4 天之前 · Phospho-ASK1 (Ser967) Antibody detects transfected ASK1 only when phosphorylated at serine 967. The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or …

2004年3月12日 · We found that treatment of COS7 cells with H 2 O 2 triggers dephosphorylation of Ser-967 through an okadaic acid-sensitive phosphatase, resulting in dissociation of the ASK1·14-3-3 complex with concomitant increase of ASK1 catalytic activity and ASK1-mediated activation of JNK and p38 pathways.

The apoptosis signal-regulating kinase-1 (ASK1) responds to oxidative stress by activating the Jun N-terminal kinase (JNK) and p38 map kinase pathways, which results in caspase activation and...

2017年12月1日 · Because S967 is a critical residue for determining the activation state of ASK1, multiple proteins converge to regulate the phosphorylation of this site. The upstream survival kinases IKKβ and PDK1 both enhance pS967, thereby inhibiting ASK1-mediated apoptosis (Bunkoczi et al., 2007, Goldman et al., 2004, Puckett et al., 2013, Seong et al., 2010).

Phospho-ASK1 (Ser967) Antibody detects transfected ASK1 only when phosphorylated at serine 967. Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues around serine 967 of human ASK1. Antibodies are puri ed by protein A and peptide a nity chromatography.

Although active Akt enhanced phosphorylation of ASK1 Ser967, overexpression of the dominant-negative Akt blunted IGF-1's ability to increase ASK1 phosphorylation (Fig. 2c). These results...

Invitrogen Anti-Phospho-ASK1 (Ser967) Polyclonal, Catalog # PA5-121348. Tested in Western Blot (WB) and ELISA (ELISA) applications. This antibody reacts with Human samples. Supplied as 100 µL purified antibody (1.18 mg/mL).

... determine whether IKK can directly catalyze the phosphor- ylation of ASK1 at Ser967, an in vitro kinase assay was performed. Interestingly, IKK, as well as IKK, phosphorylated immuno-...

We report here a direct interaction between inhibitor of B kinase (IKK) and apoptosis signal-regulating kinase 1 (ASK1), unveiling a critical node at the junction of survival, inflammation, and stress signaling networks. IKK can be activated by growth factor stimulation or tumor necrosis factor alpha engagement.

We found that treatment of COS7 cells with H 2 O 2 triggers dephosphorylation of Ser-967 through an okadaic acid-sensitive phosphatase, resulting in dissociation of the ASK1·14-3-3 complex with concomitant increase of ASK1 catalytic activity and ASK1-mediated activation of JNK and p38 pathways.