Rapid Novor Inc

05/29/2026

Heading to ASMS 2026? Check out our poster with the latest HDX-MS data for our anti-idiotype antibody discovery workflow!

📌 Poster presented by Dominic Narang
📅 June 2, 2026
🧪Antibodies & Antibody Drug Conjugates I

05/21/2026

Understanding why certain viral mutations become evolutionarily advantageous requires more than static protein structures; it requires studying proteins in motion, in environments that closely resemble their native biological context.

For SARS-CoV-2, much of what we know about the spike protein structure comes from engineered soluble constructs designed for biochemical and structural studies or for vaccines. A recent study by Sophie Shoemaker and colleagues at UC Berkeley and the Gladstone Institute of Virology addresses this gap by combining HDX-MS with enveloped virus-like particles (eVLPs) displaying full-length spike protein in a near-native membrane environment.

💡 𝗞𝗲𝘆 𝗙𝗶𝗻𝗱𝗶𝗻𝗴𝘀 💡
• 𝗩𝗮𝗹𝗶𝗱𝗮𝘁𝗶𝗼𝗻 𝗼𝗳 𝘁𝗵𝗲 𝗼𝗽𝗲𝗻-𝗶𝗻𝘁𝗲𝗿𝗳𝗮𝗰𝗲 𝘁𝗿𝗶𝗺𝗲𝗿 𝗶𝗻 𝗮 𝗻𝗮𝘁𝗶𝘃𝗲 𝗺𝗲𝗺𝗯𝗿𝗮𝗻𝗲 𝗲𝗻𝘃𝗶𝗿𝗼𝗻𝗺𝗲𝗻𝘁: The open-interface trimer was confirmed in membrane-embedded spike, showing that this conformation is an inherent property of the protein rather than an artifact of engineered soluble constructs.
• 𝗧𝗵𝗲 𝗲𝘃𝗼𝗹𝘂𝘁𝗶𝗼𝗻𝗮𝗿𝘆 𝗮𝗱𝘃𝗮𝗻𝘁𝗮𝗴𝗲 𝗼𝗳 𝘁𝗵𝗲 𝗺𝘂𝗹𝘁𝗶𝗯𝗮𝘀𝗶𝗰 𝗳𝘂𝗿𝗶𝗻 𝗰𝗹𝗲𝗮𝘃𝗮𝗴𝗲 𝘀𝗶𝘁𝗲: The additional basic residue in SARS-CoV-2 enhances furin cleavage efficiency. Cleavage at S1/S2 allosterically increases flexibility at the S2′ site, promoting TMPRSS2 processing and membrane fusion, but also favors formation of the open-interface trimer.
• 𝗧𝗵𝗲 𝗲𝘃𝗼𝗹𝘂𝘁𝗶𝗼𝗻𝗮𝗿𝘆 𝗮𝗱𝘃𝗮𝗻𝘁𝗮𝗴𝗲 𝗼𝗳 𝘁𝗵𝗲 𝗗𝟲𝟭𝟰𝗚 𝗺𝘂𝘁𝗮𝘁𝗶𝗼𝗻: D614G stabilizes the closed prefusion trimer, counteracting furin-driven destabilization and reducing premature S1 shedding that could render the virus noninfectious.

HDX-MS is uniquely suited to studies like this because it captures conformational dynamics at peptide resolution without disrupting the native complex. By enabling researchers to probe flexibility, allostery, and transient conformational states, HDX-MS provides insights that static structural techniques alone often cannot capture.

📄𝗥𝗲𝗮𝗱 𝘁𝗵𝗲 𝘀𝘁𝘂𝗱𝘆 𝗵𝗲𝗿𝗲: https://hubs.li/Q04hw9Vn0

🔬𝗟𝗲𝗮𝗿𝗻 𝗺𝗼𝗿𝗲 𝗮𝗯𝗼𝘂𝘁 𝗛𝗗𝗫-𝗠𝗦 𝗵𝗲𝗿𝗲: https://hubs.li/Q04hwbDg0

05/13/2026

🎬We’re live from PEGs Boston!

Jennifer Crha, Kyle Annibale, Mingjie Xie, Thierry Le Bihan, (and mAbel the moose 🫎) are here all week to dive into de novo polyclonal antibody sequencing, epitope mapping, and antibody characterization.

