Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferpH: 7.2
Preservative: 0.02% Sodium azide
Constituents: 59% PBS, 40% Glycerol
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab221075 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC/IF||Use a concentration of 1 - 4 µg/ml.
Fixation/Permeabilization: PFA/Triton X-100
FunctionBinds 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.
Sequence similaritiesBelongs to the epsin family.
Contains 1 ENTH (epsin N-terminal homology) domain.
Contains 3 UIM (ubiquitin-interacting motif) repeats.
DomainThe NPF repeat domain is involved in EPS15 binding.
The DPW repeat domain is involved in AP2A2 and clathrin binding.
The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction with the AP-2 complex subunit AP2B1.
modificationsPhosphorylated 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.
Cellular localizationCytoplasm. Cell membrane. Nucleus. Membrane > clathrin-coated pit. Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145.
- Information by UniProt
- EH domain binding mitotic phosphoprotein antibody
- EH domain-binding mitotic phosphoprotein antibody
- EPN 1 antibody
ab221075 has not yet been referenced specifically in any publications.