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O6127

Sigma-Aldrich

Octyl–Agarose

saline suspension

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About This Item

MDL number:
UNSPSC Code:
23151817
NACRES:
NA.56

form

saline suspension

matrix activation

epoxy

matrix attachment

amino

matrix spacer

12 atoms

capacity

≥10 mg/mL binding capacity (human serum albumin)
≥3 mg/mL binding capacity (β-lactoglobulin)

storage temp.

2-8°C

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Application

Octyl agarose is used in protein chromatography, affinity chromatography and hydrophobic interactions. Octyl agarose has been used to immobilize lipases from Penicillium camembertii (Lipase G) and Aspergillus niger.

Physical form

Suspension in 0.5 M NaCl containing preservative

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


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Purification and quantification of Saccharomyces cerevisiae cytochrome P450.
I Stansfield et al.
Methods in molecular biology (Clifton, N.J.), 53, 355-366 (1996-01-01)
M F Hammer et al.
Plant physiology, 113(1), 227-233 (1997-01-01)
A protein phosphatase was purified from the stroma of Pea (Pisum sativum L.) chloroplasts that is capable of dephosphorylating synthetic phosphopeptides. Following chromatographic purification of greater than 400-fold, two-dimensional electrophoresis indicated that the stromal protein phosphatase is a 29-kD protein.
H. P. Guan et al.
Plant physiology, 102(4), 1269-1273 (1993-08-01)
The multiple forms of branching enzyme (BE) from developing maize (Zea mays) endosperm were purified by modification of previous procedures such that amylase activity could be eliminated completely from the BE preparation. Three distinct assays for BE activity (phosphorylase a
S M Moghimi
Biochimica et biophysica acta, 1590(1-3), 131-139 (2002-06-14)
A two-step approach is described to chemically camouflage the inert surface of model polystyrene nanospheres of 60 nm in diameter against recognition by the body's defenses. The first step was based on the strong protein adsorbing potency of polystyrene, and
Annalisa Tassoni et al.
Plant physiology, 128(4), 1303-1312 (2002-04-16)
Polyamine-binding proteins have been identified in a wide range of organisms, including mammals, yeasts, and bacteria. In this work, we have investigated specific spermidine binding to plant membrane proteins purified from microsomes of etiolated maize (Zea mays) coleoptiles. In the

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