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S1799

Sigma-Aldrich

SP Sepharose™

Fast Flow, aqueous ethanol suspension, 45-165 μm (wet), exclusion limit ~4,000,000 Da

Sinonimo/i:

Sulfopropyl-Sepharose™

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About This Item

Numero MDL:
MFCD00148494
Codice UNSPSC:
47101511
NACRES:
NA.56

Livello qualitativo

200

Forma fisica

aqueous ethanol suspension

Gruppo funzionale matrice

, —CH2-SO3-

Dimensione particelle

45-165 μm (wet)

Dimensione pori

~4,000,000 Da exclusion limit

Capacità

180-250 μeq/mL, gel

Temperatura di conservazione

2-8°C

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Applicazioni

SP Sepharose™ is used in protein chromatography, ion exchange chromatography and cation exchange media. SP Sepharose™ has been used to study inhibitory proteins and peptides from the rhizomes of zingiberaceae plants as well as to study the subunit heterogeneity and molecular evolution of soybean basic 7S globulin. SP Sepharose™ has also assisted with advancing industrial applications of preparation of chitosan oligosaccharides.

Stato fisico

Suspension in 0.2 M sodium acetate and 20% ethanol

Note legali

Sepharose is a trademark of Cytiva

Pittogrammi

Flame
GHS02

Avvertenze

Warning

Indicazioni di pericolo

H226

Classi di pericolo

Flam. Liq. 3

Codice della classe di stoccaggio

3 - Flammable liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

100.4 - 109.4 °F

Punto d’infiammabilità (°C)

38 - 43 °C

Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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Surachai Supattapone et al.
Methods in molecular biology (Clifton, N.J.), 459, 117-130 (2008-06-26)
The infectious agents of prion diseases are unorthodox, and they seem to be composed primarily of a misfolded glycoprotein called the prion protein (PrP). Replication of prion infectivity is associated with the conversion of PrP from its normal, cellular form
C Y Cheng et al.
Biotechnology and applied biochemistry, 32 ( Pt 3), 197-203 (2000-12-15)
A chitosan-degrading fungus, designated Aspergillus sp. Y2K, was isolated from soil. The micro-organism was used for producing chitosanase (EC 3.2.1.132) in a minimal medium containing chitosan as the sole carbon source. The induced chitosanase was purified to homogeneity from the
Andrei D Shutov et al.
Bioscience, biotechnology, and biochemistry, 74(8), 1631-1634 (2010-08-12)
Basic 7S globulin, a cysteine-rich protein from soybean seeds, consists of subunits containing 27 kD and 16 kD chains linked by disulfide bonding. Three differently sized subunits of the basic 7S globulin were detected and partially separated by SP Sepharose
Maneerat Yodjun et al.
Applied biochemistry and biotechnology, 166(8), 2037-2050 (2012-03-07)
Ammonium sulphate cut protein extracts, and their pepsin hydrolysates, from the rhizomes of 15 plants in the Zingiberaceae family were screened for their in vitro angiotensin I-converting enzyme inhibitory (ACEI) activity. The protein extract from Zingiber ottensii had the highest
James C Geoghegan et al.
The Journal of biological chemistry, 282(50), 36341-36353 (2007-10-18)
The central pathogenic event of prion disease is the conformational conversion of a host protein, PrPC, into a pathogenic isoform, PrPSc. We previously showed that the protein misfolding cyclic amplification (PMCA) technique can be used to form infectious prion molecules
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