This is a purified rabbit anti-human JNK2 Monoclonal Antibody, Recombinant, that can be used in the validated applications of Western blot, ELISA, and immunohistochemistry. This JNK2 Monoclonal Antibody was obtained from a rabbit immunized with purified, human cell-derived, recombinant human JNK2.
Antibody characteristics include:
Applications: This JNK2 Monoclonal Antibody, Recombinant, has been validated for use in Western blot, ELISA, and immunohistochemistry
Host species and isotype: This is a rabbit Monoclonal IgG against human JNK2
Clone ID of monoclonal antibody (mAb): The JNK2 monoclonal antibody clone ID is 011
Immunogen: Recombinant human JNK2 protein
Product size: 100 µg
As described by NCBI, Mitogen-activated protein kinase 9 (MAPK9), also well known as c-Jun N-terminal kinase (JNK2), is a member of MAP kinase subfamily belonging to the protein kinase superfamily. As an integration point for multiple biochemical signals, MAPKs are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. MAPK9 responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, such as c-Jun and ATF2. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis. JNK protein kinases includes JNK1 and JNK2, and the activity of JNK2 was approximately 10-fold greater than that of JNK1 in c-Jun phosphorylation. JNK2 is activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells. Inaddition, JNK2 blocks the ubiquitination of tumor suppressor p53, and thus increases the stability of p53 in nonstressed cells. Several alternatively spliced transcript variants of JNK2 with different binding patterns have been identified: alpha-1 and alpha-2 preferentially bind to c-Jun, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.