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Merck
CN

C2629

乙酰胆碱酯酶 来源于电鳗

Type III, aqueous solution, ≥1,000 units/mg protein

别名:

AChE, 乙酰胆碱乙酰水解酶, 胆碱酯酶,乙酰基

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化学文摘社编号:
UNSPSC Code:
12352200
EC Number:
232-559-3
MDL number:
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type

Type III

form

aqueous solution

specific activity

≥1,000 units/mg protein

impurities

~5 mg/mg protein (NH4)2SO4

color

clear to slightly hazy light yellow

shipped in

dry ice

storage temp.

−20°C

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General description

分子量: 280 kDa
等电点: 5.5
消光系数: E1%= 18.0(280 nm)

来自 Electrophorus electricus 的乙酰胆碱酯酶是由 4 个相等的亚基组成的四聚体,每个亚基 70kDa。每个子单元包含一个活性位点。该酶是含有己糖胺的糖蛋白。

Biochem/physiol Actions

体内乙酰胆碱的主要降解酶。 将乙酰胆碱 + H2O 转化为胆碱+乙酸。

Analysis Note

The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.

Other Notes

One unit will hydrolyze 1.0 μmole of acetylcholine to choline and acetate per min at pH 8.0 at 37 °C.

Disclaimer

Excellent stability while frozen; avoid repeated freeze-thaw cycles.

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)

法规信息

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H Soreq et al.
Proceedings of the National Academy of Sciences of the United States of America, 87(24), 9688-9692 (1990-12-01)
To study the primary structure of human acetylcholinesterase (AcChoEase; EC 3.1.1.7) and its gene expression and amplification, cDNA libraries from human tissues expressing oocyte-translatable AcChoEase mRNA were constructed and screened with labeled oligodeoxynucleotide probes. Several cDNA clones were isolated that
M D Wilson et al.
Nucleic acids research, 29(6), 1352-1365 (2001-03-10)
Chromosome 7q22 has been the focus of many cytogenetic and molecular studies aimed at delineating regions commonly deleted in myeloid leukemias and myelodysplastic syndromes. We have compared a gene-dense, GC-rich sub-region of 7q22 with the orthologous region on mouse chromosome
C E Felder et al.
Journal of molecular graphics & modelling, 15(5), 318-327 (1998-06-26)
The electrostatic potentials for the three-dimensional structures of cholinesterases from various species were calculated, using the Delphi algorithm, on the basis of the Poisson-Boltzmann equation. We used structures for Torpedo californica and mouse acetylcholinesterase, and built homology models of the
R Karpel et al.
Experimental cell research, 210(2), 268-277 (1994-02-01)
To study the molecular mechanisms underlying the intensive expression of acetylcholinesterase (AChE) in different tumor types, we characterized levels and composition of its messenger RNA (mRNA) sequences in heterologous tumor cell lines, primary tumor biopsies, and normal fetal and adult
C F Bartels et al.
American journal of human genetics, 52(5), 928-936 (1993-05-01)
Acetylcholinesterase is present in innervated tissues, where its function is to terminate nerve impulse transmission. It is also found in the red blood cell membrane, where its function is unknown. We report the first genetic variant of human acetylcholinesterase and

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