Search Thermo Fisher Scientific
Search Thermo Fisher Scientific
Invitrogen
MA1-25064 detects alpha Adaptin from human, rat, and bovine samples.
MA1-25064 has been successfully used in Western blot procedures. The antibody reacts with polypeptides of approximately 100 kDa in bovine liver, human heart fibroblasts, MDBK cells, but not with any components in the 110-115 kDa range from these sources or from rat PC12 cells, neuroblastoma or astrocytes. The antibody stains the intact alpha adaptor, as well as the 37 and 40 kDa fragments, but not the 63-66 kDa group of alpha fragments obtained by trypsin cleavage of the alpha subunits molecules. Not tested in other applications.
The MA1-25064 immunogen is AP2 polypeptides from bovine brain.
Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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