporting the development of vaccines against viral and bacterial diseases. We believe that this transaction is a determining step in the establishment of Nexelis as an unrivaled global vaccine player,” said Nexelis CEO Benoit Bouche in the press release.

“Strategic outsourcing will optimize GSK’s footprint and increase our agility so that we can continue to accelerate the development of the candidate vaccines in our pipeline. Based on the previous successful transfer of other laboratory activities to Nexelis, we are confident that this will be a great fit due to the quality and agility of the Nexelis organization,” added Emmanuel Hanon, head of GSK Vaccines R&D, in the press release.

Nexelis’ recent acquisition of GSK’s Marburg, Germany-based vaccines clinical bioanalytical laboratory expands its bioanalytical capabilities.

Nexelis Expands Bioanalytical Services with Bioanalytical Lab Acquisition

Almac Sciences, a member of the Almac Group, has further expanded its biologics testing laboratory with a significant £500,000 (US$686,294)-investment in mass spectrometry equipment, the company said in a Jan. 26, 2021 press release.

The company invested in a Thermo Orbitrap liquid chromatography–mass spectrometry (LC–MS) instrument, which substantially increases the company’s capabilities in solving biologic analytical challenges. The instrument is capable of offering a complete analysis package to current good manufacturing practices (CGMP), including amino acid sequencing, peptide mapping, disulfide bridge analysis using MS and tandem MS (MS/MS), glycosylation analysis, identification of post-translational modifications (e.g., acetylation), phosphorylation, and biomarker discovery.

The new high-resolution mass spectrometer has been installed at Almac’s global headquarters in Northern Ireland and will support its biologics offering for the analysis of peptides, proteins, glycoproteins, and antibody products. The instrument adds to the existing industry support at the company’s new biologic testing laboratory in Athlone, Ireland, which was just announced three months earlier and which supports quality control release and characterization of biologics.

The additional service this new instrument offers will provide an extended range of MS services, including the quantitation of genotoxic impurities, structure elucidation, isotopic purity determinations, and high-resolution MS of both large and small molecules. The addition also further complements the range of analytical services offered by Almac’s global analytical testing facilities in the United Kingdom, Ireland, and North America.

“This new mass spectrometer reinforces Almac’s vision of delivering the best for our customers and substantially enhances the level and depth of services we provide,” said John Robson, vice-president Analytical Services, Almac Sciences, in the press release.

The £500,000 (US$686,294)-investment in mass spectrometry support will accelerate biologics development and approval.

Almac Invests in Expanding Global Biologics Testing Solutions

Contec announced on Jan. 19, 2020 that it has introduced ReFIBE sterile cleanroom wipes, sustainable polyester wipes made from recycled post-consumer plastic bottles.

According to a company press release, the plastic bottles are first chopped into flakes and cleaned, then the flakes are melted, filtered, and formed into chips, which are melted and made into yarn. Finally, the yarn is knitted into sterile and non-sterile 9” x 9” and 12” x 12” ReFIBE wipes.

Laser-cut with heat-sealed edges, ReFIBE are cleanroom laundered and made with 100% polyester, Contec said in the press release.

“ReFIBE has been such a fulfilling project to work on,” said Amy Russ, global project manager for the Cleanroom Division at Contec, in the press release. “We consider it our responsibility to offer clean, sustainable alternatives to our customers, and ReFIBE wipes are just the beginning. We are excited to develop more sustainable options for both existing Contec products and new innovations in the months and years to come.”

New Technology

ReFIBE sterile cleanroom wipes are sustainable polyester wipes made from recycled post-consumer plastic bottles.

Contec Launches Sustainable Cleanroom Wipes

Pall Laboratory’s AcroPrep high-volume 24-well filter plates, launched in late January 2021, allows for laboratories to work within a 24-well format from cell growth, harvest, and biomolecule isolation to final analysis while offering a high throughput, less work steps and sample losses, and reduced processing times.

Designed for biotechnology and pharmaceutical laboratories, the well filter plates process volumes up to 7 mL for simple plate-to-plate transfers and a time-saving, cost-cutting filtration platform. The plates feature a polypropylene construction which promotes low protein binding to minimize sample loss. Plates are available in several pore sizes, including Omega PES membrane in all molecular weight cut-offs, and a polyethylene/polypropylene membrane.

"Pall's introduction of the industry's broadest line of 24-well filter plates provides researchers with the ultimate convenience of a true one-stop resource for their filtration workflow needs," said Lori Euler, Pall's product manager, Molecular, in a Jan. 26, 2021 company press release. "The new plates permit seamless operations throughout 24-well plate manual and automated processes, creating higher efficiencies and greater productivity.”

Designed for biotechnology and pharmaceutical laboratories, the well filter plates process volumes up to 7 mL for simple plate-to-plate transfers and a time-saving, cost-cutting filtration platform.

Pharmaceutical Technology's In the Lab eNewsletter 02-03-2021