MAPK8, 9

Mouse IgG2a

Human JNK1 Fusion Protein

C- J un N H2-terminal k inase (JNK) binds to the c-Jun terminal transactivation domain and phosphorylates it on Ser-63 and Ser-73.  Phosphorylation enhances the transcriptional activity of c-Jun. The Ser-Pro-acidic sequence targeted by JNK kinase activity establishes it as a prolinedirected kinase related to the MAP kinases and cyclin/dependent kinases.  JNK may act as a tumor promoter in response to UV-irradiation since its activity is potently stimulated by radiation.  This has relevance to observations that c-Jun transcriptional activity is upregulated by UV irradiation. In addition to UV irradiation, JNK is also activated by some other forms of cellular stress, including heatshock.  Both the JNK1 (46 kDa) and JNK2 (54 kDa) isozymes appear equally capable of binding to the c-Jun terminal transactivation domain following induction by UV irradiation or heatshock. G151-666 recognizes both the JNK1 and JNK2 isozymes of JNK1. A bacterially expressed fusion protein of human JNK1 was used as immunogen.

G151-666 C- J un N H2-terminal k inase (JNK) binds to the c-Jun terminal transactivation domain and phosphorylates it on Ser-63 and Ser-73.  Phosphorylation enhances the transcriptional activity of c-Jun. The Ser-Pro-acidic sequence targeted by JNK kinase activity establishes it as a prolinedirected kinase related to the MAP kinases and cyclin/dependent kinases.  JNK may act as a tumor promoter in response to UV-irradiation since its activity is potently stimulated by radiation.  This has relevance to observations that c-Jun transcriptional activity is upregulated by UV irradiation. In addition to UV irradiation, JNK is also activated by some other forms of cellular stress, including heatshock.  Both the JNK1 (46 kDa) and JNK2 (54 kDa) isozymes appear equally capable of binding to the c-Jun terminal transactivation domain following induction by UV irradiation or heatshock. G151-666 recognizes both the JNK1 and JNK2 isozymes of JNK1. A bacterially expressed fusion protein of human JNK1 was used as immunogen.

Mouse IgG2a

克隆 G151-666 (RUO)

0.5 mg/ml

Western blot (Routinely Tested), Immunoprecipitation (Tested During Development)

Human (QC Testing)

MAPK8, 9

Aqueous buffered solution containing ≤0.09% sodium azide.

研发参考(6) 1. Adler V, Fuchs SY, Kim J. jun-NH2-terminal kinase activation mediated by UV-induced DNA lesions in melanoma and fibroblast cells. Cell Growth Differ. 1995; 6(11):1437-1446. (Clone-specific: Immunoprecipitation, Western blot). 2. Adler V, Pincus MR, Brandt-Rauf PW, Ronai Z. Complexes of p21RAS with JUN N-terminal kinase and JUN proteins. Proc Natl Acad Sci U S A. 1995; 92(23):10585-10589. (Clone-specific: Immunoprecipitation). 3. Adler V, Schaffer A, Kim J, Dolan L, Ronai Z. UV irradiation and heat shock mediate JNK activation via alternate pathways. J Biol Chem. 1995; 270(44):26071-26077. (Clone-specific: Immunoprecipitation, Western blot). 4. Devary Y, Rosette C, DiDonato JA, Karin M. NF-kappa B activation by ultraviolet light not dependent on a nuclear signal. Science. 1993; 261(5127):1442-1445. (Biology). 5. Dérijard B, Hibi M, Wu IH. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell. 1994; 76(6):1025-1037. (Biology). 6. Hibi M, Lin A, Smeal T, Minden A, Karin M. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev. 1993; 7(11):2135-2148. (Biology).