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SML2361

Sigma-Aldrich

Kinesore

>97% (HPLC)

Synonym(s):

3,5-Dibromo-4-hydroxy-benzoic acid 2-[[2,5-dimethyl-1-(3-nitrophenyl)-1H-pyrrol-3-yl]methylene]hydrazide, 3,5-Dibromo-N′-{[2,5-dimethyl-1-(3-nitrophenyl)-1H-pyrrol-3-yl]methylene}-4-hydroxybenzohydrazide

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About This Item

Empirical Formula (Hill Notation):
C20H16Br2N4O4
CAS Number:
Molecular Weight:
536.17
MDL number:
UNSPSC Code:
31401503
NACRES:
NA.77

Assay

>97% (HPLC)

form

powder

color

white to brown

solubility

DMSO: 2 mg/mL, clear

storage temp.

2-8°C

Related Categories

Biochem/physiol Actions

Kinesore is a cell penetrant and potent activator of kinesin-1 that induces kinesin light chain tetratricopeptide repeat domain-dependent kinesin-1 activation in the absence of organelle cargo-adaptor engagement. It inhibits kinesin-1 interaction with peptide fragment of organelle-specific cargo adaptors. Kinesore induces kinesin light chain conformational switch that causes remodeling of the microtubule network in cells.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Thomas S Randall et al.
Proceedings of the National Academy of Sciences of the United States of America, 114(52), 13738-13743 (2017-12-13)
The microtubule motor kinesin-1 interacts via its cargo-binding domain with both microtubules and organelles, and hence plays an important role in controlling organelle transport and microtubule dynamics. In the absence of cargo, kinesin-1 is found in an autoinhibited conformation. The
Yerbol Tagay et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 10(31), e2302229-e2302229 (2023-09-20)
The principal cause of death in cancer patients is metastasis, which remains an unresolved problem. Conventionally, metastatic dissemination is linked to actomyosin-driven cell locomotion. However, the locomotion of cancer cells often does not strictly line up with the measured actomyosin
Raeann Goering et al.
eLife, 12 (2023-03-04)
RNA molecules are localized to specific subcellular regions through interactions between RNA regulatory elements and RNA binding proteins (RBPs). Generally, our knowledge of the mechanistic details behind the localization of a given RNA is restricted to a particular cell type.

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