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Key Documents

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SML0006

Sigma-Aldrich

CK-666

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

Sinónimos:

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

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About This Item

Fórmula empírica (notación de Hill):
C18H17FN2O
Número de CAS:
442633-00-3
Peso molecular:
296.34
MDL number:
MFCD03036271
UNSPSC Code:
12352200
PubChem Substance ID:
329825083
NACRES:
NA.77

product name

CK-666, ≥98% (HPLC), powder

Quality Level

100

assay

≥98% (HPLC)

form

powder

color

white to tan

solubility

DMSO: ≥25 mg/mL

storage temp.

2-8°C

SMILES string

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)

InChI key

UXRKUKRXVWJFER-UHFFFAOYSA-N

Application

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

Biochem/physiol Actions

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
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
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
Ivana Viktorinová et al.
PLoS genetics, 13(11), e1007107-e1007107 (2017-11-28)
Symmetry breaking is involved in many developmental processes that form bodies and organs. One of them is the epithelial rotation of developing tubular and acinar organs. However, how epithelial cells move, how they break symmetry to define their common direction
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