Recombinant Human Epsin 1 protein (GST tag N-Terminus)
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Recombinant Human Epsin 1 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 550 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Epsin-1, EH domain-binding mitotic phosphoprotein, EPS-15-interacting protein 1, EPN1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Epsin 1 protein (GST tag N-Terminus) (AB162265)
ab162265 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Epsin 1 works as an endocytic accessory protein that plays a role in clathrin-mediated endocytosis facilitating the internalization of various receptors and membrane proteins. It interacts with clathrin and AP-2 adaptor complex helping to deform the membrane to form vesicles. Epsin 1 is known to bind phospholipids via its ENTH domain which is important for its function at the plasma membrane. This protein does not work alone and is part of larger protein complexes that include other proteins involved in vesicle formation and maturation.
Pathways
Epsin 1 participates in the endocytic pathway essential for the regulation of nutrient uptake and signaling receptor modulation. It coordinates with proteins such as dynamin and adaptin ensuring the proper invagination of the membrane and vesicle scission. Epsin 1 is also linked to the actin cytoskeleton affecting pathways linked to signal transduction and cellular organization.
Specifications
Form
Liquid
General info
Function
Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis (PubMed : 10393179, PubMed : 10557078).
Sequence similarities
Belongs to the epsin family.
Post-translational modifications
Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation.. Ubiquitinated.
Target data
Product promise
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