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02065

Sigma-Aldrich

Adenosine 5′-triphosphate, immobilized on Agarose 4B

suitable for affinity chromatography, powder (lyophilized)

Synonym(s):

5′-ATP-agarose 4B

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1 ML
$161.16
5 ML
$3,382.00

About This Item

UNSPSC Code:
41106305
eCl@ss:
32160414
PubChem Substance ID:
NACRES:
NA.51

$161.16

List Price$170.00Save 5%
Web-Only Promotion

Available to ship onApril 30, 2025Details


Request a Bulk Order

form

powder (lyophilized)

Quality Level

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

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[1][2].

Storage Class

11 - Combustible Solids

wgk_germany

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.
Lee C-Y et al.
Analytical biochemistry, 77(1), 90-102 (1977-01-01)
Zhengyu Yin et al.
Biochemistry, 48(2), 336-345 (2008-12-31)
(-)-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
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
Cheng-Zhu Wu et al.
Archives of pharmacal research, 33(12), 1997-2001 (2010-12-31)
The molecular chaperone heat shock protein 90 (Hsp90) is responsible for maintaining the correct folding and stability of many signaling proteins. It is a promising target of cancer therapeutics and several other diseases, including neurodegenerative disease, nerve injuries, inflammation, and
ATP-and dATP-substituted agaroses and the purification of ribonucleotide reductases.
O Berglund et al.
Methods in enzymology, 34, 253-261 (1974-01-01)

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