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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A propos de cet article
Formule empirique (notation de Hill) :
C168H293N67O42
Poids moléculaire :
3923.55
NACRES:
NA.77
UNSPSC Code:
12352200
Assay:
≥97% (HPLC)
Form:
lyophilized solid
Quality level:
Storage condition:
OK to freeze, desiccated (hygroscopic)
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Laissez-nous vous aiderassay
≥97% (HPLC)
form
lyophilized solid
potency
1 μM IC50
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, desiccated (hygroscopic)
color
white
solubility
water: 2 mg/mL
shipped in
ambient
storage temp.
−20°C
Quality Level
Catégories apparentées
General description
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.
Biochem/physiol Actions
Cell permeable: yes
Primary Target
JNK
JNK
Product does not compete with ATP.
Reversible: no
Packaging
Packaged under inert gas
Physical form
Supplied as a trifluoroacetate salt.
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Other Notes
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.
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
Legal Information
Sold under license of U.S. Patents 6,043,083 and 6,410,693.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
Classe de stockage
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
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
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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