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Merck

TRYPSEQM-RO

Roche

Trypsin Sequencing Grade, modified

from bovine pancreas

Szinonimák:

Trypsin

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Enzyme Commission szám:
UNSPSC kód:
12352204

biológiai forrás

bovine pancreas

Minőségi szint

grade

protein sequencing grade

form

lyophilized (salt-free)

molekulatömeg

24.000 g/mol

kiszerelés

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

gyártó/kereskedő neve

Roche

tárolási körülmény

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

koncentráció

0.01-0.2 % (w/w)

technika/technikák

protein sequencing: suitable

szennyeződések

Chymotrypsin

szín

white

optimális pH

8.0

oldhatóság

10 g/L

alkalmasság

suitable for protein modification

UniProt elérési szám

alkalmazás(ok)

life science and biopharma

idegen aktivitás

Contaminating activities corresponds
Chymotrypsin , contains

tárolási hőmérséklet

2-8°C

Géninformáció

Általános leírás

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 such as liquid chromatography, mass spectrometry (MS).

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

Egyediség

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.

Alkalmazás

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
  • Protein digestion during lipoprotein preparation for liquid chromatography-tandem mass spectrometry (LC-MS/MS)

Minőség

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

Elkészítési megjegyzés

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.

Tárolás és stabilitás

Store dry

Egyéb megjegyzések

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

Piktogramok

Exclamation markHealth hazard

Figyelmeztetés

Danger

Figyelmeztető mondatok

Veszélyességi osztályok

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

Célzott szervek

Respiratory system

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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
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
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
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)

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