02065
Adenosine 5′-triphosphate, immobilized on Agarose 4B
suitable for affinity chromatography, powder (lyophilized)
Sinónimos:
5′-ATP-agarose 4B
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Form:
powder (lyophilized)
Storage temp.:
−20°C
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powder (lyophilized)
contains
60% lactose as stabilizer
technique(s)
affinity chromatography: suitable
capacity
≥1 μmol/mL, packed gel capacity (5′-ATP)(bound by a C6-spacer to C-8 of ATP)
storage temp.
−20°C
Quality Level
Categorías relacionadas
General description
The lactose-stabilizer must be removed prior to use by washing the gel onto filter with water or buffer.
Application
Adenosine 5′-triphosphate, immobilized on Agarose 4B (5′-ATP-agarose 4B) is intended for use in affinity chromatography. 5′-ATP-agarose 4B has been shown to bind enzymes with affinity to 5′-ATP. 5′-ATP-agarose 4B may be considered for used with enzymes that bind to other ATP-agarose and sepharose affinity media or beads.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Other Notes
Purification of cofactor-dependent enzymes by affinity chromatography.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Purification of cofactor-dependent enzymes by affinity chromatography.
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Analytical biochemistry, 77(1), 90-102 (1977-01-01)
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(-)-Epigallocatechin-3-gallate (EGCG), a major component of green tea, protects against certain types of cancers, although the mechanism has not yet been determined. It was previously demonstrated that EGCG blocks aryl hydrocarbon receptor (AhR)-mediated transcription induced by the potent carcinogen 2,3,7,8-tetrachlorodibenzo-p-dioxin
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G A Nevinsky et al.
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This article presents evidence that protein kinase activity is an intrinsic property of secretory immunoglobulin A (sIgA) from milk of healthy human mothers. Polyclonal sIgA was purified by sequential chromatography on protein A-Sepharose, DEAE-cellulose, and gel filtration on Toyopearl HW-55
E Roggen et al.
European journal of biochemistry, 147(2), 225-232 (1985-03-01)
Poly(A) polymerase has been purified to near homogeneity from the cytoplasm of Artemia salina cryptobiotic gastrulae by ion-exchange chromatography on DEAE-cellulose, DEAE-Sepharose CL-6B and phosphocellulose P11, gel filtration on CL-Sepharose 6B, affinity chromatography on poly(A)-Sepharose 4B and ATP-agarose. The enzyme
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