JNK2 Protein, Human (sf9, His)

JNK2 is a critical serine/threonine protein kinase that centrally regulates multiple cellular processes, including proliferation, apoptosis, and differentiation. JNK2 is activated by MAP2K4/MKK4 and MAP2K7/MKK7 in the SAP/JNK pathway and regulates AP-1 transcriptional activity by phosphorylating components such as JUN and ATF2. JNK2 Protein, Human (sf9, His) is the recombinant human-derived JNK2 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of JNK2 Protein, Human (sf9, His) is 424 a.a., with molecular weight of ~49.5 kDa.

JNK2, a serine/threonine-protein kinase, is a central player in diverse cellular processes, encompassing cell proliferation, differentiation, migration, transformation, and programmed cell death. Activation of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway by extracellular stimuli, such as pro-inflammatory cytokines or physical stress, involves the phosphorylation and activation of JNK2 by dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7. Within this cascade, JNK2 phosphorylates critical transcription factors, particularly components of AP-1 like JUN and ATF2, thereby modulating AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, JNK2 inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Additionally, JNK2 plays a crucial role in stressed cell apoptosis by phosphorylating key regulatory factors, including TP53 and YAP1. In T-cells, JNK2, along with MAPK8, is essential for the polarized differentiation of T-helper cells into Th1 cells. Furthermore, upon T-cell receptor (TCR) stimulation, JNK2 is activated to regulate JUN protein levels by interacting with CARMA1, BCL10, MAP2K7, and MAP3K7/TAK1. JNK2 is also instrumental in osmotic stress-induced disruption of epithelial tight junctions and, when activated, promotes beta-catenin/CTNNB1 degradation, thereby inhibiting the canonical Wnt signaling pathway. Additionally, JNK2 participates in neurite growth in spiral ganglion neurons and phosphorylates the CLOCK-BMAL1 heterodimer, contributing to the regulation of the circadian clock. Notably, JNK2 isoforms exhibit distinct binding patterns, with alpha-1 and alpha-2 preferentially binding to JUN, while beta-1 and beta-2 bind to ATF2. However, phosphorylation efficiency remains consistent across all isoforms, and JUNB is not a substrate for JNK2 alpha-2, with JUND binding only weakly to it.

Human

Sf9 insect cells

C-His

P45984 (M1-R424)

5601  [NCBI]

Approximately 49.5 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.