The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use a concentration of 1 µg/ml. Detects a band of approximately 48 kDa (predicted molecular weight: 48 kDa). Also detects a band of approximately 44-kDa.
Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells (By similarity). Phosphorylates heat shock factor protein 4 (HSF4). JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme.
JNK1 has 4 isoforms. JNK1 alpha 2 and JNK1 beta 2 are both 48-kDa. JNK alpha 1 and JNK1 beta 1 are 44-kDa. ab85139 detects bands at approximately 44-kDa, 48-kDa and 54-kDa. We hypothesise that the bands at 44-kDa and 48-kDa correspond to different isoforms of JNK1. JNK1 has several potential phosphorylation sites (Swissprot). The band at 54-kDa may be a phosphorylated form of the JNK1 protein.
Guo CH et al. The analgesic effect of rolipram is associated with the inhibition of the activation of the spinal astrocytic JNK/CCL2 pathway in bone cancer pain. Int J Mol Med38:1433-1442 (2016).
Read more (PubMed: 28025994) »
Krishna SN et al. A fluorescence-based thermal shift assay identifies inhibitors of mitogen activated protein kinase kinase 4. PLoS One8:e81504 (2013).
Read more (PubMed: 24339940) »