2012年1月20日 · An affinity probe derived from necrosulfonamide and coimmunoprecipitation using anti-RIP3 antibodies both identified the mixed lineage kinase domain-like protein (MLKL) as the interacting target. MLKL was phosphorylated by RIP3 at the threonine 357 and serine 358 residues, and these phosphorylation events were critical for necrosis.

2021年6月22日 · MLKL kinase-like domain dimerization interrupts the monomeric conformation and induces oligomerization of full-length MLKL, suggesting a serial activation model of MLKL mediated...

Proteintech's Rabbit Recombinant Phospho-MLKL (Ser358) antibody is validated in WB, ELISA and shows reactivity with human samples.

2022年9月29日 · MLKL undergoes RIPK3-mediated phosphorylation at threonine 357/serine 358 in human and serine 345 in mouse, shown by purple circles. In addition, MLKL can be ubiquitinated at different lysine ...

2017年7月18日 · Activation of the pseudokinase mixed lineage kinase domain-like (MLKL) upon its phosphorylation by the protein kinase RIPK3 triggers necroptosis, a form of programmed cell death in which rupture of cellular membranes yields release of intracellular components.

Phospho-MLKL (Thr357/Ser358) recognizes endogenous levels of MLKL protein only when phosphorylated at Thr357 and Ser358. This antibody can recognize single phosphorylation sites at Thr357 or Ser358, or when dually phosphorylated at both sites.

mlkl是tnf（肿瘤坏死因子）诱导的坏死性凋亡过程中的关键靶标，它作为ripk1和ripk3下游的效应蛋白发挥作用。 RIPK3在Ser227位点被磷酸化，此磷酸化为MLKL激活所必需。

在当前研究中，我们开发了特异性检测人类MLKL蛋白在细胞坏 死途径中第357位苏氨酸和358位丝氨酸磷酸化的单克隆抗体。通过一 系列的生化试验，我们发现necrosome从胞浆向质膜和细胞器膜上转位， 这种转变使MLKL在磷酸化驱使的聚合后获得与脂质直接结合的能力。

2024年7月19日 · RIPK3激活后，会进一步磷酸化并激活混合谱系激酶样结构域（MLKL）。 MLKL 是坏死性凋亡的执行者。 被激活的MLKL会转位至细胞膜，插入并形成孔道，导致细胞膜的破裂和细胞内容物的泄露。 对该信号通路进行总结： 死亡受体激活 （如TNF受体）→ RIPK1激活并与RIPK3结合 形成坏死小体→ RIPK3磷酸化MLKL → MLKL转位至细胞膜 并形成孔道→ 细胞膜破裂 和细胞内容物泄露→炎症反应. 坏死性凋亡信号通路的调控机制和临床 相关性 仍在研究中，其 …

An affinity probe derived from necrosulfonamide and coimmunoprecipitation using anti-RIP3 antibodies both identified the mixed lineage kinase domain-like protein (MLKL) as the interacting target. MLKL was phosphorylated by RIP3 at the threonine 357 and serine 358 residues, and these phosphorylation events were critical for necrosis.