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Merck
CN

A1271

腺苷5-单磷酸-琼脂糖

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)

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

Quality Level

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相关类别

Application

腺苷5′-单磷酸琼脂糖(5′-AMP琼脂糖)已被用于亲和色谱以分离β和γ-谷氨酸脱羧酶,这对于控制大脑中的γ-氨基丁酸(GABA)合成很重要。

Physical form

用乳糖稳定化的冻干粉

存储类别

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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分析证书(COA)

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S K Lee et al.
FEBS letters, 316(3), 261-263 (1993-02-01)
The mosquito homolog of mammalian DNA polymerase epsilon, formerly known as a proliferating cell nuclear antigen (PCNA)-independent form of DNA polymerase delta, has been purified from mosquito larval extracts. The polymerase epsilon was separated from DNA polymerase alpha by chromatography
C D Murphy et al.
Applied and environmental microbiology, 67(10), 4919-4921 (2001-09-26)
Streptomyces cattleya is unusual in that it produces fluoroacetate and 4-fluorothreonine as secondary metabolites. We now report the isolation of an NAD(+)-dependent fluoroacetaldehyde dehydrogenase from S. cattleya that mediates the oxidation of fluoroacetaldehyde to fluoroacetate. This is the first enzyme
F James et al.
The Journal of biological chemistry, 270(38), 22344-22350 (1995-09-22)
The plant enzyme S-adenosylmethionine:methionine S-methyltransferase (EC 2.1.1.12, MMT) catalyzes the synthesis of S-methylmethionine. MMT was purified 620-fold to apparent homogeneity from leaves of Wollastonia biflora. The four-step purification included fractionation with polyethylene glycol, affinity chromatography on adenosine-agarose, anion exchange chromatography
D L Martin
Cellular and molecular neurobiology, 7(3), 237-253 (1987-09-01)
1. Glutamate decarboxylase is a focal point for controlling gamma-aminobutyric acid (GABA) synthesis in brain. Several factors that appear to be important in the regulation of GABA synthesis have been identified by relating studies of purified glutamate decarboxylase to conditions
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

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