Skip to Content
Merck
CN

SML2326

MSC1094308

≥98% (HPLC)

Synonym(s):

N-((6-Fluoro-2,3,4,9-tetrahydro-1H-carbazol-3-yl)methyl)-4,4-bis(4-fluorophenyl)butan-1-amine, N-[4,4-Bis(4-fluorophenyl)butyl]-6-fluoro-2,3,4,9-tetrahydro-1H-carbazole-3-methanamine

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View

About This Item

Empirical Formula (Hill Notation):
C29H29F3N2
CAS Number:
Molecular Weight:
462.55
UNSPSC Code:
12352200
NACRES:
NA.21
Assay:
≥98% (HPLC)
Form:
powder
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


assay

≥98% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 2 mg/mL, clear

storage temp.

2-8°C

SMILES string

FC1=CC=C(C(C2=CC=C(F)C=C2)CCCNCC3CCC(NC4=C5C=C(F)C=C4)=C5C3)C=C1

InChI key

OCZIMUMAPGQEBH-UHFFFAOYSA-N

Biochem/physiol Actions

MSC1094308 binding to drugable hotspot of p97 has the ability to block the D2 ATPase activity.
MSC1094308 is a reversible, non-ATP-competitive, type I AAA ATPase VPS4B-selective allosteric inhibitor (IC50 = 0.71 μM) with =10-fold reduced potency toward the type II AAA ATPase VCP/p97 and NSF (IC50 = 7.2 and >40 μM, respectively). MSC1094308 specifically inhibits p97-mediated Ub-GFP degradation without affecting proteasome-dependent ODD-luc degradation using a dual reporter HeLa cell line (10 μM) and exhibits comparable efficacy as DBeQ against 50 ng/mL TNFα-induced IκBα degradation in HeLa cells (10 μM).
Reversible, non-ATP-competitive, AAA ATPase VPS4B & VCP/p97 allosteric inhibitor against cellular p97, but not proteasome, substrates degradation.


Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library