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.

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

N-glycopedia: libraries for native N-glycan structural analysis - Nature Communications

Researchers 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...

nature.com

Chris Ashwood@cashwood.proteaglyco.com · last yr.

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.

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 · 2mo ago

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

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

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(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

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 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.

dlvr.it

(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

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 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.

dlvr.it

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 · 6mo ago

(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

1/ The Dolphin Head (Sh2-308) is an emission nebula in the Canis Major region: a huge bubble created by material expelled by the star WR6, swept by its powerful stellar wind. It’s also a target that drove me crazy for four years before I finally started to get a grip on it. ➡️ 🔭 #Astrophotography

The Dolphin Head nebula in Canis Major constellation, photographed from my terrace

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 · 6mo ago

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