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SML0006

Sigma-Aldrich

CK-666

≥98% (HPLC), powder, Arp2/3 comple inhibitor

Synonyme(s) :

2-Fluoro-N-[2-(2-methyl-1H-indol-3-yl)ethyl]-benzamide, CK 666, CK-0944666

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About This Item

Formule empirique (notation de Hill):
C18H17FN2O
Numéro CAS:
442633-00-3
Poids moléculaire :
296.34
Numéro MDL:
MFCD03036271
Code UNSPSC :
12352200
ID de substance PubChem :
329825083
Nomenclature NACRES :
NA.77

product name

CK-666, ≥98% (HPLC), powder

Niveau de qualité

100

Pureté

≥98% (HPLC)

Forme

powder

Couleur

white to tan

Solubilité

DMSO: ≥25 mg/mL

Température de stockage

2-8°C

Chaîne SMILES 

Cc1[nH]c2ccccc2c1CCNC(=O)c3ccccc3F

InChI

1S/C18H17FN2O/c1-12-13(14-6-3-5-9-17(14)21-12)10-11-20-18(22)15-7-2-4-8-16(15)19/h2-9,21H,10-11H2,1H3,(H,20,22)

Clé InChI

UXRKUKRXVWJFER-UHFFFAOYSA-N

Application

CK-666 may be used to study Arp2/3-mediated structural changes in cells.

Actions biochimiques/physiologiques

CK-666 binds to Arp2/3 complex, stabilizes the inactive state of the complex and prevents its movement into active conformation.
CK-666 is a cell-permeable inhibitor of actin assembly mediated by actin-related protein Arp2/3 complex.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Satoko Sakamoto et al.
PLoS biology, 16(9), e2004874-e2004874 (2018-09-27)
Formin is one of the two major classes of actin binding proteins (ABPs) with nucleation and polymerization activity. However, despite advances in our understanding of its biochemical activity, whether and how formins generate specific architecture of the actin cytoskeleton and
Byron Hetrick et al.
Chemistry & biology, 20(5), 701-712 (2013-04-30)
Actin-related protein 2/3 (Arp2/3) complex is a seven-subunit assembly that nucleates branched actin filaments. Small molecule inhibitors CK-666 and CK-869 bind to Arp2/3 complex and inhibit nucleation, but their modes of action are unknown. Here, we use biochemical and structural
Aaron S Dhanda et al.
mBio, 9(2) (2018-04-11)
Palladin is an important component of motile actin-rich structures and nucleates branched actin filament arrays in vitro Here we examine the role of palladin during Listeria monocytogenes infections in order to tease out novel functions of palladin. We show that
Akriti Prashar et al.
Frontiers in cellular and infection microbiology, 8, 133-133 (2018-05-19)
Legionella pneumophila (Lp) exhibits different morphologies with varying degrees of virulence. Despite their detection in environmental sources of outbreaks and in respiratory tract secretions and lung autopsies from patients, the filamentous morphotype of Lp remains poorly studied. We previously demonstrated
Shao-Chen Sun et al.
PloS one, 6(4), e18392-e18392 (2011-04-16)
Mammalian oocyte meiotic maturation involves oocyte polarization and a unique asymmetric division, but until now, the underlying mechanisms have been poorly understood. Arp2/3 complex has been shown to regulate actin nucleation and is widely involved in a diverse range of
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