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Merck
CN

G7550

Sigma-Aldrich

Sephadex® G-75

Superfine

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About This Item

CAS号:
MDL编号:
UNSPSC代码:
23151817
NACRES:
NA.56

质量水平

技术

buffer exchange: suitable

基质活性基团

phase

溶胀

1 g swells to 12-15 mL

珠子尺寸

20-50 μm

应用

life science and biopharma

相容性

Cytiva

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相关类别

一般描述

Sephadex® G-75是成熟的凝胶过滤介质,用于分子量为>80,000的大生物分子的脱盐和缓冲液交换。
Sephadex®是葡聚糖与环氧氯丙烷交联制备的凝胶过滤介质。不同类型的Sephadex的交联度不同,因此其溶胀程度和分子分级范围也不同。Sephadex® G-75用于较大的分子。

应用

Sephadex® G-75是凝胶过滤介质,用于凝胶过滤色谱和蛋白质色谱。它已用于脱盐过程,以研究壳聚糖纳米颗粒(CSNPs)中L-天冬酰胺酶II(ASNase II)的生产、纯化和固定化。

法律信息

Sephadex is a registered trademark of Cytiva
Sepharose is a trademark of Cytiva

替代产品

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


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John G Vontas et al.
The Biochemical journal, 362(Pt 2), 329-337 (2002-02-21)
A novel glutathione S-transferase (GST)-based pyrethroid resistance mechanism was recently identified in Nilaparvata lugens [Vontas, Small and Hemingway (2001) Biochem. J. 357, 65-72]. To determine the nature of GSTs involved in conferring this resistance, the GSTs from resistant and susceptible
Sofia R Pauleta et al.
Biochemistry, 43(35), 11214-11225 (2004-09-16)
The gene for pseudoazurin was isolated from Paracoccus pantotrophus LMD 52.44 and expressed in a heterologous system with a yield of 54.3 mg of pure protein per liter of culture. The gene and protein were shown to be identical to
Engineering a Disulfide Bond in Recombinant Manganese Peroxidase Results in Increased Thermostability
Reading, N.S., and Aust, S.D.
Biotechnol. Progress, 16(3), 326-333 (2000)
L Shilpa Satheesh et al.
Indian journal of experimental biology, 49(5), 366-374 (2011-05-28)
Antimicrobial activity of protease inhibitor isolated from Coccinia grandis (L.) Voigt. has been reported. A 14.3 kDa protease inhibitor (PI) was isolated and purified to homogeneity by ammonium sulfate precipitation (20-85% saturation), sephadex G-75, DEAE sepharose column and trypsin-sepharose affinity
Fatah Chérifi et al.
The protein journal, 29(7), 466-474 (2010-08-19)
A procoagulant metalloproteinase called CCSV-MPase was purified from C. cerastes venom by successive chromatographic methods starting with gel-filtration through Sephadex G-75; ion-exchange DEAE-Cellulose A-50; affinity chromatography on Benzamidine Sepharose 6B and RP-HPLC on a C8 column. CCSV-MPase has been isolated

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