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Méret kiválasztása
Nézet módosítása
| Csomagméret | Cikkszám | Elérhetőség | Ár |
|---|---|---|---|
| 4 x 25 μg | Az elérhetőséggel kapcsolatos kérdésekkel kérjük, forduljon Vevőszolgálatunkhoz. | 58 900,00 Ft | |
| 4 x 100 μg | Az elérhetőséggel kapcsolatos kérdésekkel kérjük, forduljon Vevőszolgálatunkhoz. | 178 000,00 Ft |
58 900,00 Ft
Az elérhetőséggel kapcsolatos kérdésekkel kérjük, forduljon Vevőszolgálatunkhoz.
Műszaki ügyfélszolgálat
Segítségre van szüksége? Szakértő tudósaink csapata készséggel áll az Ön rendelkezésére.
Segíthetünk?recombinant
expressed in Pichia pastoris
assay
95% (gel filtration)
form
lyophilized
specific activity
≥150 units/mg protein
packaging
pkg of 4 × 100 μg (03708969001), pkg of 4 × 25 μg (03708985001)
manufacturer/tradename
Roche
storage temp.
−20°C
General description
This trypsin preparation is generated from the recombinant Pichia pastoris strain and is, thus, free of chymotrypsin. Trypsin recombinant, Proteomics Grade, exhibits high specific activity.
Application
Biochem/physiol Actions
Serine endopeptidase, hydrolyzing specifically proteins and peptides at the carboxy side of the basic amino acids Arg and Lys. Amide and ester bonds of Arg and Lys are also cleaved.
Preparation Note
Stabilizers: Ca2+ in mM concentration range
Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin, α1-antitrypsin, APMSF, and antipain.
Storage conditions (working solution): -15 to -25°C
The reconstituted solution is stable for 1 month at -15 to -25°C. Avoid repeated freezing/thawing!
Inhibitors: TLCK, DFP, PMSF, leupeptin, soybean trypsin inhibitor, trypsin inhibitor from hen egg, aprotinin, α2-macroglobulin, α1-antitrypsin, APMSF, and antipain.
Storage conditions (working solution): -15 to -25°C
The reconstituted solution is stable for 1 month at -15 to -25°C. Avoid repeated freezing/thawing!
Following reconstitution in 10 mM HCl, Trypsin, recombinant, proteomics grade is stable at -15 to -25 °C for up to one month. After first reconstitution the product must be stored in appropriate aliquots to avoid repeated freezing and thawing.
Other Notes
For life science research only. Not for use in diagnostic procedures.
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Ez a tétel | |||
|---|---|---|---|
| assay 95% (gel filtration) | assay - | assay - | assay - |
| specific activity ≥150 units/mg protein | specific activity ≥10,000 units/mg protein | specific activity ≥10,000 units/mg protein | specific activity - |
| recombinant expressed in Pichia pastoris | recombinant expressed in Pichia pastoris | recombinant expressed in Pichia pastoris | recombinant - |
| form lyophilized | form lyophilized powder | form lyophilized powder | form lyophilized (salt-free) |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| manufacturer/tradename Roche | manufacturer/tradename - | manufacturer/tradename - | manufacturer/tradename Roche |
signalword
Danger
target_organs
Respiratory system
Tárolási osztály
11 - Combustible Solids
wgk
WGK 1
flash_point_f
does not flash
flash_point_c
does not flash
hcodes
Hazard Classifications
Eye Irrit. 2 - Met. Corr. 1 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
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Kapcsolódó tartalom
Alexander Schmidt et al.
Methods in molecular biology (Clifton, N.J.), 492, 21-38 (2009-02-26)
Proteomics may be defined as the systematic analysis of proteins expressed in a given organism (Electrophoresis 16:1090-1094, 1995). Important technical innovations in mass spectrometry (MS), protein identification methods, and database annotation, over the past decade, now make it possible to
A Acera et al.
Eye (London, England), 25(9), 1225-1233 (2011-06-28)
To analyze tear protein profile variations in patients with keratoconus (KC) and to compare them with those of control subjects. Tears from 12 normal subjects and 12 patients with KC were analyzed by two-dimensional gel electrophoresis (2-DE) and liquid chromatography-mass
Globális kereskedelmi áruazonosító szám
| Cikkszám | GTIN |
|---|---|
| 3708969001 | 04061831833713 |
| 3708985001 | 04061831833720 |