Tanveer Batth

Tanveer Batth

@tsbatth.bsky.social

Co-founder/CEO KPL ApS , #Proteomics researcher in Copenhagen, Denmark at Københavns Universitet, NNF Center for Protein Research #science, #technology, #culture, memes and vibes.

927 followers1K following138 posts

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Tanveer Batth
@tsbatth.bsky.social

🚀 We're very excited to announce KRysin! We have been working on this for a long time and our preprint is finally today on bioRxiv 🧵👇 www.biorxiv.org/content/10.6...

biorxiv.orgHigh-fidelity bispecific protease KRysin for deeper plasma proteomics and phosphoproteomicsBottom-up proteomics relies on efficient and reproducible proteolytic digestion. Yet trypsin, the most widely used protease, frequently misses cleavages, particularly near prolines, acidic and phospho...
Tanveer Batth
@tsbatth.bsky.social

🤝 Thanks to Genovis, KRysin is now commercially available, and we’re really excited to see how the community puts it to work 👀 We’re far from done in the lab, so expect us to keep flexing our skillz 💪😉

Tanveer Batth
@tsbatth.bsky.social

🙏 Huge thanks to Cristina Hernandez-Rollan, Claire Koenig, Chairman Mao, Jesper V. Olsen. Questions and feedback very welcome , feel free to reach out !💬

Tanveer Batth
@tsbatth.bsky.social

⚡ Throughput: across LC gradients from 60 to 500 samples per day, KRysin identified more plasma protein groups at every throughput (median 903 at 60 SPD, 539 at 500 SPD). That’s 21 to 31% more than Trypsin/LysC and 31 to 40% more than Trypsin 📈

Tanveer Batth
@tsbatth.bsky.social

🧬 Phospho time! We digested HeLa extracts at 1:50 and 1:150 enzyme-to-substrate, enriched with Ti-IMAC and ran narrow-window DIA. KRysin yielded about 25% more class I phosphosites than Trypsin/LysC (48,807 vs 39,158) 🔥

Tanveer Batth
@tsbatth.bsky.social

✅ Digestion completeness: across all three workflows and every timepoint, 85 to 95% of KRysin peptides had zero missed cleavages. Trypsin/LysC came in at 63 to 82%.

Tanveer Batth
@tsbatth.bsky.social

🎯 After 18 hours of direct digestion with minimal sample handling and prep, median proteins CVs of below 10%, while Trypsin/LysC was above 40% ... without normalization 🫣

Tanveer Batth
@tsbatth.bsky.social

✂️ KRysin cleaves C-terminal to lysine and arginine and generates Tryptic peptides. That means standard search settings and your existing LC-MS/MS workflow. Just swap it in.

Tanveer Batth
@tsbatth.bsky.social

🩸 For plasma samples we digested human platelet-poor plasma directly, after protein aggregation capture (PAC), or in urea for 1, 2 and 18 h, and acquired everything by narrow-window DIA on the Orbitrap Astral.

Tanveer Batth
@tsbatth.bsky.social

🤔 Why digestion? Efficiency and reproducibility at this step cap what bottom-up proteomics can measure. Missed cleavages split signal across multiple peptide forms and add variability, and complex samples like plasma are where that hurts most.

Tanveer Batth reposted

eLife
@elife.bsky.social

Systematic characterisation of site-specific proline hydroxylation using hydrophilic interaction chromatography and mass spectrometry

buff.lySystematic characterisation of site-specific proline hydroxylation using hydrophilic interaction chromatography and mass spectrometryA robust workflow for the identification of proline hydroxylation sites in proteins was established, using hydrophilic interaction chromatography enrichment and LC-MS/MS together with refining and filtering...
Tanveer Batth
@tsbatth.bsky.social

