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Merck
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SML1959

Sigma-Aldrich

GA3-AM

≥95% (HPLC)

Sinónimos:

(1α,2β,4aα,4bβ,10β)-2,4a,7-Trihydroxy-1-methyl-8-methylenegibb-3-ene-1,10-dicarboxylic Acid 1,4a-Lactone Acetoxymethyl Ester, (1S,2S,4aR,4bR,7S,9aS,10S,10aR)-1,2,4b,5,6,7,8,9,10,10a-decahydro-2,7-dihydroxy-1-methyl-8-methylene-13-oxo-4a,1-(Epoxymethano)-7,9a-methanobenz[a]azulene-10-acetic acid (acetyloxy)methyl ester, Gibberellic Acid Acetoxymethyl Ester

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About This Item

Fórmula empírica (notación de Hill):
C22H26O8
Número de CAS:
1373154-68-7
Peso molecular:
418.44
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

100

assay

≥95% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 2 mg/mL, clear

storage temp.

−20°C

Biochem/physiol Actions

GA3-AM is a cell permeable analog of the plant hormone gibberellic acid that acts as a chemical dimerizer or chemical inducer of dimerization. GA3 and rapamycin chemically inducible dimerization systems are orthogonal. GA3-AM has been used in conjunction with a rapamycin dimerization system and CRISPR/Cas9 activators for temporal control of CRISPR/Cas9 activator function, enabling temporal regulation of multiple genes.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Takafumi Miyamoto et al.
Nature chemical biology, 8(5), 465-470 (2012-03-27)
Using a newly synthesized gibberellin analog containing an acetoxymethyl group (GA(3)-AM) and its binding proteins, we developed an efficient chemically inducible dimerization (CID) system that is completely orthogonal to existing rapamycin-mediated protein dimerization. Combining the two systems should allow applications
Zehua Bao et al.
ACS synthetic biology, 6(4), 686-693 (2017-01-06)
The concerted action of multiple genes in a time-dependent manner controls complex cellular phenotypes, yet the temporal regulation of gene expressions is restricted on a single-gene level, which limits our ability to control higher-order gene networks and understand the consequences
Shameika R Wilmington et al.
PloS one, 11(4), e0152679-e0152679 (2016-04-05)
A common way to study protein function is to deplete the protein of interest from cells and observe the response. Traditional methods involve disrupting gene expression but these techniques are only effective against newly synthesized proteins and leave previously existing
Maxime Boutry et al.
Nature communications, 12(1), 5354-5354 (2021-09-11)
Mitochondrial division is not an autonomous event but involves multiple organelles, including the endoplasmic reticulum (ER) and lysosomes. Whereas the ER drives the constriction of mitochondrial membranes, the role of lysosomes in mitochondrial division is not known. Here, using super-resolution

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