form
aqueous ethanol suspension
matrix active group
, —CH2-SO3-
particle size
45-165 μm (wet)
pore size
~4,000,000 Da exclusion limit
capacity
180-250 μeq/mL, gel
storage temp.
2-8°C
Quality Level
Application
SP 琼脂糖凝胶 ™ 用于蛋白质色谱、离子交换色谱和阳离子交换介质。SP琼脂糖凝胶™ 已被用于姜科植物根茎中抑制蛋白和多肽的研究以及大豆碱性 7S 球蛋白亚基异质性和分子进化的研究。此外，SP 琼脂糖凝胶 ™ 还有助于推动壳寡糖制备的工业应用。
Physical form
悬浮于0.2 M乙酸钠和20%乙醇中
Legal Information
Sepharose is a trademark of Cytiva
signalword
Warning
hcodes
Hazard Classifications
Flam. Liq. 3
存储类别
3 - Flammable liquids
wgk
WGK 1
flash_point_f
100.4 - 109.4 °F
flash_point_c
38 - 43 °C
法规信息
新产品
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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
C Y Cheng et al.
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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
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
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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