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애플리케이션
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.
물리적 형태
Suspension in 0.5 M NaCl containing preservative
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
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시험 성적서(COA)
Lot/Batch Number
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
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
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
Koji Iwamoto et al.
Plant physiology, 133(2), 893-900 (2003-09-16)
Mannitol-1-phosphate (M1P) dehydrogenase (M1PDH; EC 1.1.1.17), an enzyme catalyzing the reduction of Fru-6-phosphate (F6P) to M1P in algal mannitol biosynthesis, was purified to homogeneity from a cell homogenate of the eulittoral red alga Caloglossa continua (Okamura) King et Puttock. The
P De Prada et al.
Applied and environmental microbiology, 63(7), 2928-2931 (1997-07-01)
Two extracellular, heat-labile alkaline phosphatases were purified from a psychrophilic Arthrobacter isolate, D10. The enzymes were active over different pH ranges, used distinct substrates, and had different kinetic properties. Each enzyme reacted specifically to its own antibody during immunoblot analysis.
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