#science #peerreview

Thiago Carvalho@cyrilpedia.bsky.social

'Reviewers were paid 220 GBP per manuscript only if they completed the review on time, and the review met editorial quality expectations (...) Fast & Fair reduced time to first decision with reviews from a mean of 37.7 working days under conventional peer review to 5.5 working days.' #Preprint

biorxiv.orgbiorxiv.org

Tanveer Batth reposted

Chris Ashwood
@cashwood.proteaglyco.com

Now published in Nature Communications: www.nature.com/articles/s41... The anomer collapsing advance is something we continue to use today, and we hope others may find it useful. Furthermore, this library is the largest representation to date of the human N-glycome (3x the next biggest) #glycotime

nature.comN-glycopedia: libraries for native N-glycan structural analysis - Nature CommunicationsResearchers created N-glycopedia, a reference library of 226 sugar molecules found on proteins, enabling a native glycomics method to precisely identify and measure these sugars, which influence immun...
Chris Ashwood@cashwood.proteaglyco.com

By deep characterisation of 186 N-glycan standards, we @thencfg.bsky.social have made the most comprehensive targeted LC-MS glycomic assay to date. Non-reduced native glycan analysis is key. We hope this enables anyone with QqQ and interest in #glycotime to measure specific N-glycan structures.

Tanveer Batth
@tsbatth.bsky.social

Super excited to be attending #ASMS2026 in San Diego with team KPL 🎉 We’ll be at the Wednesday poster sessions (June 3, 10:30–2:30) sharing the latest on KRysin — our new protease for plasma proteomics and PTM analysis. Come say hi or reach out if you’re unable to attend 👍🏽👍🏽 #ASMS #Proteomics

KPL ApS@kplaps.bsky.social

KPL ApS is heading to #ASMS2026 in San Diego ! 🔬 We'll be presenting two posters on KRysin, our latest R&D development! 📌 WP 613 – KRysin for PTM Analysis 📌 WP 092 – KRysin for Plasma Proteome Analysis Come find us! 👇 Wednesday, June 3 | 10:30 am – 2:30 pm #ASMS #Proteomics#TeamMassSpec

Tanveer Batth
@tsbatth.bsky.social

Our latest bioRxiv preprint characterizes our recombinant Arg-C Zero protease (available now at kplbio.com/arg-c-zero/ 😏) What you may learn might surprise you!!1!! (ie. equivalent protein group ID's to Trypsin with half the peptide IDs) www.biorxiv.org/content/10.6... #proteomics #teammasspsec

biorxiv.orgbiorxiv.org
KPL ApS@kplaps.bsky.social

🔬 New preprint from KPL ApS: Arg-C Zero, recombinant arginyl endopeptidase with >99% cleavage efficiency, R-P bond cleavage, acid-compatible labile PTM workflows, and histone analysis without derivatization. 📄 doi.org/10.64898/202... 🛒 kplbio.com/arg-c-zero/ #Proteomics #MassSpec #PTM #Enzymes

Tanveer Batth reposted

Andrew G. York
@andrewgyork.bsky.social

I've been getting questions about this paper all week: www.cell.com/cell/abstrac... They make EXTRAORDINARY claims - fortunately, these are trivial to verify/falsify. Unfortunately, there's other concerns.

cell.comElectromagnetic field-inducible in vivo gene switch for remote spatiotemporal control of gene expressionThe EMF-inducible gene switch (Ei) platform provides precise spatiotemporal control of gene expression through Cyb5b-mediated calcium oscillations. This system enables Ei-OSK-driven in vivo rejuvenati...

Tanveer Batth reposted

Manuel Kleiner
@manuelkleiner.bsky.social

I thought it was quite mind boggling to see that around 10% of the protein in a standard yeast based bread is actually yeast protein! Here our #metaproteomics analysis of microbial protein in fermented foods pubs.rsc.org/en/Content/A... Congratulations to first authors Laura Winkler and Ayesha Awan

pubs.rsc.orgAssessing the diversity and functional profile of the “microbial proteome” in fermented foodsFermented foods are staples in diets worldwide and are known for their health benefits. Microorganisms are the key to fermented food production as they convert raw substrates into digestible, nutritio...

