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Mass Spectrometry Grade Proteases
Mass Spectrometry Grade Proteases
Thermo Scientific™

Mass Spectrometry Grade Proteases

Improve sequence coverage and protein identification for mass spectrometry with high-quality, MS-grade proteases provided in stable liquid or lyophilized formats. Suitable for either in-solution or in-gel digestion workflows, each protease may be used individually or in combination to improve protein sequence coverage.
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Catalog NumberQuantityProduct Type
900591 mgTrypsin Protease
900532 μgAsp-N Endoproteinase
900564 x 25 μgChymotrypsin Endoproteinase
900545 x 10 μgGlu-C Endoproteinase
903051 x 100 μgTrypsin Protease
A4000720 μgTrypsin/Lys-C Protease Mix
A410075 x 20 μgTrypsin/Lys-C Protease Mix
A40009100 μgTrypsin/Lys-C Protease Mix
900511 x 20 μgLys-C Endoproteinase
90307100 μgLys-C Protease
900575 x 20 μgTrypsin Protease
900585 x 100 μgTrypsin Protease
Catalog number 90059
Price (USD)
700.40
Special offer
Online exclusive
Ends: 15-Aug-2025
824.00
Save 123.60 (15%)
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Quantity:
1 mg
Product Type:
Trypsin Protease
Recurring order eligible. Learn more »
Request bulk or custom format
Price (USD)
700.40
Special offer
Online exclusive
Ends: 15-Aug-2025
824.00
Save 123.60 (15%)
Each
Add to cart
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Protein characterization, identification, and quantification by MS begins with efficient, reproducible protein digestion. Sequence specific proteases are utilized to cleave proteins into smaller fragments or peptides. Trypsin is the protease of choice for protein digestion. However, separate or sequential digestion with alternative proteases can improve individual protein sequence coverage, or generate unique peptide sequences for different MS applications.
Exceptional selectivity—trypsin has >95% C-terminal lysine and arginine specificity; LysC has >90% C-terminal lysine cleavage specificity
High purity—no detectable chymotrypsin activity (trypsin)
Complete digestion—trypsin/LysC enzyme combination reduces tryptic missed cleavages
Enhanced stability—trypsin chemically modified for reduced autolytic activity
Convenient—enzymes provided in stable lyophilized or liquid formats

Trypsin Protease is a mass spectrometry (MS)-grade serine protease derived from porcine pancreatic extracts that specifically cleaves at the carboxyl side of lysine and arginine residues. The enzyme is TPCK-treated to eliminate chymotryptic activity and chemically modified by methylation, yielding a highly active and more stable form of the enzyme. Trypsin Protease can tolerate commonly used partially denaturing conditions, such as 0.1% SDS, 1 M urea, and 10% acetonitrile. Trypsin Protease is most active at pH 7 to 9 and can be reversibly inactivated at pH < 4. Trypsin can be purchased lyophilized in 1-mg 5-packs of 20 μg or 100 μg quantities and in solution at 100 μg.

Lys-C Protease is a mass spectrometry (MS)-grade serine protease isolated from Lysobacter enzymogenes. Lys-C Protease has high activity and specificity for lysine residues, resulting in larger peptides and less sample complexity than trypsin (i.e., fewer peptides). Unlike trypsin, Lys-C Protease can cleave lysines followed by prolines, making it ideal for sequential protein digestion followed by trypsin to decrease missed cleavages. These unique Lys-C Protease properties ensure high digestion efficiency when used alone or followed by tryptic digestion. Additionally, Lys-C prototypic peptides typically have higher charge states, making it an enzyme of choice for use with ETD fragmentation.

Lys-C Protease is commonly used in phosphopeptide enrichment workflows because it generates peptides with primary amines at both the N- and C-terminus, allowing the fragments to be double-labeled with amine-reactive isobaric tags. This results in enhanced peptide ionization and improved limits of quantitation since more fragment ions can be re-isolated during MS3 acquisition. This enzyme can be used for in-solution or in-gel digestion workflows to produce peptides for LC-MS/MS protein identification.

