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Accelerating breakthroughs in Proteomics

CinderBio enables deeper discovery with new Archaeal enzymes, providing additional proteome coverage.

5min

Single-step sample preparation

100%

De novo antibody sequence with one enzyme in one run

>50%

Additional sequence coverage for known IDs

1 hour

From sample to novel biomarkers

CinderBio offers scientists a better way with a new class of heat and acid stable HyperThermoacidic Archaeal enzymes that reveal much more of the proteome while significantly shortening sample prep and digestion times. Derived from archaea that thrive in the acidic waters of volcanic hot springs, these enzymes are the key to unlocking new discoveries.

Overview

A new generation of proteases

For decades, Proteomics had relied on mesophilic enzymes and their multi-step, multi-day sample preparation before realizing results. These standard approaches are limited in their coverage, redundancy, and reach.

HTA-Protease Advantages

Antibodies

Histones

Nucleic acid-binding proteins

Mitochondrial and membrane proteins

Novel biomarkers

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HTA-Proteases vs Standard Proteases

Detect more—faster and easier

Get faster and better results with the same LC-MS/MS process

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Peer Reviewed Results

Research Partners

Funding Partners

National Science Foundation
Chobani Incubator
United States Department of Agriculture
First Look West
Mount Wilson Ventures
Intertech Ventures
Cleantech to Market
Stanford BASES

Highly efficient hyperthermal acidic proteases combined with hybridfragmentation schemes provide five times more unique peptide reads than trypsin or chymotrypsin, greatly boosting confidence in de novo sequencing. This approach enables confident de novo antibody sequencing based on a single LC-MS run.

IN BRIEF

Laura Perez Paneda, Tereza Kadava, Tatiana M. Shamorkina, ..., Narlock-Brand, Steven M. Yannone, Joost Snijder, and Albert J.R. Heck

AUTHORS

JOURNAL

Deep coverage and extended sequence reads obtained with a single archaeal protease expedite de novo protein sequencing by mass spectrometry

Antibody Sequencing

March 11, 2026

High Throughput Proteomics

Call Systems

Recent Peer-Reviewed Papers

From volcanoes to the bench: Advantages of novel HyperThermoacidic Archaeal proteases for proteomics workflows

October 30, 2023

Novel HTA-proteases function at 70–90°C and pH 2–4, enabling a rapid, 5-minute, single-step preparation for bottom-up proteomics without chaotropes. Their unique cleavage expands sequence coverage for challenging proteins, offering significant advances for high-throughput and clinical proteomics.

Maxwell C. McCabe, Varun Gejji,, Adam Barnebey , Gary Siuzdak , ..., Saviola, Steven M. Yannone, Kirk C. Hansen

AUTHORS

IN BRIEF

JOURNAL

Slow tryptic digestion limits clinical proteomics. The novel "Krakatoa" protease solves this, digesting samples in 5-30 minutes. Combined with rapid LC-MS, it quantifies over 150 proteins and key peptides from raw biofluids in under an hour, enabling true real-time clinical analysis.

IN BRIEF

Steven M. Yannone, Vikas Tuteja, Olena Goleva, Donald Y. M. Leung, ..., Nathan G. Hendricks, Sarah Parker, Jennifer E. Van Eyk, and Simion Kreimer​​

AUTHORS

JOURNAL

Toward Real-Time Proteomics: Blood to Biomarker Quantitation in under One Hour

Biomarker Discovery

Difficult Proteins

March 20, 2025

High Throughput Proteomics

High Throughput Proteomics

Analytical Chemistry

Difficult Proteins

How To Use

Journal of Proteomics

Our Products

Join the proteases revolution and see more biology

CinderBio offers two unique enzymes that can be used together for maximum proteome coverage

CB23726

~100 Reactions

Krakatoa

  • HTA-Protease with E, L, F preferred cleavage

  • Optimal at 80°C, pH 3.0

  • Shelf-stable at room temperature for 2+ years

  • Ships ready to use

$450 USD

CB14057

~100 Reactions

Vesuvius

  • HTA-Protease with E, L, F preferred cleavage

  • Optimal at 80°C, pH 3.0

  • Only 11% peptide overlap with Krakatoa

  • Shelf-stable at room temperature for 2+ years

  • Ships ready to use

$450 USD

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