Datasheet

生物学的記述

Specificity	Phospho-Elk-1 (Ser383) Antibody [P22B17] detects endogenous levels of total Elk-1 protein only when it is phosphorylated at Ser383.
Background	Phospho-Elk-1 at Ser383 marks the activated form of the ETS-domain transcription factor Elk-1, a ternary complex factor that partners with serum response factor (SRF) to bind serum response elements (SREs) in immediate early gene promoters. Elk-1 features an N-terminal ETS DNA-binding domain, a B-box for SRF interaction, and a C-terminal transactivation domain rich in serine/threonine phosphorylation sites. Mitogen-activated protein kinases (MAPKs), particularly ERK1/2, phosphorylate Ser383 and adjacent Ser389 within this domain, with Ser383 serving as the primary site for ERK specificity and transcriptional potentiation. This phosphorylation enhances pre-existing Elk-1-p300 interactions through the C-terminal region and p300 N-terminus, while generating novel binding interfaces that recruit p300's histone acetyltransferase activity for chromatin remodeling and SRE-driven gene activation like c-fos. JNK/SAPK also targets Ser383, driving stress-responsive transcription, whereas CAMK4, p38, and PAK1 contribute under diverse stimuli. Phospho-Ser383-Elk-1 localizes to mitotic spindle poles from metaphase to telophase, interacting with Aurora-A kinase to facilitate pole positioning, before shifting to the midbody in cytokinesis; Aurora inhibitors disrupt this localization, retaining it on DNA. Ser383 phosphorylation couples growth factor/stress signals to rapid immediate early gene induction, supporting proliferation, survival, and cell cycle progression. Dysregulation links to brain tumors where elevated phospho-Elk-1 correlates with aggressive proliferation, and Alzheimer's, where inhibition ameliorates pathology.

Specificity

Phospho-Elk-1 (Ser383) Antibody [P22B17] detects endogenous levels of total Elk-1 protein only when it is phosphorylated at Ser383.

Background

Phospho-Elk-1 at Ser383 marks the activated form of the ETS-domain transcription factor Elk-1, a ternary complex factor that partners with serum response factor (SRF) to bind serum response elements (SREs) in immediate early gene promoters. Elk-1 features an N-terminal ETS DNA-binding domain, a B-box for SRF interaction, and a C-terminal transactivation domain rich in serine/threonine phosphorylation sites. Mitogen-activated protein kinases (MAPKs), particularly ERK1/2, phosphorylate Ser383 and adjacent Ser389 within this domain, with Ser383 serving as the primary site for ERK specificity and transcriptional potentiation. This phosphorylation enhances pre-existing Elk-1-p300 interactions through the C-terminal region and p300 N-terminus, while generating novel binding interfaces that recruit p300's histone acetyltransferase activity for chromatin remodeling and SRE-driven gene activation like c-fos. JNK/SAPK also targets Ser383, driving stress-responsive transcription, whereas CAMK4, p38, and PAK1 contribute under diverse stimuli. Phospho-Ser383-Elk-1 localizes to mitotic spindle poles from metaphase to telophase, interacting with Aurora-A kinase to facilitate pole positioning, before shifting to the midbody in cytokinesis; Aurora inhibitors disrupt this localization, retaining it on DNA. Ser383 phosphorylation couples growth factor/stress signals to rapid immediate early gene induction, supporting proliferation, survival, and cell cycle progression. Dysregulation links to brain tumors where elevated phospho-Elk-1 correlates with aggressive proliferation, and Alzheimer's, where inhibition ameliorates pathology.

使用情報

Application

WB

Dilution

WB

1:1000

Reactivity

Human

Source

Mouse Monoclonal Antibody

MW

45 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/23322625/
https://pubmed.ncbi.nlm.nih.gov/12514134/

Phospho-Elk-1 (Ser383) Antibody [P22B17]

生物学的記述

使用情報

References

Application Data