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420116

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

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:

JNK Inhibitor I, (L)-Form, Cell-Permeable, c-Jun NH₂-terminal kinase, SAPK Inhibitor I, (L)-JNKI1, ( L)-HIV-TAT₄₈₋₅₇-PP-JBD₂₀, H-GRKKRRQRRRPPRPKRPTTLNLFPQVPRSQDT-NH₂

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About This Item

Fórmula empírica (notación de Hill):
C168H293N67O42
Peso molecular:
3923.55
Código UNSPSC:
12352200
NACRES:
NA.77

Nivel de calidad

Análisis

≥97% (HPLC)

formulario

lyophilized solid

potencia

1 μM IC50

fabricante / nombre comercial

Calbiochem®

condiciones de almacenamiento

OK to freeze
desiccated (hygroscopic)

color

white

solubilidad

water: 2 mg/mL

Condiciones de envío

ambient

temp. de almacenamiento

−20°C

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. 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.
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.

Acciones bioquímicas o fisiológicas

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

Envase

Packaged under inert gas

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

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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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
Lili Xu et al.
Immunity, 33(3), 313-325 (2010-09-28)
The molecular mechanisms underlying retinoic acid (RA) augmentation of T cell receptor (TCR) and transforming growth factor-β (TGF-β)-induced Foxp3 transcription and inhibition of the latter by cytokines such as IL-27 were here shown to be related processes involving modifications of baseline
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
Roberta Caruso et al.
Journal of immunology (Baltimore, Md. : 1950), 178(9), 5957-5965 (2007-04-20)
Helicobacter pylori (Hp) infection is associated with gastric inflammation and ulceration. The pathways of tissue damage in Hp-infected subjects are complex, but evidence indicates that T cell-derived cytokines enhance the synthesis of matrix metalloproteinases (MMP) that contribute to mucosal ulceration
Kai Fang et al.
International journal of inflammation, 2020, 6150942-6150942 (2020-03-06)
It has been reported that pathological angiogenesis contributes to both experimental colitis and inflammatory bowel disease. Recently, we demonstrated that endothelial caveolin-1 plays a key role in the pathological angiogenesis of dextran sodium sulfate (DSS) colitis. However, the molecular mechanism

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