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02065

Sigma-Aldrich

Adenosine 5′-triphosphate, immobilized on Agarose 4B

suitable for affinity chromatography, powder (lyophilized)

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Synonym(s):
5′-ATP-agarose 4B
UNSPSC Code:
41106305
eCl@ss:
32160414
PubChem Substance ID:
NACRES:
NA.51

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.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
G A Nevinsky et al.
Applied biochemistry and biotechnology, 75(1), 77-91 (1999-04-24)
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
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)
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

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