Key features and details
- Suitable for: Blocking
Product nameTAK1 peptide
See all TAK1 proteins and peptides
Purity70 - 90% by HPLC.
Our Abpromise guarantee covers the use of ab150779 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Constituents: 10% DMSO, 0.1% BSA, 0.15% EDTA, 0.6% Tris
50mM Tris, 5mM EDTA
- MAP3K 7
FunctionComponent of a protein kinase signal transduction cascade. Mediator of TRAF6 and TGF-beta signal transduction. Activates IKBKB and MAPK8 in response to TRAF6 signaling. Stimulates NF-kappa-B activation and the p38 MAPK pathway. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK, but not that of NF-kappa-B.
Sequence similaritiesBelongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.
Contains 1 protein kinase domain.
modificationsAssociation with TAB1/MAP3K7IP1 promotes autophosphorylation and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Thr-187 by PP2A and PPP6C leads to inactivation.
Ubiquitinated, leading to proteasomal degradation (By similarity). Requires 'Lys-63'-linked polyubiquitination for autophosphorylation and subsequent activation. 'Lys-63'-linked ubiquitination does not lead to proteasomal degradation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Deubiquitinated by Y.enterocolitica YopP.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab150779 has not yet been referenced specifically in any publications.