Összes fotó(1)
Fontos dokumentumok
10634425001
Roche
n-Octylglucoside
non-ionic
Szinonimák:
Octyl β-D-glucopyranoside, n-Octyl glucoside, OGP
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
Tapasztalati képlet (Hill-képlet):
C14H28O6
CAS-szám:
Molekulatömeg:
292.37
Beilstein:
84118
MDL-szám:
UNSPSC kód:
12352200
PubChem Substance ID:
Javasolt termékek
Teszt
99% (GC)
molekulatömeg
micellar avg mol wt 25,000
292.4
kiszerelés
pkg of 10 g
gyártó/kereskedő neve
Roche
aggregált szám
84
technika/technikák
dialysis: suitable
CMC
20-25 mM (20-25°C)
átmeneti hőmérséklet
cloud point >100 °C
kiszállítva
ambient
SMILES string
CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O
InChI
1S/C14H28O6/c1-2-3-4-5-6-7-8-19-14-13(18)12(17)11(16)10(9-15)20-14/h10-18H,2-9H2,1H3/t10-,11-,12+,13-,14-/m1/s1
Nemzetközi kémiai azonosító kulcs
HEGSGKPQLMEBJL-RKQHYHRCSA-N
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Általános leírás
1-O-n-Octyl-β-D-glucopyranoside, octylglucoside, is a detergent with an octyl chain as hydrophobic residue and glucose as hydrophilic part. It is a non-ionic, dialyzable, mild and non-denaturing detergent which is used for the solubilization, isolation and reconstitution of membrane proteins.
Alkalmazás
N-Octylglucoside has been shown to increase the resolution of proteins in 2D gels. It is a mild and non-denaturing detergent for the solubilization and reconstitution of membrane proteins. N-Octylglucoside is easily removed by dialysis. N-Octylglucoside has been used in mass spectrometric immunoassay to homogenize MALDI (matrix assisted laser desorption/ionization) matrix draw and elution.
Non-ionic, dialyzable detergent for the solubilization and isolation of membrane proteins. Has been shown to increase the resolution of proteins in 2D gels.
Minőség
Purity: 99% (from C), homogeneous (GC)
Ease of removal*: ++
CMC**: 14.5 mM at +25°C
Formula: C14H28O6
Ease of removal*: ++
CMC**: 14.5 mM at +25°C
Formula: C14H28O6
Elkészítési megjegyzés
Working concentration: 46 mM
Working solution: Solubility: > 50% (w/v) in double-dist. water, Tris-HCl 0.05 mol/l; pH7.4 or K-phosphate buffer 0.1 mol/l, pH 7.0 at 25 °C.
Storage conditions (working solution): Stability in Solution
A stock solution is stable at 2 to 8 °C for approx. 3 days. We would expect a long term stability of 6-12 months if stored frozen in portions at -15 to -25 °C, provided bacterial contamination is avoided.
Working solution: Solubility: > 50% (w/v) in double-dist. water, Tris-HCl 0.05 mol/l; pH7.4 or K-phosphate buffer 0.1 mol/l, pH 7.0 at 25 °C.
Storage conditions (working solution): Stability in Solution
A stock solution is stable at 2 to 8 °C for approx. 3 days. We would expect a long term stability of 6-12 months if stored frozen in portions at -15 to -25 °C, provided bacterial contamination is avoided.
Tárolás és stabilitás
Store at 15 to 25 °C. (Store dry!)
Egyéb megjegyzések
For life science research only. Not for use in diagnostic procedures.
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 1
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
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Az ügyfelek ezeket is megtekintették
W A Petri et al.
The Journal of biological chemistry, 254(11), 4313-4316 (1979-06-10)
The glycoprotein of vesicular stomatitis (VS) virus was selectively liberated from the virion membrane by the dialyzable nonionic detergent, beta-D-octylglucoside. The isolated viral glycoprotein could be rendered virtually free of phospholipid and detergent, under which conditions it formed tail-to-tail glycoprotein
Howard R Mellor et al.
The Biochemical journal, 374(Pt 2), 307-314 (2003-05-29)
The N-alkyl moiety of N-alkylated imino sugars is crucial for therapeutic activities of these compounds as inhibitors of glycosphingolipid (GSL) biosynthesis and as antivirals. The improved potency afforded by a long N-alkyl moiety is coincident with increased compound-induced cytotoxicity. Therefore
Olgica Trenchevska et al.
Journal of proteome research, 9(11), 5969-5973 (2010-09-09)
Protein biomarkers are essential in assessing pathogenic processes. The impetus for finding new biomarkers has been accelerated by the arrival of the "omics" technologies. However, equally important is the rediscovery of existing biomarkers with these new approaches as novel variants
Olgica Trenchevska et al.
Proteome science, 9(1), 19-19 (2011-04-12)
Post-translational modifications and genetic variations give rise to protein variants that significantly increase the complexity of the human proteome. Modified proteins also play an important role in biological processes. While sandwich immunoassays are routinely used to determine protein concentrations, they
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