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S1799

Sigma-Aldrich

SP Sepharose™

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

Synonym(s):

Sulfopropyl-Sepharose™

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About This Item

MDL number:
MFCD00148494
UNSPSC Code:
47101511
NACRES:
NA.56
Pricing and availability is not currently available.

Quality Level

200

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

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This Item
SPC50120SPC25120CCF100
SP Sepharose™ Fast Flow, aqueous ethanol suspension, 45-165 μm (wet), exclusion limit ~4,000,000 Da

S1799

SP Sepharose™

SP Sephadex® C-50 sodium form

SPC50120

SP Sephadex® C-50 sodium form

SP Sephadex®

SPC25120

SP Sephadex®

CM Sepharose™ Fast Flow

CCF100

CM Sepharose™

pore size

~4,000,000 Da exclusion limit

pore size

200,000 exclusion limit (av. mol. wt.)

pore size

-

pore size

4,000,000 exclusion limit (av. mol. wt.)

particle size

45-165 μm (wet)

particle size

-

particle size

-

particle size

45-165 μm (wet bead)

matrix active group

, —CH2-SO3-

matrix active group

-

matrix active group

-

matrix active group

-

form

aqueous ethanol suspension

form

-

form

-

form

suspension

capacity

180-250 μeq/mL, gel

capacity

2.0-2.8 meq/g ion exchange capacity

capacity

2.0-2.6 meq/g

capacity

90-130 μeq/mL(gel basis)

storage temp.

2-8°C

storage temp.

-

storage temp.

-

storage temp.

2-8°C

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.

Physical form

Suspension in 0.2 M sodium acetate and 20% ethanol

Legal Information

Sepharose is a trademark of Cytiva

pictograms

Flame
GHS02

signalword

Warning

hcodes

H226

Hazard Classifications

Flam. Liq. 3

Storage Class

3 - Flammable liquids

wgk_germany

WGK 1

flash_point_f

100.4 - 109.4 °F

flash_point_c

38 - 43 °C

  • Specification Sheet

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    Certificates of Analysis (COA)

    Lot/Batch Number
    MKCN6271
    MKBX7639V
    MKCL9928
    MKCK1423
    MKCJ9889

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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
    View All Related Papers

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