Efficient protein digestion can be completed in two hours at 37°C. Lys-C Protease remains active in highly denaturing conditions, such as 8 M urea, 2 M guanidine-HCl, 1% SDS, 2% CHAPS, and 40% acetonitrile, and functions well at pH 7–9 (maximal activity at pH 8). This lyophilized enzyme has a mass of 30 kDa and is stable for one year when stored at –20°C. This Lys-C enzyme is packaged lyophilized (20 μg or 100 μg quantities).

Trypsin/Lys-C Protease Mix is a lyophilized mixture of trypsin and LysC proteases that has been optimized to improve digestion efficiency of proteins. Although trypsin is routinely used for protein digestion, this protease alone is not sufficient to fully digest proteins at the carboxyl-end of lysine and arginine residues. Therefore, Lys-C protease is commonly combined with trypsin to sequentially digest proteins with fewer missed cleavages. Trypsin/Lys-C Protease Mix is provided in flexible formats of 20 μg, 5 x 20 μg, or 100 μg. Digestion can be completed in as little as 1.5–3 hours or up to overnight, depending on enzyme to protein ratio.

Chymotrypsin, GluC, Asp-N Proteases

• Increased sequence coverage—better protein characterization results from overlapping peptides with complementary chromatographic, ionization, and fragmentation properties
• High specific activity—each protease has excellent enzymatic specificity
• Stable—provided in a lyophilized format

Asp-N Protease is an MS-grade zinc metalloproteinase derived from a mutant strain of Pseudomonas fragi and requires a trace amount of zinc for activity. Asp-N Protease cleaves primarily at the amino side of aspartate and cysteic acid that results from cysteine oxidation. Cleavage can also occur at glutamic acid; however, the rate of cleavage at the glutamyl residue is significantly lower than the rate of cleavage at the aspartic acid residue. Asp-N Protease can efficiently digest protein in 2–20 hours at 37°C with activity greater than 20,000 units/mg protein and remains active under denaturing conditions, such as 1 M urea, 2 M guanidine·HCl, 0.1% SDS, 2% CHAPS, and 10% acetonitrile, with optimal activity at pH 6–8. This lyophilized enzyme has a mass of 27 kDa and is stable for one year when stored at -20°C.

Glu-C Protease, also referred to as V-8 protease, is an MS-grade serine protease isolated from Staphylococcus aureus. Glu-C Protease specifically cleaves the carboxyl side of glutamic acid residues in ammonium bicarbonate and ammonium acetate buffers, generating a limited number of peptide fragments. Cleavage can also occur at both glutamic and aspartic acid residues in phosphate buffers. Glu-C Protease can efficiently digest protein in 5–18 hours at 37°C with activity greater than 500 units/mg protein and remains active under denaturing conditions, such as 2 M urea, 1 M guanidine·HCl, 0.1% SDS, 2% CHAPS, and 20% acetonitrile. Glu-C Protease activity is optimal at pH 8. This lyophilized enzyme has a mass of 27 kDa and is stable for one year when stored at -20°C.

Chymotrypsin Protease is an MS-grade endoproteinase isolated from bovine pancreas that specifically cleaves at the carboxyl side of tyrosine, phenylalanine, tryptophan, and leucine. Two predominant forms of chymotrypsin protease, A and B, are found in equal amounts in bovine pancreas. They are similar proteins (80% homology) but have different proteolytic characteristics. Both forms of chymotrypsin protease are present in Thermo Scientific Chymotrypsin Protease. Since trypsin may co-purify with chymotrypsin protease derived from natural sources, Chymotrypsin Protease has been treated with TLCK to eliminate potential tryptic activity, improving digestion specificity. Chymotrypsin Protease can tolerate mild denaturing conditions, such as 0.1% SDS, 2 M urea, 2 M guanidine·HCl, 1% CHAPS, and 30% acetonitrile, with optimal activity at pH 7.5–8.5. This lyophilized enzyme has a mass of 25 kDa and is stable for one year when stored at -20°C.