Tanveer Batth reposted

Mohammed AlQuraishi
@moalquraishi.bsky.social

New OpenFold3 preview out! (OF3p2) It closes the gap to AlphaFold3 for most modalities. Most critically, we're releasing everything, including training sets & configs, making OF3p2 the only current AF3-based model that is functionally trainable & reproducible from scratch🧵1/9

Tanveer Batth reposted

KPL ApS
@kplaps.bsky.social

🇫🇮🔬 We're at #FinnProt2026 in Espoo, Finland! Our CTO Cristina Hernandez Rollan is presenting a poster with the latest from our R&D pipeline 👀 Stop by to get an early look at what's next from KPL! #Proteomics #MassSpectrometry #TeamMassSpec

Tanveer Batth reposted

Kermit Murray
@kkmurray.bsky.social

(BioRxiv All) Seamless workflow of hydroxy acid-modified metal oxide chromatography for rapid and sensitive phosphoproteomics sample preparation: Phosphoproteomics by liquid chromatography/tandem mass spectrometry requires efficient phosphopeptide enrichment, but conventional… #BioRxiv #MassSpecRSS

dlvr.itSeamless workflow of hydroxy acid-modified metal oxide chromatography for rapid and sensitive phosphoproteomics sample preparationPhosphoproteomics by liquid chromatography/tandem mass spectrometry requires efficient phosphopeptide enrichment, but conventional workflows are often time-consuming and prone to sample loss, particularly at low input. Here, we present Rapid Hydroxy Acid-Modified Metal Oxide Chromatography (Rapid HAMMOC), a streamlined, TiO2-based enrichment workflow that features three key improvements. First, we optimized the TiO2 column loading conditions and found that alternative pH-buffering agents and organic solvents, such as sodium bicarbonate combined with ethyl acetate, outperformed the commonly used Tris-based buffer with isopropanol. Second, to minimize sample loss and manual handling in desalting, phosphopeptides eluted under basic conditions were directly loaded onto a dual-membrane StageTip composed of stacked strong anion exchange (SAX) and reversed-phase styrene-divinylbenzene (SDB) membranes (SAX-SDB StageTip). Third, the addition of lauryl maltose neopentyl glycol (LMNG), which is readily removed during desalting, suppressed nonspecific adsorption. Rapid HAMMOC provided markedly improved sensitivity, identifying approximately 5,000 class I phosphosites from 5g of K562 cell digests, with a median 7.9-fold increase in intensity compared to the original workflow. Rapid HAMMOC also identified, on average, approximately 8,000 class I phosphosites from as little as 0.5 g input from HeLa, A549, and HCT116 cells. Furthermore, coupling Rapid HAMMOC with anti-puromycin immunoprecipitation enabled single-day profiling of nascent polypeptides from ultra-low input samples, yielding 2,310 high-confidence co-translational phosphosites. Beyond providing a practical enrichment workflow, this study offers broadly applicable insights that can be extended to other TiO2-based phosphoproteomic methods.

Tanveer Batth reposted

Kermit Murray
@kkmurray.bsky.social

(BioRxiv All) Expanding Glycopeptide Identification with Match-Between-Glycans in FragPipe: Glycosylation is one of the most important, but also most complex, post-translational modifications of proteins, playing a pivotal role in various pathological processes. Mass… #BioRxiv #MassSpecRSS

dlvr.itExpanding Glycopeptide Identification with Match-Between-Glycans in FragPipeGlycosylation is one of the most important, but also most complex, post-translational modifications of proteins, playing a pivotal role in various pathological processes. Mass spectrometry-based large-scale glycoproteomics analysis offers a powerful approach to explore the fundamental roles of glycosylation in both physiological and pathological contexts. Traditionally, DDA glycopeptide assignment relies on information-dense MS2 spectra, containing sufficient fragmentation information to identify both the peptide and glycan moieties. Achieving this fragmentation can be difficult, especially for low-abundant glycopeptides and/or large, complex glycans. These glycopeptides are often not assigned using current data analysis software, yet they can be of biological relevance. Here, we introduce a method called match-between-glycans (MBG), which expands glycopeptide identification while maintaining the existing glycoproteome analysis workflow. MBG enables expanding the set of identified glycopeptides to include those without MS2 spectra, or with lower quality MS2 spectra, by looking for MS1 signals displaced from other identified glycopeptides by one or multiple monosaccharide unit(s). MBG can also identify glycans not included in the glycan database, such as those containing adducts or modifications, allowing these glycans to be recovered without a drastic expansion of the search space. Combined with target-decoy FDR control, we show this method is capable of accurately expanding glycopeptide identifications and providing a more complete quantitative profile of glycosylation at each glycosite. MBG is fully integrated into the glycoproteomics workflows in FragPipe, allowing seamless, one-click operation.

