表单
saline suspension
标记范围
2-10 μmol per mL
基质
Cross-linked 4% beaded agarose
基质活化
cyanogen bromide
基质附着
amino
基质隔离区
1 atom
储存温度
2-8°C
应用
L-Phenylalanine-agarose is used in protein chromatography, affinity chromatography and amino acid resins. L-Phenylalanine-agarose has been used to purify and characterize a cysteine protease of Fasciola gigantica adult worms as well as to purify a proteolytic enzyme of the liver fluke Fasciola species.
外形
Suspension in 2.0 M NaCl containing preservative
储存分类代码
12 - Non Combustible Liquids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
新产品
此项目有
T Aoki et al.
Molecular and biochemical parasitology, 8(2), 89-97 (1983-06-01)
A proteolytic enzyme of the liver fluke Fasciola sp. was purified as described previously by ammonium sulfate fractionation, gel filtration on Sephadex G-200 column and L-phenylalanine-agarose chromatography. Leupeptin, a peptide aldehyde of microbial origin, competitively inhibited the enzyme activity with
H R Onishi et al.
The Journal of biological chemistry, 254(23), 11943-11952 (1979-12-10)
The nonspecific alkaline phosphatase of yeast (Saccharomyces strain 1710) has been purified by ion exchange, hydrophobic, and affinity chromatography. This vacuolar enzyme has a molecular weight of 130,000 and is composed of subunits (probably of 66,000 molecular weight). It also
B O Fagbemi et al.
Veterinary parasitology, 43(3-4), 223-232 (1992-07-01)
A 26-28 kDa protease was isolated from Fasciola gigantica adult worms by a two-stage purification process of column chromatography in a Sephacryl S-200 column and affinity chromatography in an L-phenylalanine-agarose column. This protease is a cysteine (thiol) proteinase with an
K H Lau et al.
The Journal of biological chemistry, 260(8), 4653-4660 (1985-04-25)
A partially purified bovine cortical bone acid phosphatase, which shared similar characteristics with a class of acid phosphatase known as tartrate-resistant acid phosphatase, was found to dephosphorylate phosphotyrosine and phosphotyrosyl proteins, with little activity toward other phosphoamino acids or phosphoseryl
J F Geissler et al.
Journal of bacteriology, 170(4), 1709-1714 (1988-04-01)
A soluble benzoate-coenzyme A (CoA) ligase was purified from the phototrophic bacterium Rhodopseudomonas palustris. Synthesis of the enzyme was induced when cells were grown anaerobically in light with benzoate as the sole carbon source. Purification by chromatography successively on hydroxylapatite
我们的科学家团队拥有各种研究领域经验，包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持