应用
Reactive Red 120-agarose is used in affinity chromatography, protein chromatography and dye resins. Reactive Red 120-agarose has been used to study wheat quality breeding as well as to provide strong evidence that purified human P-glycoprotein (Pgp) functions as an ATP-dependent drug transporter.
外形
Suspension in 0.5 M NaCl containing preservative
储存分类代码
10 - Combustible liquids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
S V Ambudkar et al.
Methods in enzymology, 292, 492-504 (1998-08-26)
Human Pgp from the vinblastine-resistant cell line, KB-V1, can be purified by sequential conventional chromatography on DEAE-sepharose CL-6B resin followed by a wheat germ agglutinin column. By including glycerol (osmolyte protectant) and lipid during the solubilization and chromatography procedures most
Gregory A Bannikov et al.
American journal of veterinary research, 68(9), 995-1004 (2007-09-04)
To characterize and purify covalent complexes of matrix metalloproteinase-9 (MMP-9) and haptoglobin released by bovine granulocytes in vitro. Blood samples obtained from healthy cows and cows with acute and chronic inflammation to obtain WBCs and sera. WBCs were isolated by
P C Larosa et al.
Plant physiology, 96(1), 245-250 (1991-05-01)
Tobacco (Nicotiana tabacum L. var Wisconsin 38) cells that are adapted to 428 millimolar NaCl accumulate proline mainly due to increased synthesis from glutamate. These cells were used to evaluate the possible role of Delta(1)-pyrroline-5-carboxylate reductase in the regulation of
S Takeda et al.
Journal of biochemistry, 114(5), 684-690 (1993-11-01)
A particulate fraction consisting of heavy organelles such as nuclei and mitochondria was prepared from Ehrlich ascites tumor cells. From this fraction we have purified a GTP-binding protein with a molecular mass of 33 kDa (MTG33) by guanidine hydrochloride extraction
C F Barroga et al.
Protein science : a publication of the Protein Society, 5(6), 1093-1099 (1996-06-01)
The nucleotide-binding component of the high-affinity ribose transport system of Escherichia coli, RbsA, was overproduced from a T7-7 expression vector, and the protein was purified. Biochemical analyses of the purified protein indicated that the ATP analogues, 5'-FSBA and 8-azido ATP
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