Datasheet

生物学的記述

Specificity	Phospho-MOB1 (Thr12) Antibody [F15P10] detects endogenous levels of total MOB1 protein only when it is phosphorylated at Thr12.
Background	Phospho-MOB1 (Thr12) designates the activated conformation of MOB1A/B adaptor proteins central to the Hippo tumor suppressor pathway that governs organ size, proliferation, and apoptosis through kinase cascade amplification. MOB1 organizes a compact globular fold with an N-terminal extension and core domain that undergoes phosphorylation at Thr12 by MST1/2 kinases, stabilizing an open conformation where the Switch helix dissociates to expose binding interfaces for LATS1/2 N-terminal regulatory regions. This phospho-Thr12 event allosterically activates LATS1/2 catalytic domains through dynamic scaffolding that juxtaposes MST-phosphorylated activation loops with MOB1 phospho-sites, enabling trans-phosphorylation that ramps up YAP/TAZ inhibitory serine phosphorylation for cytoplasmic retention and proteasomal degradation via β-TRCP ubiquitin ligase. Phospho-MOB1 further engages NDR1/2 kinases with differential affinity modulated by Thr12/Thr35 phosphates that pull N-terminal strands into β-sheet configurations stabilizing kinase-MOB complexes for mitotic exit and ploidy control. The resultant LATS-YAP/TAZ axis integrates upstream inputs, such as cell density and mechanotransduction, through Merlin-expanded sensing to transcriptionally repress CTGF, Cyr61, and c-Myc, thereby facilitating contact inhibition during epithelial morphogenesis. Phospho-MOB1 coordinates tissue homeostasis in liver regeneration and neural tube closure, with ubiquitous expression ensuring robust pathway fidelity across proliferative niches.

Specificity

Phospho-MOB1 (Thr12) Antibody [F15P10] detects endogenous levels of total MOB1 protein only when it is phosphorylated at Thr12.

Background

Phospho-MOB1 (Thr12) designates the activated conformation of MOB1A/B adaptor proteins central to the Hippo tumor suppressor pathway that governs organ size, proliferation, and apoptosis through kinase cascade amplification. MOB1 organizes a compact globular fold with an N-terminal extension and core domain that undergoes phosphorylation at Thr12 by MST1/2 kinases, stabilizing an open conformation where the Switch helix dissociates to expose binding interfaces for LATS1/2 N-terminal regulatory regions. This phospho-Thr12 event allosterically activates LATS1/2 catalytic domains through dynamic scaffolding that juxtaposes MST-phosphorylated activation loops with MOB1 phospho-sites, enabling trans-phosphorylation that ramps up YAP/TAZ inhibitory serine phosphorylation for cytoplasmic retention and proteasomal degradation via β-TRCP ubiquitin ligase. Phospho-MOB1 further engages NDR1/2 kinases with differential affinity modulated by Thr12/Thr35 phosphates that pull N-terminal strands into β-sheet configurations stabilizing kinase-MOB complexes for mitotic exit and ploidy control. The resultant LATS-YAP/TAZ axis integrates upstream inputs, such as cell density and mechanotransduction, through Merlin-expanded sensing to transcriptionally repress CTGF, Cyr61, and c-Myc, thereby facilitating contact inhibition during epithelial morphogenesis. Phospho-MOB1 coordinates tissue homeostasis in liver regeneration and neural tube closure, with ubiquitous expression ensuring robust pathway fidelity across proliferative niches.

使用情報

Application

WB

Dilution

WB

1:1000

Reactivity

Human, Mouse, Rat, Monkey

Source

Rabbit Monoclonal Antibody

MW

24 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/27335147/
https://pubmed.ncbi.nlm.nih.gov/26108669/

Application Data

WB

Validated by Selleck

Lane 1: Ramos, Lane 2: Ramos (λ phosphatase treated)