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表单
saline suspension
标记范围
≥6 mg per mL
基质
crosslinked 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
p-Aminomethylbenzenesulfonamide is an agarose in saline suspension that can be used in affinity chromatography, protein chromatography and specialty resins. p-Aminomethylbenzenesulfonamide has been used in studies assessing inhibition of mitochondrial carbonic anhydrase and ureagenesis.
外形
Suspension in 0.5 M NaCl containing preservative.
B E Alber et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(15), 6909-6913 (1994-07-19)
Carbonic anhydrase (CA) from acetate-grown Methanosarcina thermophila was purified > 10,000-fold (22% recovery) to apparent homogeneity with a specific activity of 4872 units/mg. The estimated native molecular mass of the enzyme is 84 kDa based on gel filtration chromatography. SDS/PAGE
L G Puskás et al.
Microbiology (Reading, England), 146 ( Pt 11), 2957-2966 (2000-11-07)
Intact cells of the purple non-sulfur bacterium Rhodopseudomonas palustris growing anaerobically, but not aerobically, contain carbonic anhydrase (CA) activity. The native enzyme was purified >2000-fold to apparent homogeneity and found to be a dimer with an estimated molecular mass of
S Sender et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 47(1), 43-50 (1998-12-19)
Flounders Platichthys flesus were investigated with respect to isolation, purification, and cellular localization of carbonic anhydrase (CA) in the respiratory system. CA was purified from gills and erythrocytes and was shown to exclusively represent a soluble enzyme with an apparent
B Ulmasov et al.
Proceedings of the National Academy of Sciences of the United States of America, 97(26), 14212-14217 (2000-12-20)
Carbonic anhydrase XII (CA XII) is a transmembrane glycoprotein with an active extracellular CA domain that is overexpressed on cell surfaces of certain cancers. Its expression has been linked to tumor invasiveness. To characterize its catalytic properties, we purified recombinant
D K Srivastava et al.
Journal of the American Chemical Society, 129(17), 5528-5537 (2007-04-05)
Despite the similarity in the active site pockets of carbonic anhydrase (CA) isozymes I and II, the binding affinities of benzenesulfonamide inhibitors are invariably higher with CA II as compared to CA I. To explore the structural basis of this
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