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AP2A1 Antibody (C-term) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession O95782
Clone Names 100430282
Additional Information
Gene ID 160
Other Names AP-2 complex subunit alpha-1, 100 kDa coated vesicle protein A, Adaptor protein complex AP-2 subunit alpha-1, Adaptor-related protein complex 2 subunit alpha-1, Alpha-adaptin A, Alpha1-adaptin, Clathrin assembly protein complex 2 alpha-A large chain, Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit, AP2A1, ADTAA, CLAPA1
Target/Specificity The synthetic peptide sequence used to generate the antibody AP13905b was selected from the C-term region of AP2A1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name AP2A1
Synonyms ADTAA, CLAPA1
Function 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. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). 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 (By similarity).
Cellular Location Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV
Tissue Location Expressed in the brain (at protein level) (PubMed:23676497). Isoform A: Expressed in forebrain, skeletal muscle, spinal cord, cerebellum, salivary gland, heart and colon. Isoform B: Widely expressed in tissues and also in breast cancer and in prostate carcinoma cells.
Research Areas
Citations (0)
citation

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Background

This gene encodes the alpha 1 adaptin subunit of theadaptor protein 2 (AP-2) complex found in clathrin coated vesicles.The AP-2 complex is a heterotetramer consisting of two largeadaptins (alpha or beta), a medium adaptin (mu), and a smalladaptin (sigma). The complex is part of the protein coat on thecytoplasmic face of coated vesicles which links clathrin toreceptors in vesicles. Alternative splicing of this gene results intwo transcript variants encoding two different isoforms. A thirdtranscript variant has been described, but its full length naturehas not been determined.

References

Mitchell, R.S., et al. J. Virol. 82(16):7758-7767(2008)Kitagawa, Y., et al. Virology 373(1):171-180(2008)Stove, V., et al. J. Virol. 79(17):11422-11433(2005)Lu, W., et al. Neuron 47(3):407-421(2005)Pope, S.N., et al. J. Steroid Biochem. Mol. Biol. 94 (1-3), 203-208 (2005) :

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$ 277.78
Cat# BP13905b
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