420116

Sigma-Aldrich

JNK Inhibitor I, (L)-Form, Cell-Permeable - Calbiochem

The JNK Inhibitor I, (L)-Form, Cell-Permeable controls the biological activity of JNK. This small molecule/inhibitor is primarily used for Phosphorylation & Dephosphorylation applications.

Sinónimos:
c-Jun NH₂-terminal kinase, SAPK Inhibitor I, (L)-JNKI1, ( L)-HIV-TAT₄₈₋₅₇-PP-JBD₂₀, H-GRKKRRQRRRPPRPKRPTTLNLFPQVPRSQDT-NH₂, JNK Inhibitor I, (L)-Form, Cell-Permeable - Calbiochem
Empirical Formula (Hill Notation):
C168H293N67O42
Peso molecular:
3923.55

storage conditions

-20C

Nivel de calidad

100

ensayo

≥97% (HPLC)

formulario

lyophilized solid

potencia

1 μM IC50

manufacturer/tradename

Calbiochem®

condiciones de almacenamiento

OK to freeze
desiccated (hygroscopic)

color

white

solubilidad

water: 2 mg/mL

enviado en

ambient

Descripción general

A cell-permeable, biologically active peptide consisting of a carboxyl- terminal sequence derived from the JNK-binding domain (JBD) and an amino-terminal peptide containing the HIV-TAT48-57 sequence that imparts cell-permeability. Blocks the activation domain of c-Jun NH2-terminal kinase (JNK) and prevents the activation of the transcription factor c-Jun (IC50 ~1 µM). Contains the minimal 20-amino acid inhibitory domain of islet-brain (IB), which is critical for interaction with JNK.The peptide is covalently linked to the 10-amino acid HIV-TAT48-57 sequence that acts as a carrier peptide and to two proline residue spacers. Inhibits IL-1β-induced c-Jun and c-fos expression in insulin secreting βTC-3 cells and offers protection against apoptosis. Does not affect insulin secretion and has no significant effect on the activities of ERK1, ERK2, or p38.
A cell-permeable, biologically active peptide consisting of a carboxyl terminal sequence derived from the JNK-binding domain (JBD) and an amino terminal peptide containing the HIV-TAT48-57 sequence. Blocks c-Jun NH2-terminal kinase (JNK) signaling by preventing the activation of the transcription factor c-jun (IC50 ~ 1 µM). This effect appears to be due to inhibition of phosphorylation of the activation domains of JNK. Contains the minimal 20-amino acid inhibitory domain of islet-brain (IB) that is shown to be critical for interaction with JNK linked to the 10-amino acid HIV-TAT48-57 sequence as a carrier peptide and two proline residues as spacer. Inhibits IL-1β-induced c-jun and c-fos expression in insulin secreting βTC-3 cells and offers protection against apoptosis. Does not affect insulin secretion and has no effect on either ERK 1/2 or p38 activities.

Envase

1 mg in Plastic ampoule
Packaged under inert gas

Acciones bioquímicas o fisiológicas

Product does not compete with ATP.
Cell permeable: yes
Primary Target
JNK
Reversible: no

Advertencia

Toxicity: Standard Handling (A)

Secuencia

H-Gly-Arg-Lys-Lys-Arg-Agr-Gln-Arg-Arg-Arg-Pro-Pro-Arg-Pro-Lys-Arg-Pro-Thr-Thr-Leu-Asn-Leu-Phe-Pro-Gln-Val-Pro-Arg-Ser-Gln-Asp-Thr-NH₂

Forma física

Supplied as a trifluoroacetate salt.

Reconstitución

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Otras notas

Barr, R.K., et al. 2002. J. Biol. Chem.277, 10987.
Bonny, C., et al. 2001. Diabetes50, 77.

Información legal

Sold under license of U.S. Patents 6,043,083 and 6,410,693.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

WGK Alemania

WGK 1

Punto de inflamabilidad F

Not applicable

Punto de inflamabilidad C

Not applicable

C Bonny et al.
Diabetes, 50(1), 77-82 (2001-01-09)
Stress conditions and proinflammatory cytokines activate the c-Jun NH2-terminal kinase (JNK), a member of the stress-activated group of mitogen-activated protein kinases (MAPKs). We recently demonstrated that inhibition of JNK signaling with the use of the islet-brain (IB) 1 and 2...
Renae K Barr et al.
The Journal of biological chemistry, 277(13), 10987-10997 (2002-01-16)
The c-Jun N-terminal kinases (JNKs) are a subfamily of the mitogen-activated protein kinases (MAPKs). Although progress in evaluating the functions of other MAPKs has been facilitated by the characterization of specific inhibitors, no JNK-directed inhibitor is commercially available. We have...

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