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S1799

Sigma-Aldrich

SP Sepharose™

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

Synonyme(s) :

Sulfopropyl-Sepharose™

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About This Item

Numéro MDL:
MFCD00148494
Code UNSPSC :
47101511
Nomenclature NACRES :
NA.56

Niveau de qualité

200

Forme

aqueous ethanol suspension

Groupe de la matrice active

, —CH2-SO3-

Taille des particules

45-165 μm (wet)

Dimension de pores

~4,000,000 Da exclusion limit

Capacité

180-250 μeq/mL, gel

Température de stockage

2-8°C

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Application

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.

Forme physique

Suspension in 0.2 M sodium acetate and 20% ethanol

Informations légales

Sepharose is a trademark of Cytiva

Pictogrammes

Flame
GHS02

Mention d'avertissement

Warning

Mentions de danger

H226

Classification des risques

Flam. Liq. 3

Code de la classe de stockage

3 - Flammable liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

100.4 - 109.4 °F

Point d'éclair (°C)

38 - 43 °C

Certificats d'analyse (COA)

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Andreas Güntert et al.
Journal of Alzheimer's disease : JAD, 21(2), 585-596 (2010-06-24)
Alzheimer's disease (AD) is a progressive neurodegenerative disorder where definite diagnosis can only be made postmortem, and for which the most promising peripheral markers of disease state and severity have been found in the cerebrospinal fluid. However, recent results suggest
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
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
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
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
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