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SML2207

Sigma-Aldrich

SR-4995

≥98% (HPLC)

Synonym(s):

CID 16016685, N-Butyl-N′-(10,11-dihydro-10-methyl-11-oxodibenzo[b,f][1,4]thiazepin-8-yl)urea

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5 MG
CHF 97.50
25 MG
CHF 429.00

CHF 97.50

Estimated to ship on06 April 2025

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5 MG
CHF 97.50
25 MG
CHF 429.00

About This Item

Empirical Formula (Hill Notation):
C19H21N3O2S
CAS Number:
891509-95-8
Molecular Weight:
355.45
UNSPSC Code:
12352200
NACRES:
NA.77

CHF 97.50

Estimated to ship on06 April 2025

Request a Bulk Order

Assay

≥98% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 2 mg/mL, clear

storage temp.

−20°C

SMILES string

CN1C(C(C=CC=C2)=C2SC3=C1C=C(NC(NCCCC)=O)C=C3)=O

InChI

1S/C19H21N3O2S/c1-3-4-11-20-19(24)21-13-9-10-17-15(12-13)22(2)18(23)14-7-5-6-8-16(14)25-17/h5-10,12H,3-4,11H2,1-2H3,(H2,20,21,24)

InChI key

UGYXUEPBYOKNOL-UHFFFAOYSA-N

Biochem/physiol Actions

SR-4995 is a potent and selective ligand of α-β-hydrolase domain containing 5 (ABHD5) that activates adipose triglyceride lipase (ATGL) by dissociating ABHD5 from its inhibitory regulator, perilipin-1 (PLIN1) and PLIN5. SR-4995 directly binds to ABHD5 and prevents ABHD5 to PLIN1. SR-4995 induces lipolysis in adipocytes and muscle, avoiding PKA-dependent signaling.
potent and selective ligand of ABHD5 that activates ATGL by dissociating ABHD5 from PLIN1 and PLIN5

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000109531
0000061780
0000061781
0000054779

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Elizabeth A Rondini et al.
The Journal of pharmacology and experimental therapeutics, 363(3), 367-376 (2017-09-21)
Current knowledge regarding acute regulation of adipocyte lipolysis is largely based on receptor-mediated activation or inhibition of pathways that influence intracellular levels of cAMP, thereby affecting protein kinase A (PKA) activity. We recently identified synthetic ligands of α-β-hydrolase domain containing
Matthew A Sanders et al.
Cell metabolism, 22(5), 851-860 (2015-09-29)
Fat and muscle lipolysis involves functional interactions of adipose triglyceride lipase (ATGL), α-β hydrolase domain-containing protein 5 (ABHD5), and tissue-specific perilipins 1 and 5 (PLIN1 and PLIN5). ABHD5 potently activates ATGL, but this lipase-promoting activity is suppressed when ABHD5 is

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