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Final Product TypeEnzyme
For Use With (Equipment)Mass Spectrometer
GradeMS
Quantity1 mg
Shipping ConditionProducts are shipped with ice.
Workflow StepProtein Digestion
Detection MethodMass Spectrometry
FormPowder
Product LinePierce™
Product TypeTrypsin Protease
Starting MaterialProtein Samples, Cell Lysate
Unit SizeEach
Contents & Storage
Upon receipt, store at -20°C in a non frost-free freezer.
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3217159Certificate of AnalysisJul 14, 2025A40009
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Citations & References (17)

Citations & References
Abstract
Microsecond dynamics control the HIV-1 envelope conformation.
Authors:Bennett AL,Edwards RJ,Kosheleva I,Saunders C,Bililign Y,Williams A,Manosouri K,Saunders KO,Haynes BF,Acharya P,Henderson R
Journal:bioRxiv : the preprint server for biology
PubMed ID:37292605
The HIV-1 Envelope (Env) glycoprotein facilitates host cell fusion through a complex series of receptor-induced structural changes. Although significant progress has been made in understanding the structures of various Env conformations and transition intermediates that occur within the millisecond timescale, faster transitions in the microsecond timescale have not yet been ... More
Weight loss increases skeletal muscle mitochondrial energy efficiency in obese mice.
Authors:Ferrara PJ,Lang MJ,Johnson JM,Watanabe S,McLaughlin KL,Maschek JA,Verkerke ARP,Siripoksup P,Chaix A,Cox JE,Fisher-Wellman KH,Funai K
Journal:Life metabolism
PubMed ID:37206438
Weight loss from an overweight state is associated with a disproportionate decrease in whole-body energy expenditure that may contribute to the heightened risk for weight regain. Evidence suggests that this energetic mismatch originates from lean tissue. Although this phenomenon is well documented, the mechanisms have remained elusive. We hypothesized that ... More
Proteomic Analysis of Tears and Conjunctival Cells Collected with Schirmer Strips Using timsTOF Pro: Preanalytical Considerations.
Authors:Akkurt Arslan M,Kolman I,Pionneau C,Chardonnet S,Magny R,Baudouin C,Brignole-Baudouin F,Kessal K
Journal:Metabolites
PubMed ID:35050124
This study aimed to investigate the human proteome profile of samples collected from whole (W) Schirmer strips (ScS) and their two parts-the bulb (B) and the rest of the strip (R)-with a comprehensive proteomic approach using a trapped ion mobility mass spectrometer, the timsTOF Pro. Eight ScS were collected from ... More
Subcellular proteomics combined with bioenergetic phenotyping reveals protein biomarkers of respiratory insufficiency in the setting of proofreading-deficient mitochondrial polymerase.
Authors:McLaughlin KL,Kew KA,McClung JM,Fisher-Wellman KH
Journal:Scientific reports
PubMed ID:32107436
The mitochondrial mutator mouse is a well-established model of premature aging. In addition to accelerated aging, these mice develop hypertrophic cardiomyopathy at ~13 months of age, presumably due to overt mitochondrial dysfunction. Despite evidence of bioenergetic disruption within heart mitochondria, there is little information about the underlying changes to the ... More
The RNA helicase Dbp10 coordinates assembly factor association with PTC maturation during ribosome biogenesis.
Authors:Mitterer V,Hamze H,Kunowska N,Stelzl U,Henras AK,Hurt E
Journal:Nucleic acids research
PubMed ID:38113283
During ribosome biogenesis a plethora of assembly factors and essential enzymes drive the unidirectional maturation of nascent pre-ribosomal subunits. The DEAD-box RNA helicase Dbp10 is suggested to restructure pre-ribosomal rRNA of the evolving peptidyl-transferase center (PTC) on nucleolar ribosomal 60S assembly intermediates. Here, we show that point mutations within conserved ... More
17 total citations

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