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| 사이즈/SKU | 재고 정보 | 가격 (VAT 별도) |
|---|---|---|
4 x 25 μg | 오늘 배송 예정재고 수량 조회Seoul Warehouse South Korea | ₩323,684 |
₩323,684
오늘 배송 예정세부사항
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
optimum pH
8.0
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
Gene Information
cow ... PRSS1(780933)
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 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.
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.
Application
Use Trypsin Sequencing Grade, modified, to generate glycopeptides from purified glycoproteins.
It is used for:
It is used for:
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.
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.
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
Analysis Note
Purity: Free of impurities that may interfere with the separation of peptides in reversed-phase HPLC.
Other Notes
For life science research only. Not for use in diagnostic procedures.
signalword
Danger
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
저장 등급
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable