T7575
Trypsin Protease
Single-use aliquots ensuring consistent proteolytic activity, suitable for mass spectrometry
Synonyme(s) :
Proteomics grade, Trypsin, TPCK treated
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A propos de cet article
UNSPSC Code:
12352204
NACRES:
NA.56
Specific activity:
≥10,000 BAEE units/mg protein
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Laissez-nous vous aiderNom du produit
Trypsin Singles, Proteomics Grade,
grade
Proteomics Grade
form
ready-to-use solution
specific activity
≥10,000 BAEE units/mg protein
mol wt
average mol wt 23.29 kDa
optimum pH
~8.0
storage temp.
2-8°C
Quality Level
Catégories apparentées
Application
Trypsin Singles, Proteomics Grade have been used for protein digestion to analyse generated peptides via MALDI-TOF MS (matrix assisted laser desorption ionization-time of flight mass spectrometry). It has been used for the digestion of proteins to analyse generated peptides via LC-MS (liquid chromatography–mass spectrometry)/MS.
Features and Benefits
- Convenient, single-use 1 μg size
- Eliminates repetitive pipetting
- Reductively methylated to minimize autolytic activity
- TPCK treated to quench chymotryptic activity
- Extensively purified
General description
Experience all of the advantages of Proteomics Grade Trypsin in a convenient, single-use 1 μg package.
Trypsin Singles, Proteomics Grade exhibit excellent proteolytic efficiency, generating more tryptic peptides leading to greater sequence coverage of your peptide of interest. Mass spectra are significantly simplified due to the reduced number of interfering autolytic peaks and their ambiguous adducts. Proteomics Grade Trypsin has been extensively purified from porcine pancreas to enable accurate and precise cleavage on the carboxylic side of Arg and Lys residues. The enzyme has been exhaustively processed by reductive methylation to minimize autolysis and chymotryptic activity has been quenched by TPCK treatment. Further purification steps including affinity chromatography and drying from dilute acid produce a highly purified, high specific activity trypsin purposely suited for the demanding criteria of proteomics research, and designed to function in either solution or gel-based digests.
Trypsin Singles, Proteomics Grade exhibit excellent proteolytic efficiency, generating more tryptic peptides leading to greater sequence coverage of your peptide of interest. Mass spectra are significantly simplified due to the reduced number of interfering autolytic peaks and their ambiguous adducts. Proteomics Grade Trypsin has been extensively purified from porcine pancreas to enable accurate and precise cleavage on the carboxylic side of Arg and Lys residues. The enzyme has been exhaustively processed by reductive methylation to minimize autolysis and chymotryptic activity has been quenched by TPCK treatment. Further purification steps including affinity chromatography and drying from dilute acid produce a highly purified, high specific activity trypsin purposely suited for the demanding criteria of proteomics research, and designed to function in either solution or gel-based digests.
signalword
Danger
Hazard Classifications
Acute Tox. 4 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral - Eye Irrit. 2 - Flam. Liq. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Classe de stockage
3 - Flammable liquids
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David J Gonzalez et al.
The Journal of biological chemistry, 285(36), 28220-28228 (2010-06-29)
Through elaboration of its botulinum toxins, Clostridium botulinum produces clinical syndromes of infant botulism, wound botulism, and other invasive infections. Using comparative genomic analysis, an orphan nine-gene cluster was identified in C. botulinum and the related foodborne pathogen Clostridium sporogenes
Zahraa I Khamis et al.
Journal of Cancer, 1, 70-79 (2010-09-16)
In situ neoplastic prostate cells are not lethal unless they become invasive and metastatic. For cells to become invasive, the prostate gland must undergo degradation of the basement membrane and disruption of the basal cell layer underneath the luminal epithelia.
Melt With This Kiss: Paralyzing and Liquefying Venom of The Assassin Bug Pristhesancus plagipennis (Hemiptera: Reduviidae).
Walker AA, et al.
Molecular and Cellular Proteomics, 16, 552-552 (2017)
Identification of protein binders in artworks by MALDI-TOF/TOF tandem mass spectrometry.
Tripkovic T, et al.
Talanta, 113, 49-61 (2013)
Tiziana Cabras et al.
Molecular & cellular proteomics : MCP, 9(10), 2099-2108 (2010-06-30)
The acidic soluble fraction of whole saliva of type 1 diabetic children was analyzed by reversed phase (RP)(1)-HPLC-ESI-MS and compared with that of sex- and age-matched control subjects. Salivary acidic proline-rich phosphoproteins (aPRP), histatins, α-defensins, salivary cystatins, statherin, proline-rich peptide
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