Anti-phospho-TAK1 (Ser412) Antibody

Evaluated by Western Blotting in lysate from lipopolysaccharide (LPS) stimulated RAW 264.7 cells.

Western Blotting Analysis: A 1:250 dilution from a representative lot detected TAK1 phosphorylated at serine 412 in RAW 264.7 cells stimulated with lipopolysaccharide (LPS; 1 g/ml; 20 min) but, not in lysate from non-stimulated RAW 264.7 cells.

Anti-phospho-TAK1 (Ser412), Cat. No. 06-1425, is a rabbit polyclonal antibody that detects phospho-TAK1 (Ser412) and is tested for use in Western Blotting and Peptide Inhibition Assay.

Tested applications

Western Blotting Analysis: A 1:500 dilution from a representative lot detected TAK1 phosphorylated at serine 412 in RAW 264.7 cells stimulated with lipopolysaccharide stimulated (LPS; 1 g/ml; 20 min), untreated with Lambda Protein Phosphatase but, not in lipopolysaccharide (LPS) stimulated RAW 264.7 cells treated with Lambda Protein Phosphatase.

Peptide Inhibition Assay: Target band detection in lysate from RAW 264.7 cells stimulated with lipopolysaccharide (LPS; 1 g/ml; 20 min) was prevented by pre-blocking of a representative lot with the immunogen phosphorylated peptide, but not with the corresponding non-phosphorylated peptide.

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

This antibody recognizes TAK1 phosphorylated at Ser412.

Mitogen-activated protein kinase kinase kinase 7 (UniProt: O43318 also known as Transforming growth factor-beta-activated kinase 1, TGF-beta-activated kinase 1, EC:2.7.11.25) is encoded by the MAP3K7 (also known as TAK1) gene (Gene ID: 6885) in human. TAK1 is a serine/threonine kinase that plays a key role in the cascade of cellular responses evoked by changes in the environment. Its protein kinase domain is localized in amino acids 36-291. Although, a majority of TAK1 resides in cytoplasm, when complexed with TAK1-binding proteins 1 and 2 (TAB1 and TAB2), it also localizes to the membrane. Four isoforms of TAK1 have been described that are produced by alternative splicing. Isoform 1A is the most abundant in ovary, skeletal muscle, spleen and blood mononuclear cells. Isoform 1B is highly expressed in brain, kidney and small intestine. Isoform 1C is the major form in prostate and isoform 1D is the less abundant form. TAK1 MAPKKK is activated by TAB1 to transform growth factor-beta (TGF-beta) signaling. TAK1 can also associate with TAB1 to form a unique MAPKKK complex that is thought to activate AP-1 and the NFkappaB signaling pathways. TAK1 has been linked to both IL-1alpha and TNFalpha signaling. Studies show that the TAK1-TAB1 complex may have anti-inflammatory effects by aiding stercurensin in regulating the NFkappaB-dependent inflammatory pathways. It is also suggested that TAK1 activation in mediating downstream signaling requires an additional phosphorylation at Ser-412, which is critical for TAK1 response to proinflammatory stimuli, such as TNF alpha , LPS, and IL-1β. Phosphorylation of TAK1 at Serine 412 is a pivotal regulatory mechanism that influences its activity and downstream signaling pathways, impacting cellular responses and disease processes. (Ref.: Xu, Y-R., and Lei, C-Q. (2021). Front. Immunol. 11; 608976; Fan, Y., et al. (2012). Cell Signal. 24(7); 1381-1389; Ouyang, C., et al. (2014). J Biol Chem. 289(35), 24226-37).

Target molecular weight ~ 67 kDa observed; 67.19 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

KLH-conjugated linear peptide corresponding to 12 amino acids surrounding phosphoserine 412, from the Isoform-2/1A of human TAK1.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.