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Merck

TRYPSEQM-RO

Roche

Trypsin Sequencing Grade, modified

from bovine pancreas

Synonim(y):

Trypsin

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Wybierz wielkość

4 X 25 μG

853,00 zł

853,00 zł


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Informacje o tej pozycji

UNSPSC Code:
12352204
NACRES:
NA.54

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Nazwa produktu

Trypsin Sequencing Grade, modified, from bovine pancreas

optimum pH

8.0

biological source

bovine pancreas

form

lyophilized (salt-free)

mol wt

24.000 g/mol

packaging

pkg of 4 × 100 μg (11418033001)
pkg of 4 × 25 μg (11418025001)

manufacturer/tradename

Roche

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

concentration

0.01-0.2 % (w/w)

technique(s)

protein sequencing: suitable

impurities

Chymotrypsin

color

white

solubility

10 g/L

suitability

suitable for protein modification

UniProt accession no.

application(s)

life science and biopharma

foreign activity

Contaminating activities corresponds
Chymotrypsin , contains

storage temp.

2-8°C

Quality Level

Gene Information

cow ... PRSS1(780933)

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Ta pozycja
TRYPSEQ-RORTRYP-RO650275
grade

protein sequencing grade

grade

-

grade

-

grade

-

biological source

bovine pancreas

biological source

bovine pancreas

biological source

-

biological source

-

technique(s)

protein sequencing: suitable

technique(s)

-

technique(s)

-

technique(s)

-

Gene Information

cow ... PRSS1(780933)

Gene Information

-

Gene Information

-

Gene Information

-

form

lyophilized (salt-free)

form

lyophilized (salt-free)

form

lyophilized

form

lyophilized solid

concentration

0.01-0.2 % (w/w)

concentration

-

concentration

-

concentration

-

Analysis Note

Purity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC.

Application

Use Trypsin Sequencing Grade, modified, to generate glycopeptides from purified glycoproteins.
It is used for:
  • Protein-structure elucidation
  • Tryptic mapping
  • Fingerprinting analysis
  • Sequence analysis
  • Translocation studies
  • Protein identification[1][2][3][4]
  • Protein digestion during lipoprotein preparation for liquid chromatography-tandem mass spectrometry (LC-MS/MS)[5]

Biochem/physiol Actions

Trypsin is a serine endopeptidase. At pH 7.5–9, it specifically hydrolyzes proteins and peptide bonds C-terminally of Iysine and arginine. Amide and ester bonds of Arg and Lys are also cleaved. The specificity of Trypsin Sequencing Grade, modified, is verified with the oxidized B-chain of insulin (insulin Box) as a substrate. High concentrations of Trypsin Sequencing Grade, modified, one part by weight enzyme with 9 parts by weight insulin Box, are incubated for 18 hours to detect traces ofchymotrypsin impurities.

General description

Trypsin Sequencing Grade, modified, is isolated from bovine pancreas as a highly purified and specific protease, and subsequently modified.

Trypsin is a highly efficient and specific protease widely used in proteomics for protein digestion. It produces short peptides with specific characteristics that are compatible with current separation and identification methods[6] such as liquid chromatography, mass spectrometry (MS).[7][8]

Inhibitors:
TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin,α1-antitrypsin, APMSF, and antipain.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Preparation Note

Working concentration: 1/100 to 1/5 of the protein by weight
Storage conditions (working solution): -15 to -25 °C
Trypsin Sequencing Grade, modified, is more resistant to autolysis, even at pH values in the neutral and weakly basic range. The enzyme can be used in high concentrations.
A solution in 1% acetic acid or 1 mM HCI can be used for up to one week when stored at 2 to 8° C. Stored in aliquots at -15 to -25 °C, the solution is stable for at least one year without loss of activity.
Store dry
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pictograms

Exclamation markHealth hazard

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Klasa składowania

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Comparative proteomics analysis of human FFPE testicular tissues reveals new candidate biomarkers for distinction among azoospermia types and subtypes.
Davalieva, et al.
Journal of proteomics, 267, 104686-104686 (2022)
Xuchu Wang et al.
Molecular & cellular proteomics : MCP, 12(8), 2174-2195 (2013-05-11)
Thellungiella halophila, a close relative of Arabidopsis, is a model halophyte used to study plant salt tolerance. The proteomic/physiological/transcriptomic analyses of Thellungiella plant leaves subjected to different salinity levels, reported herein, indicate an extraordinary ability of Thellungiella to adapt to
Jianke Li et al.
PloS one, 5(10), e13455-e13455 (2010-10-27)
Honeybee (Apis mellifera) exhibits divisions in both morphology and reproduction. The queen is larger in size and fully developed sexually, while the worker bees are smaller in size and nearly infertile. To better understand the specific time and underlying molecular
Proteomics Using Protease Alternatives to Trypsin Benefits from Sequential Digestion with Trypsin
Dau T, et al.
Analytical Chemistry, 92(14), 9523?9527-9523?9527 (2020)
Scott J Walmsley et al.
Journal of proteome research, 12(12), 5666-5680 (2013-10-15)
Trypsin is an endoprotease commonly used for sample preparation in proteomics experiments. Importantly, protein digestion is dependent on multiple factors, including the trypsin origin and digestion conditions. In-depth characterization of trypsin activity could lead to improved reliability of peptide detection

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