|Application ||WB, FC, E|
|Other Accession||P35603, Q7ZW98, Q801Q8, P84092, P84091, Q4R706, Q5ZMP6, Q3ZC13, NP_001020376.1, NP_004059.2|
|Predicted||Bovine, Chicken, Monkey, Rat, Xenopus, Zebrafish, C.Elegans|
|Calculated MW||49655 Da|
|Antigen Region||387-415 aa|
|Other Names||AP-2 complex subunit mu, AP-2 mu chain, Adaptin-mu2, Adaptor protein complex AP-2 subunit mu, Adaptor-related protein complex 2 subunit mu, Clathrin assembly protein complex 2 mu medium chain, Clathrin coat assembly protein AP50, Clathrin coat-associated protein AP50, HA2 50 kDa subunit, Plasma membrane adaptor AP-2 50 kDa protein, AP2M1, CLAPM1, KIAA0109|
|Target/Specificity||This AP2M1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 387-415 amino acids from the C-terminal region of human AP2M1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||AP2M1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X- X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane- associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (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|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a subunit of the heterotetrameric coat assembly protein complex 2 (AP2), which belongs to the adaptor complexes medium subunits family. The encoded protein is required for the activity of a vacuolar ATPase, which is responsible for proton pumping occurring in the acidification of endosomes and lysosomes. The encoded protein may also play an important role in regulating the intracellular trafficking and function of CTLA-4 protein. Two transcript variants encoding different isoforms have been found for this gene.
Kahlfeldt, N., et al. J. Biol. Chem. 285(4):2734-2749(2010)
Boucrot, E., et al. PLoS ONE 5 (5), E10597 (2010) :
Yoshida, T., et al. Int. J. Mol. Med. 24(2):233-246(2009)
Levecque, C., et al. Am. J. Physiol., Cell Physiol. 297 (1), C160-C168 (2009) :
Stanasila, L., et al. Mol. Pharmacol. 74(3):562-573(2008)
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