DCL6B100
DEAE - 琼脂糖凝胶™
CL-6B
别名:
二乙氨乙基 - 琼脂糖凝胶™
产品名称
DEAE - 琼脂糖凝胶™, CL-6B
form
suspension
technique(s)
affinity chromatography: suitable
matrix
6% cross-linked agarose
bead size
45-165 μm
pore size
~4,000,000 Da exclusion limit
pH
3—12
capacity
130-170 μeq/mL binding capacity (gel volume)(gel volume)
Quality Level
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Application
DEAE-Sepharose ® 用于亲和层析、蛋白层析和离子交换层析。DEAE-Sepharose ™ 已被用于研究人类疾病的发病机制和开发检测艰难梭菌致病菌株毒素的新方法 。
General description
DCL6B100-500 mL 更新后的产品编号为 GE17-0710-01
Legal Information
DEAE-Sepharose is a registered trademark of Cytiva
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
ppe
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
法规信息
危险化学品
此项目有
R K Sinha et al.
Vaccine, 15(6-7), 689-699 (1997-04-01)
Six different secretory proteins of molecular weights (15, 26, 30, 41, 55 and 70 kDa) were isolated from 8-day-old culture filtrate of Mycobacterium tuberculosis H37Ra using different column chromatography techniques. These proteins were further examined for their ability to induce
I Yu Bakunina et al.
Biochemistry. Biokhimiia, 67(6), 689-695 (2002-07-20)
An alpha-N-acetylgalactosaminidase IV able to remove blood type specificity of human A(II)-erythrocytes and not effecting B(III)-erythrocytes was isolated from the marine bacterium Arenibacter latericius KMM 426T. The alpha-N-acetylgalactosaminidase IV preparation exhibits high activity during inhibition of hemagglutination with blood group
M A Heine et al.
Molecular biology of the cell, 4(11), 1189-1204 (1993-11-01)
Epitope-tagged Xenopus nucleolin was expressed in Escherichia coli cells and in Xenopus oocytes either as a full-length wild-type protein or as a truncation that lacked the distinctive carboxy glycine/arginine-rich (GAR) domain. Both full-length and truncated versions of nucleolin were tagged
J J Wheeler et al.
Gene therapy, 6(2), 271-281 (1999-08-06)
A detergent dialysis procedure is described which allows encapsulation of plasmid DNA within a lipid envelope, where the resulting particle is stabilized in aqueous media by the presence of a poly(ethyleneglycol) (PEG) coating. These 'stabilized plasmid-lipid particles' (SPLP) exhibit an
M L Zapp et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(17), 7734-7738 (1991-09-01)
The Rev protein of human immunodeficiency virus type 1 is a sequence-specific RNA binding protein that is essential for viral replication. Here we present evidence that Rev is a stable oligomer both in vitro and in vivo. Analysis of Rev
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