Rwanda – Africa’s Next Biotech Hub – Welcomes Promega

Promega sponsored a preconference workshop for grad and undergrad students at the University of Rwanda’s biotechnology campus in Huye, the capital city of Rwanda’s Southern Province.

More than twenty years after the Rwandan genocide when some 800,000 people were killed in just 100 days by ethnic extremists, Rwanda is on a path to not only healing and order, but also technological advancement. Now politically and functionally stable, which is an exception to the rule in east Africa, the country is recognizing that biotechnology is one of the key drivers to help improve the health and well being of its citizens. Rwanda is focusing on providing the resources and training needed to grow its capabilities in biotechnology, and could be on track to become an African biotech hub.

Rwanda, and its biotech push, caught the attention of Promega by way of customers working with its Belgium-Netherlands-Luxembourg (BNL) branch office. Researchers who are also African ex-patriots working at Université libre de Bruxelles (ULB), a French-speaking private research university in Brussels, Belgium, invited Promega to attend a conference in Rwanda earlier this month organized by the Society for the Advancement of Science in Africa (SASA) and the Rwanda Biotechnology Association focusing on translational science and biotechnology advances in Africa. Promega was a main sponsor of the conference along with US medical device manufacturer Medtronic. Continue reading

A Nickel’s Worth of Free Advice: Biotech and the Law

This year’s participants in Emerging Techniques in Protein and Genetic Engineering, a two-credit graduate course offered in partnership with the Department of Oncology, UW-Madison, held July 17-21, 2017.

Today’s author extends thanks to Heather Gerard, Intellectual Property Manager, Promega Corporation for contributing her expertise to this post.

Students most often come to the BTC Institute with the primary goal of learning about molecular biology technologies. Our mission is to help them update their experimental tool-box, facilitating more capable studies of DNA, RNA and proteins back in their home laboratories.

But what else do we do? Well, we’re glad you asked. Continue reading

Mass Spectrometry Application: Antibody Quantitation for Preclinical PK studies

Isoform_Antibodies_LinkedInTherapeutic monoclonal antibodies (mAbs) represent the majority of therapeutics biologics now on the market, with more than 20 mAbs approved as drugs (1–3). During preclinical development of therapeutic antibodies, multiple variants of each antibody are assessed for pharmacokinetic (PK) characteristics across model systems such as rodents, beagles and  primates. Ligand-binding assays (LBA) are the standard technology used to perform the PK studies for mAb candidates (4). Ligand-binding assays (LBAs) are methods used  to detect and measure a macromolecular interaction between a ligand and a binding molecule. In LBAs, a therapeutic monoclonal antibody is considered to be the ligand, or analyte of interest, while the binding molecule is usually a target protein.

LBAs have certain well-documented limitations (5). Specific assay reagents are often not available early in a program. Interferences from endogenous proteins, antidrug antibodies, and soluble target ligands are potential complicating factors.

Liquid chromatography coupled to tandem mass spectrometry (LC–MS/MS)-based methods represent a viable and complementary addition to LBA for mAb quantification in biological matrixes. LC–MS/MS provides specificity, sensitivity, and multiplexing capability.

A recent reference (6) illustrates an automated method to perform LC–MS/MS-based quantitation, with IgG1 conserved peptides, a heavy isotope labeled mAb internal standard,and anti-human Fc enrichment. The method was applied to the pharmacokinetic study of a mAb dosed in cynomolgus monkey, and the results were compared with the immunoassay data. The interesting finding of the difference between ELISA and LC–MRM-MS data indicated that those two methods can provide complementary information regarding the drug’s PK profile.

Literature Cited

  1. Mao, T. et al. (2013) Top-Down Structural Analysis of an Intact Monoclonal Antibody by Electron Capture Dissociation-Fourier Transform Ion Cyclotron Resonance-Mass Spectrometry. Anal.Chem. 85, 4239–46.
  2. Weiner, L. M. et al. (2010) Monoclonal antibodies: versatile platforms for cancer immunotherapy. Nat. Rev. Immunol. 10, 317–27.
  3. Nelson, A. et al. (2010) Development trends for human monoclonal antibody therapeutics. Nat. Rev. Drug Discovery. 9, 767–74.
  4. DeSilva, B. et al. (2003) Recommendations for the Bioanalytical Method Validation of Ligand-Binding Assays to Support Pharmacokinetic Assessments of MacromoleculesPharm. Res. 20, 1885–00.
  5. Ezan, al. (2009) Critical comparison of MS and immunoassays for the bioanalysis of therapeutic antibodiesBioanalysis 1, 1375–88.
  6. Zhang, Q. et al. (2014) Generic Automated Method for Liquid Chromatography–Multiple Reaction Monitoring Mass Spectrometry Based Monoclonal Antibody Quantitation for Preclinical Pharmacokinetic Studies. Anal.Chem. 86, 8776–84.

Representations of Science

As a storyteller, I notice that there are two stories to most life science research. The first is the story of process, and the second is that of results. Coming from a liberal arts background, the nuance of the second – how chemistry, concentration, base pairs and phosphorylated molecules interact to deliver a measurable result – often escapes me.

I can appreciate process: an idea, followed by a near-endless series of small tests to evaluate the viability of that idea. I can appreciate the sifting of signal from noise, and the dangerous seduction of a tangent, a curious detail, and the empty promise of a lead. Conceptually, these things make art and science close cousins. I can walk comfortably on a conceptual ground, but the hard grammar delivers a path beyond my training and knowledge.

To my eye, this research looks like nothing more than the transfer of clear liquids from tube-to-tube. Sometimes the application of heat is involved, and refrigeration is essential. Visually, the two most exciting things you’ll encounter are a slight color change in a microcentrifuge tube or a bar graph. At the cellular level, we may find a grand narrative of transformation , death, and recovery; at the molecular level we can witness attraction, separation, reconciliation. Yet capturing these events requires either a miracle or a mountain of costly resources. When we want to visually communicate the story of pure DNA , we are left with the story of pipetting liquids.

In developing video protocols for our products, I’ve attempted to keep that point in mind. There are things I cannot practically show, and what I can show needs to be carefully presented in order to remain both accurate and interesting. I’ve also tried to cut details that work better in text without introducing confusion for end users.

Here’s one of the results:

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I invite you to keep an eye out for future video protocols. In the meantime, you should leave a comment and let me know what procedures and products you think would benefit most from this kind of treatment.

New Online Technical Publication for Life Sciences from Promega

tp001Promega has launched a new Online Technical Publication Portal. This new online resource is your place to go for high-quality technical information about life science research, new technologies, and applications of research tools to solve laboratory problems. In addition to great articles, you will find supporting videos, animations and technical tools linked to each article for easy access. Subscribe to the RSS feed so that you will know as soon as new information is published to the site. It is also easy to share articles of interest with other scientists using e-mail or social and professional networking sites. Continue reading

The Search for Biomarkers: Beyond the Norm

Protein biomarker discovery is an area of considerable current interest in biology and medicine.
The implementation of proteomics technology in the field of protein biomarker discovery has expanded in the past few years to enable the identification of biomarkers from a variety of biological samples including cell lysates, tissue samples, serum, plasma and urine (for a review refer to Gao, J. et al. (2005) Methods. 35, 291-302).

One method utilized for the discovery of protein markers includes the use of trypsin digestion of target proteins followed by the analysis of the resulting peptide fragments by mass spectrometry. Continue reading