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BI-78D3

Catalog No. B3063 Name Sigma Aldrich
CAS Number 883065-90-5 Website http://www.sigmaaldrich.com
M. F. C13H9N5O5S2 Telephone 1-800-521-8956
M. W. 379.37106 Fax
Purity ≥98% (HPLC) Email
Storage desiccated Chembase ID: 154295

SYNONYMS

IUPAC name
4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-4H-1,2,4-triazol-3-ol
IUPAC Traditional name
4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,2,4-triazol-3-ol
Synonyms
4-(2,3-Dihydrobenzol[b][1,4]dioxin-6-yl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol

DATABASE IDS

CAS Number 883065-90-5
MDL Number MFCD12912396

PROPERTIES

Empirical Formula (Hill Notation) C13H9N5O5S2
Purity ≥98% (HPLC)
Apperance tan powder
Solubility DMSO: >10 mg/mL
MSDS Link Download
Storage Condition desiccated
Storage Temperature -20°C
German water hazard class 2

DETAILS

Description (English)
Biochem/physiol Actions
BI-78D3 is a substrate competitive inhibitor of JNK. JNK′s binds to JNK-interacting protein-1 (JIP1) (scaffolding protein) through high affinity D-domain on JIP1. This interaction is needed to place JNK next to target protein. BI-78D3 is a mimetic of a critical peptide structure of JIP1 which binds to JNK away from ATP binding domain preventing JIP1 JNK interaction thus acting as a substrate competitive inhibitor both in vitro and in vivo. The compound represents a growing number of modern kinase inhibitors acting at protein protein interacting areas (scaffolding) rather than ATP binding pockets.
Description (简体中文)
Biochem/physiol Actions
BI-78D3 is a substrate competitive inhibitor of JNK. JNK′s binds to JNK-interacting protein-1 (JIP1) (scaffolding protein) through high affinity D-domain on JIP1. This interaction is needed to place JNK next to target protein. BI-78D3 is a mimetic of a critical peptide structure of JIP1 which binds to JNK away from ATP binding domain preventing JIP1 JNK interaction thus acting as a substrate competitive inhibitor both in vitro and in vivo. The compound represents a growing number of modern kinase inhibitors acting at protein protein interacting areas (scaffolding) rather than ATP binding pockets.

REFERENCES