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Merck

A1271

Adenosine 5′-monophosphate–Agarose

lyophilized powder

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UNSPSC Code:
41106500
eCl@ss:
32160414
PubChem Substance ID:
NACRES:
NA.56
MDL number:
Biological source:
plant (Sea weed)
Form:
lyophilized powder
Storage temp.:
−20°C

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biological source

plant (Sea weed)

Quality Level

form

lyophilized powder

extent of labeling

1-5 μmol per mL

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

C-8

matrix spacer

9 atoms

storage temp.

−20°C

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1 of 4

Este artículo
A3515A6888A2810
biological source

plant (Sea weed)

biological source

-

biological source

-

biological source

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

form

lyophilized powder

form

lyophilized powder

form

aqueous glycerol suspension

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

extent of labeling

1-5 μmol per mL

extent of labeling

1-5 μmol per mL

extent of labeling

≥1 μmol per mL

extent of labeling

1-5 μmol per mL

matrix

cross-linked 4% beaded agarose

matrix

cross-linked 4% beaded agarose

matrix

cross-linked 4% beaded agarose

matrix

cross-linked 4% beaded agarose

Application

Adenosine 5′-monophosphate Agarose (5′-AMP agarose) has been used in affinity chromatography to isolate β and gamma glutamate decarboxylase, which is important for controlling gamma-aminobutyric acid (GABA) synthesis in brain.

Physical form

Lyophilized powder stabilized with lactose

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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S M Pettit et al.
Clinical chemistry, 27(1), 88-93 (1981-01-01)
We present a method for preparing human liver lactate dehydrogenase (L-lactate:NAD+ oxidoreductase; EC 1.1.1.27) isoenzyme-5 by sequential ion-exchange chromatography, general-ligand (AMP analog) affinity chromatography, and preparative isoelectric focusing. The yield ws 40%, with a 493-fold purification. The final specific activity
D W Parkin
The Journal of biological chemistry, 271(36), 21713-21719 (1996-09-06)
Trypanosomes have no de novo purine biosynthesis and thus depend upon salvage pathways to obtain purines for their metabolic pathways and for the biosynthesis of nucleic acids. An inosine-adenosine-guanosine preferring nucleoside hydrolase (IAG-nucleoside hydrolase) from the African trypanosome Trypanosoma brucei
D M Brown et al.
European journal of biochemistry, 241(1), 155-161 (1996-10-01)
We describe the purification of a H2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis. The enzyme is a monomeric flavoprotein containing flavin adenine dinucleotide in a 1:1 molar ratio with the polypeptide. The NADH oxidase has an apparent molecular
S J Wu et al.
Journal of neurochemistry, 42(6), 1607-1612 (1984-06-01)
The interactions of two forms of porcine brain glutamate decarboxylase (beta-GAD and gamma-GAD) with the effector ATP were studied by affinity chromatography. A third form, alpha-GAD, was only slightly retarded by the affinity matrix and was eluted in the buffer
M Kato et al.
Plant physiology, 120(2), 579-586 (1999-06-11)
Caffeine synthase (CS), the S-adenosylmethionine-dependent N-methyltransferase involved in the last two steps of caffeine biosynthesis, was extracted from young tea (Camellia sinensis) leaves; the CS was purified 520-fold to apparent homogeneity and a final specific activity of 5.7 nkat mg-1

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SKUGTIN
A1271-1ML04061837769276
A1271-5ML04061837769283

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