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420116

Sigma-Aldrich

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.

Sinonimo/i:

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

Formula empirica (notazione di Hill):
C168H293N67O42
Peso molecolare:
3923.55
Codice UNSPSC:
12352200
NACRES:
NA.77

Livello qualitativo

Saggio

≥97% (HPLC)

Stato

lyophilized solid

Potenza

1 μM IC50

Produttore/marchio commerciale

Calbiochem®

Condizioni di stoccaggio

OK to freeze
desiccated (hygroscopic)

Colore

white

Solubilità

water: 2 mg/mL

Condizioni di spedizione

ambient

Temperatura di conservazione

−20°C

Descrizione generale

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.

Azioni biochim/fisiol

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

Confezionamento

Packaged under inert gas

Attenzione

Toxicity: Standard Handling (A)

Sequenza

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

Stato fisico

Supplied as a trifluoroacetate salt.

Ricostituzione

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

Altre note

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

Note legali

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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
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
Pau Marfull-Oromí et al.
Methods in molecular biology (Clifton, N.J.), 2438, 287-301 (2022-02-12)
In vitro studies have provided valuable insights to the function and mechanisms in axon guidance. In this chapter, we will introduce the rodent "open-book" assay, pre- or postcrossing explant culture and the dissociated neuron culture. They have been used to

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