biological source
plant
type
Type 3000-CL
form
saline suspension
extent of labeling
≥3 μmol per mL
technique(s)
affinity chromatography: suitable
matrix
cross-linked 4% beaded agarose
suitability
suitable for chromatography
storage temp.
2-8°C
Quality Level
Application
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.
Physical form
Suspension in 0.5 M NaCl containing preservative
存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Removing trace fluorescent contaminants from GroEL preparations.
F Weber
Methods in molecular biology (Clifton, N.J.), 140, 63-64 (2001-08-04)
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.
A Y Strongin et al.
The Journal of biological chemistry, 270(10), 5331-5338 (1995-03-10)
Matrix metalloproteases are secreted by mammalian cells as zymogens and, upon activation, initiate tissue remodeling by proteolytic degradation of collagens and proteoglycans. Activation of the secreted proenzymes and interaction with their specific inhibitors determine the net enzymatic activity in the
A Craxton et al.
The Biochemical journal, 305 ( Pt 2), 491-498 (1995-01-15)
A multiple inositol polyphosphate phosphatase (formerly known as inositol 1,3,4,5-tetrakisphosphate 3-phosphatase) was purified approx. 22,000-fold from rat liver. The final preparation migrated on SDS/PAGE as a doublet with a mean apparent molecular mass of 47 kDa. Upon size-exclusion chromatography, the
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