You can find us at ⬇️
📍 𝗕𝗼𝗼𝘁𝗵 #𝟯𝟭𝟴
📌 𝗣𝗼𝘀𝘁𝗲𝗿 𝗣𝗿𝗲𝘀𝗲𝗻𝘁𝗮𝘁𝗶𝗼𝗻: Thursday, May 15 | "Conversion of Polyclonal Anti-Idiotypes into Characterized Recombinant Antibodies"

One of the highlights so far? Welcoming a very special guest: Jennifer's mom, and a longtime Rapid Novor supporter. 😊

If you’re attending PEGS this week, come say hello!

05/08/2026

Technology has come a long way, but some things never change… 😅

What's one thing that would improve your life in the lab?

05/07/2026

We’re counting down to and excited to be part of this year’s event!

📍Stop by Booth 318 anytime next week (May 11–15) to connect with Mingjie Xie, Thierry le Bihan, Jennifer Crha, and Kyle Annibale.

Catch Thierry’s presentation on anti-idiotype antibodies on Tuesday and the corresponding poster on Thursday!

𝘊𝘰𝘯𝘷𝘦𝘳𝘴𝘪𝘰𝘯 𝘰𝘧 𝘗𝘰𝘭𝘺𝘤𝘭𝘰𝘯𝘢𝘭 𝘈𝘯𝘵𝘪-𝘐𝘥𝘪𝘰𝘵𝘺𝘱𝘦𝘴 𝘪𝘯𝘵𝘰 𝘊𝘩𝘢𝘳𝘢𝘤𝘵𝘦𝘳𝘪𝘻𝘦𝘥 𝘙𝘦𝘤𝘰𝘮𝘣𝘪𝘯𝘢𝘯𝘵 𝘈𝘯𝘵𝘪𝘣𝘰𝘥𝘪𝘦𝘴:

💬𝗣𝗼𝗱𝗶𝘂𝗺 𝗣𝗿𝗲𝘀𝗲𝗻𝘁𝗮𝘁𝗶𝗼𝗻 - Track C2A
Tuesday May 12, 12:15 PM

📊 𝗣𝗼𝘀𝘁𝗲𝗿 𝗣𝗿𝗲𝘀𝗲𝗻𝘁𝗮𝘁𝗶𝗼𝗻 – Poster C091
Thursday May 15 (all day)

We’re looking forward to sharing how our REpAb platform is advancing polyclonal antibody discovery—enabling the conversion of complex mixtures into well-defined recombinant reagents.

See you there!

05/06/2026

🥳 We just celebrated our 11th anniversary!

Only five months in, and this year is already one for the books. EasyM received a provisional licence from the Ontario Ministry of Health (MOH) to provide testing for Canadian patients, and we completed enrollment for the first Canadian prospective clinical study evaluating EasyM; huge wins for our team and for patients across Canada.

We celebrated the only way we know how: with good food and good company (don't worry, we made sure our remote teammates felt included too 😉)

Here's to 11 years of great science and even greater people. Thank you to everyone who has been part of this journey!

04/30/2026

What will it take to make universal vaccines truly universal?

Universal vaccines aim to provide broad, long-lasting protection against rapidly mutating viruses like influenza, HIV, and SARS-CoV-2, reducing the need for constant reformulation. Their success depends on eliciting broadly neutralizing antibodies (bnAbs) across diverse populations.

This may be even more complex than expected.

A recent study by Martin Corcoran and Sanjana Narang, PhD et al. used high-throughput antibody gene sequencing (ImmuneDiscover) to map immunoglobulin variation across ~2,500 individuals from diverse global populations. The results were striking:

• 561 functional IGHV alleles were identified, with ~70% absent from existing reference databases (AIRR-C)
• A homozygous deletion of six IGHD genes was found in up to 30% of individuals of East and South Asian ancestry, genes often used in bnAb responses to influenza, HIV, and SARS-CoV-2

This raises an important question:
👉 If the genetic blueprint differs so widely, can all populations generate the same protective antibodies? And if not, does the immune system compensate for these gaps, or are certain populations left without a critical defence against certain pathogens?

Proteomics can help answer this by directly analyzing circulating antibodies, revealing how the immune system responds despite genetic constraints.