Tanveer Batth reposted

Chris Ashwood
@cashwood.proteaglyco.com

Maybe this is as controversial as not doing BCA before LC-MS proteomics: “match-between-glycans (MBG), which expands glycopeptide identification…MBG enables expanding the set of identified glycopeptides to include those without MS2 spectra, or with lower quality MS2 spectra,”

Kermit Murray@kkmurray.bsky.social

(BioRxiv All) Expanding Glycopeptide Identification with Match-Between-Glycans in FragPipe: Glycosylation is one of the most important, but also most complex, post-translational modifications of proteins, playing a pivotal role in various pathological processes. Mass… #BioRxiv #MassSpecRSS

dlvr.itExpanding Glycopeptide Identification with Match-Between-Glycans in FragPipeGlycosylation is one of the most important, but also most complex, post-translational modifications of proteins, playing a pivotal role in various pathological processes. Mass spectrometry-based large-scale glycoproteomics analysis offers a powerful approach to explore the fundamental roles of glycosylation in both physiological and pathological contexts. Traditionally, DDA glycopeptide assignment relies on information-dense MS2 spectra, containing sufficient fragmentation information to identify both the peptide and glycan moieties. Achieving this fragmentation can be difficult, especially for low-abundant glycopeptides and/or large, complex glycans. These glycopeptides are often not assigned using current data analysis software, yet they can be of biological relevance. Here, we introduce a method called match-between-glycans (MBG), which expands glycopeptide identification while maintaining the existing glycoproteome analysis workflow. MBG enables expanding the set of identified glycopeptides to include those without MS2 spectra, or with lower quality MS2 spectra, by looking for MS1 signals displaced from other identified glycopeptides by one or multiple monosaccharide unit(s). MBG can also identify glycans not included in the glycan database, such as those containing adducts or modifications, allowing these glycans to be recovered without a drastic expansion of the search space. Combined with target-decoy FDR control, we show this method is capable of accurately expanding glycopeptide identifications and providing a more complete quantitative profile of glycosylation at each glycosite. MBG is fully integrated into the glycoproteomics workflows in FragPipe, allowing seamless, one-click operation.
Tanveer Batth
@tsbatth.bsky.social

Our latest #proteomics product to top off our Lys-C and Trypsin offerings. A high quality optimal premix of Lys-C and Trypsin that enables reproducible proteomic analysis! Make sure to follow @kplaps.bsky.social for more exciting news and updates! #TeamMassSpec

KPL ApS@kplaps.bsky.social

🧪 Just launched: Trypsin/Lys-C Premium Mix 🚀 We found that with the right formulation, you can add Lys-C and Trypsin together instead of sequentially. So we made it 💡 ✅ One step ✅ Lowest missed cleavages in its class ✅ Fully recombinant 🪧Available now 🔗 kplbio.com/trypsinlysc/

Tanveer Batth reposted

Chris Ashwood
@cashwood.proteaglyco.com

Replying to @laureloldach.bsky.social

Check out the first author! pubmed.ncbi.nlm.nih.gov/30671891/

pubmed.ncbi.nlm.nih.govImproving Precursor Selectivity in Data-Independent Acquisition Using Overlapping Windows - PubMedA major goal of proteomics research is the accurate and sensitive identification and quantification of a broad range of proteins within a sample. Data-independent acquisition (DIA) approaches that acquire MS/MS spectra independently of precursor information have been developed to overcome the reprod …

Tanveer Batth reposted

Amanda Moehring
@flybehaviour.bsky.social

Ooooh. Cool new paper on origins of life. A simple 45-nucleotide RNA molecule that can perfectly copy itself. www.science.org/doi/10.1126/...

science.orgA small polymerase ribozyme that can synthesize itself and its complementary strandThe emergence of a chemical system capable of self-replication and evolution is a critical event in the origin of life. RNA polymerase ribozymes can replicate RNA, but their large size and structural ...

