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SML1959

Sigma-Aldrich

GA3-AM

≥95% (HPLC)

Synonym(e):

(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

Empirische Formel (Hill-System):
C22H26O8
CAS-Nummer:
1373154-68-7
Molekulargewicht:
418.44
UNSPSC-Code:
12352200
NACRES:
NA.77

Qualitätsniveau

100

Assay

≥95% (HPLC)

Form

powder

Farbe

white to beige

Löslichkeit

DMSO: 2 mg/mL, clear

Lagertemp.

−20°C

Biochem./physiol. Wirkung

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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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
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
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

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