At Rapid Novor, our proteomics-driven polyclonal antibody sequencing service (REpAb) is built for this kind of discovery. By sequencing the full circulating antibody repertoire directly from serum, REpAb enables researchers to identify which antibody clones are actually being expressed.

📄 𝗥𝗲𝗮𝗱 𝘁𝗵𝗲 𝗽𝗮𝗽𝗲𝗿 𝗵𝗲𝗿𝗲:
https://hubs.li/Q04d-M7g0

🔬 𝗟𝗲𝗮𝗿𝗻 𝗮𝗯𝗼𝘂𝘁 𝗥𝗘𝗽𝗔𝗯 𝗵𝗲𝗿𝗲:
https://hubs.li/Q04d-HVk0

04/29/2026

Discover how to turn your polyclonal anti-idiotypes into fully characterized recombinants that actually work. Join us at PEGS Boston!

Join Thierry Le Bihan as he shares how our integrated proteomics workflow enables the discovery and validation of diverse, high-quality anti-idiotype populations, and how SPR and HDX-MS can uncover critical optimization opportunities you might otherwise miss.

🗓️ 𝗠𝗮𝘆 𝟭𝟮 | 𝟭𝟮:𝟭𝟱𝗣𝗠 | 𝗧𝗿𝗮𝗰𝗸: 𝗖𝟮𝗔

💬 𝗧𝗮𝗹𝗸: Conversion of Polyclonal Anti-Idiotypes into Characterized Recombinant Antibodies

04/16/2026

A shift away from animal testing is gaining real momentum across drug development and life sciences research.

Regulatory agencies like the FDA and EMA are increasingly supporting New Approach Methodologies (NAMs), from 𝘪𝘯 𝘷𝘪𝘵𝘳𝘰 assays to computational modeling, as credible, human-relevant alternatives to traditional animal studies. But one dependency is proving harder to resolve: antibody generation. Polyclonal antibodies remain essential tools across therapeutics, diagnostics, and basic research, yet many are still generated through animal immunization, particularly when polyclonal responses or complex antigen recognition are required.

In our latest article, we take a closer look at:
• The current landscape of animal testing and research
• The rise of NAMs in drug development
• Where animal dependencies still persist and emerging strategies

As momentum builds toward more human-relevant science, rethinking how antibodies are discovered and produced will be an important part of the transition.

👉 𝗥𝗲𝗮𝗱 𝘁𝗵𝗲 𝗳𝘂𝗹𝗹 𝗮𝗿𝘁𝗶𝗰𝗹𝗲: https://hubs.li/Q04crbkW0

Written By: Monica Mioduszewski Published: April 16, 2026 Contents Introduction How many animals are used in research? Which animals are used for testing? Why animal models remain in use Limitations of Animal Models New Approach Methodologies (NAMs):

04/15/2026

In a new study, Tao Yin, Metin Yesiltepe, and colleagues from Rutgers and the University of Cambridge report the development of humanized nanobodies targeting transferrin receptor 1 (TfR1) to enable receptor-mediated transport of biologics across the blood–brain barrier (BBB); a major hurdle in CNS drug delivery.

To determine the binding kinetics of their newly-engineered anti-TfR1 nanobodies to TfR1, the team used Rapid Novor’s SPR service, performing multi-cycle kinetic analysis in both orientations, along with custom iso-affinity analysis to easily compare binding affinities and association and dissociation rates. This provided detailed insight into binding behavior beyond standard affinity measurements.

Building on their previous work developing TNFα inhibitory nanobodies (also characterized with Rapid Novor's SPR service), the researchers engineered fusion constructs combining TfR1-binding nanobodies with TNFα-inhibitory nanobodies. These constructs successfully crossed the BBB and maintained sustained levels in both cerebrospinal fluid and serum.

The results highlight the potential of TfR1-targeting nanobodies as “NewroBus” shuttles for delivering biologics into the brain, while preserving transferrin function and avoiding hematologic toxicity.

📄 𝗥𝗲𝗮𝗱 𝘁𝗵𝗲 𝗳𝘂𝗹𝗹 𝗽𝘂𝗯𝗹𝗶𝗰𝗮𝘁𝗶𝗼𝗻 𝗵𝗲𝗿𝗲: https://hubs.li/Q04c8jvH0