JNK1

Contents: phospho-JNK1 (T183/Y185) Blocking Peptide
Catalog Number: 66-P759
Formulation: Each vial contains 100 μg of peptide in 0.5 ml PBS with 0.1% NaN₃ and 100 μg BSA.
Storage Conditions: Store at 4°C.
DO NOT FREEZE.

Prices for This Product*
Cat. No.	Size	Price	Qty	Action
66-P759-81	50 ug	$25

*International customers: Please contact your distributor for region specific pricing.

Available Formats of This Product
Cat. No.	Format	Excite (nm)	Emit (nm)	Reported Applications
66-P759	Blocking Peptides for anti-mouse/human/rat phospho-JNK1 polyclonal	N/A	N/A	WB

Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq.

Description

This is a peptide mapping to an internal domain containing phosphorylated T183/Y185 of human JNK1. The mitogen-activated protein kinases (MAPK) consist of several subgroups, including the ERK, JNK, and p38 kinases. The members of this MAPK family are regulated by many different extracellular cues ranging from cytokines, growth factors, and neuropeptides (1). These stimuli activate cell surface receptors to stresses such as cold, heat, osmolarity changes and irradiation. The pathways regulated by the MAPKs control a broad array of cellular responses ranging from survival, cell proliferation, and apoptosis (1,2). The MAPKs family is also characterized by their requirement for dual phosphorylation at a conserved threonine and tyrosine residue for enzymatic activation and both must be phosphorylated for full enzymatic activation (3). The closely related ERK1 (44 kDa) and ERK2 (42 kDa) kinases are characterized by their requirement for dual phosphorylation at a conserved T-E-Y motif (4,5). While JNK1 is activated by dual phosphorylation at a T-P-Y motif and p38 is also activated by dual phosphorylation at a T-G-Y motif (6,7).

Applications Reported

For research use only, not for diagnostic or therapeutic use. This blocking peptide has been reported for use in competition studies.

References

1. Fanger GR. 1999. Regulation of the MAKP family members: role of the subcellular localization and architectural organization. Histol Histopathol 14(3):887-894.
2. Kyriakis JM. 1999. Making the connection: coupling of stress-activated ERK/MAPK (extracellular-signal-regulated kinase/mitogen-activated protein kinase) core signaling modules to extracellular stimuli and biological responses. Biochem Soc Symp 64:29-48.
3. Prowse CN, Lew J. 2001. Mechanism of activation of ERK2 by dual phosphorylation. J Biol Chem 276(1):99-103.
4. Kyriakis JM, Banerjee P, Nikolakaki E, Dai T, Rubie EA, Ahmad MF, Avruch J, Woodgett JR. 1994. The stress-activated protein kinase subfamily of c-Jun kinases. Nature 369(6476):156-160.
5. Cha H, Shapiro P. 2001. Tyrosine-phosphorylated extracellular signal- -regulated kinase associates with Golgi complex during G2/M phase of the cell cycle: evidence for regulation of Golgi structure. J Cell Biol 153(7):1355-1367.
6. Chan ED, Winston BW, Jarpe MB, Wynes MW, Riches DW. 1997. Preferential activation of the p46 isoform of JNK/SAPK in mouse macrophages by TNF alpha. Proc Natl Acad Sci USA 94(24):13169-13174.
7. Nishida E, Gotoh Y. 1993. The MAP kinase cascade is essential for diverse signal transduction pathways. Trends Biochem Sci 18:128-131.

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