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

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human

Source
Mouse Monoclonal Antibody

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

Predicted MW
45 kDa

Datasheet & SDS

Biological Description

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

Clone
P22B17

Synonym(s)
ETS domain-containing protein Elk-1, ELK1

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%