Tanveer Batth reposted

Chris Ashwood
@cashwood.proteaglyco.com

Aside from the whisper network, how are #teammassspec finding out how much certain instrument models are down for (service delays, backordered parts, things breaking all the time, etc)?

Tanveer Batth
@tsbatth.bsky.social

Our recombinant, animal free, sustainable, artisanal 😁 Trypsin is here! High quality, high performance, drop in replacement for any existing #proteomics workflows. Designed and produced in 🇩🇰🇪🇺

KPL ApS@kplaps.bsky.social

Introducing Trypsin RMS – our third product is here. Recombinant. Methylated. Sequencing-grade. The robust trypsin #proteomics labs need, without the batch variability of animal-derived alternatives. Learn more: kplbio.com/trypsin/ #TeamMassSpec #science #proteins #enzymes

Tanveer Batth reposted

Sharpe Lab
@sharpe-lab.bsky.social

Pervanadate is more than just a phosphatase inhibitor! Read our paper just published in #sciencesignaling showing that pervanadate oxidises and activates SRC kinase too. Link: tinyurl.com/5ype7e2s Thanks for the 'focus' by: @nshahlab.bsky.social tinyurl.com/54fcjds3 @babrahaminst.bsky.social

science.orgPervanadate-induced oxidation relieves autoinhibition of the protein tyrosine kinase SRCA widely used tyrosine phosphatase inhibitor also oxidizes and activates the tyrosine kinase SRC.

Tanveer Batth reposted

KPL ApS
@kplaps.bsky.social

Trypsin is the workhorse of bottom-up #proteomics. But when was it first discovered? Lets try an emoji poll ! 😇 1836 🤭 1876 😜 1897 🤑 1931 Reply with your guess! Correct answer in the replies! #TeamMassSpec

Tanveer Batth
@tsbatth.bsky.social

New publication alert! 📢 We collaborated with @jesperolsenlab.bsky.social to comprehensively characterize LysC homologs and study their impact on proteomic experiments. For challenging samples, adding LysC can definitely make a difference in the data quality. Congrats to all authors! #proteomics

KPL ApS@kplaps.bsky.social

Does enzyme quality matter in #proteomics? New study in JPR w/ @jesperolsenlab.bsky.social shows: LysC-Trypsin reduces missed cleavages from 30% → 15% KPL's A. lyticus LysC achieves >90% efficiency in systematic comparison. Congrats to the authors! pubs.acs.org/doi/10.1021/... #TeamMassSpec

pubs.acs.orgComparative Analysis of Lysine-Specific Peptidases for Optimizing Proteomics WorkflowsThis study presents a comparative analysis of three LysC endopeptidase homologues from Achromobacter lyticus (A. lyticus),Pseudomonas aeruginosa and Lysobacter enzymogenes for mass spectrometry-based proteomics. Utilizing a protein aggregation capture workflow with HeLa cell lysates, we assessed the enzymes’ cleavage specificity, digestion efficiency, and performance across various experimental conditions. Results showed that while all three LysC homologues exhibited high cleavage specificity at lysine residues, A. lyticus LysC outperformed the two others with superior peptide identification, digestion efficiency, and protein coverage, especially at shorter digestion times. Our experiments using a combination ofA. lyticusLysC and trypsin demonstrated the importance of employing LysC for significantly minimizing missed cleavage rates in tryptic digests, especially with regard to lysine-containing peptides. This study underscores A. lyticus LysC’s potential as an optimal choice for enhancing mass spectrometry-based proteomics.
Tanveer Batth
@tsbatth.bsky.social

To everyone who's supported us, bought from us, or just followed along to see what happens ... Thank you for a great year, you're the real MVPs! 2026 pipeline is looking spicy 🌶️ new products, big announcements I believe will push the field of #proteomics forward. Stay tuned.

KPL ApS@kplaps.bsky.social

Happy Holidays from KPL! 🎄 Our first full year: 2 product launches, lots of foundation building, and countless hours pushing #proteomics forward. Our commitment: high quality, high performance, competitive prices. No compromises. 2026 is looking exciting - stay tuned! ✨