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Key Documents

SML2047

Sigma-Aldrich

BPAM344

≥98% (HPLC)

Synonym(s):

BPAM344, 4-Cyclopropyl-3,4-dihydro-7-fluoro-2H-1,2,4-benzothiadiazine 1,1-dioxide

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About This Item

Empirical Formula (Hill Notation):
C10H11FN2O2S
CAS Number:
Molecular Weight:
242.27
UNSPSC Code:
12352200
NACRES:
NA.77

Assay

≥98% (HPLC)

form

powder

color

white to beige

storage temp.

2-8°C

SMILES string

O=S1(C2=CC(F)=CC=C2N(C3CC3)CN1)=O

Biochem/physiol Actions

BPAM344 is a potent positive allosteric modulator (PAM) on the three KAR subunits GluK1b, GluK2a, and GluK3a. BPAM344 potentiates glutamate-evoked currents of GluK2a 21-fold, and noticeably decreases desensitization kinetics (from 5.5 to 775 ms).

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Christian Krintel et al.
Biophysical journal, 110(11), 2397-2406 (2016-06-09)
The 1,2,4-benzothiadiazine 1,1-dioxide type of positive allosteric modulators of the ionotropic glutamate receptor A2 (GluA2) are promising lead compounds for the treatment of cognitive disorders, e.g., Alzheimer's disease. The modulators bind in a cleft formed by the interface of two
Anja Probst Larsen et al.
Molecular pharmacology, 91(6), 576-585 (2017-04-01)
Kainate receptors (KARs) consist of a class of ionotropic glutamate receptors, which exert diverse pre- and postsynaptic functions through complex signaling regulating the activity of neural circuits. Whereas numerous small-molecule positive allosteric modulators of the ligand-binding domain of (
Ann-Beth Nørholm et al.
Journal of medicinal chemistry, 56(21), 8736-8745 (2013-10-18)
Positive allosteric modulators of ionotropic glutamate receptors are potential compounds for treatment of cognitive disorders, e.g., Alzheimer's disease. The modulators bind within the dimer interface of the ligand-binding domain (LBD) and stabilize the agonist-bound conformation, thereby slowing receptor desensitization and/or

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