420116
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.
Synonyme(s) :
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
Formule empirique (notation de Hill):
C168H293N67O42
Poids moléculaire :
3923.55
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77
Produits recommandés
Niveau de qualité
Pureté
≥97% (HPLC)
Forme
lyophilized solid
Puissance
1 μM IC50
Fabricant/nom de marque
Calbiochem®
Conditions de stockage
OK to freeze
desiccated (hygroscopic)
Couleur
white
Solubilité
water: 2 mg/mL
Conditions d'expédition
ambient
Température de stockage
−20°C
Description générale
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.
Actions biochimiques/physiologiques
Cell permeable: yes
Primary Target
JNK
JNK
Product does not compete with ATP.
Reversible: no
Conditionnement
Packaged under inert gas
Avertissement
Toxicity: Standard Handling (A)
Séquence
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
Forme physique
Supplied as a trifluoroacetate salt.
Reconstitution
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Autres remarques
Barr, R.K., et al. 2002. J. Biol. Chem.277, 10987.
Bonny, C., et al. 2001. Diabetes50, 77.
Bonny, C., et al. 2001. Diabetes50, 77.
Informations légales
Sold under license of U.S. Patents 6,043,083 and 6,410,693.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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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
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
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
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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