Phospho-AP2M1 (Thr156) Antibody (YA2113)
(Synonyms: AP-2 complex subunit mu; AP-2 mu chain; Adapter-related protein complex 2 subunit mu; Adaptin-mu2; Clathrin assembly protein complex 2 mu medium chain; Clathrin coat assembly protein AP50)
Based on 1 Customer Validation
Phospho-AP2M1 (Thr156) Antibody (YA2113) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Phospho-AP2M1 (Thr156).
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:1000-1:5000 |
Product Details
Phospho-AP2M1 (Thr156) Antibody (YA2113) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Phospho-AP2M1 (Thr156).
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size：55 kD
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
A synthetic phosphopeptide corresponding to residues surrounding Thr156 of human AP2M1
Endogenous
Affinity Purified
Non-conjugated
Phosphorylated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Verification Images
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Western blot analysis of extracts from Hela (lane 2, 20 μg), Hela (lane 3, 20 μg, Calyculin A (HY-18983), 25 nM, 30 mins) as indicated using Phospho-AP2M1 (Thr156) antibody. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in TBST for 1 hour at room temperature. The primary antibody (1:1000) and Loading control antibody (GAPDH, HY-P80954A, 1/5000) was used in 5% Bovine Serum Albumin in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/5000) was used for 1 hour at room temperature.
Background
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Function
AP2M1 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. 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 Thr-156 in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1. Plays a role in endocytosis of frizzled family members upon Wnt signaling[1][2][3][4][5][6][7][8][9][10].
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Subcellular Localization
Cell membrane; Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side
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Expression
Tissue_specificity:Expression in the brain (protein level) -
Isoforms & Post-Translational Modification
Q96CW1 has 2 isomers: Q96CW1-1: 49655 Da (predicted); Q96CW1-2: 49389 Da (predicted).
Phosphorylation at Thr-156 increases the affinity of the AP-2 complex for cargo membrane proteins during the initial stages of endocytosis -
Subunit
Adapter protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1) (By similarity). Interacts with ATP6V1H and MEGF10 (PubMed:12032142, PubMed:17643423). Interacts with EGFR and TTGN1 (By similarity). Interacts with F2R (PubMed:16581796). Interacts with PIP5K1C; tyrosine phosphorylation of PIP5K1C weakens the interaction (By similarity). Interacts with KIAA0319; required for clathrin-mediated endocytosis of KIAA0319 (PubMed:19419997). Interacts with DVL2 (via DEP domain) (By similarity). Interacts with KCNQ1; mediates estrogen-induced internalization via clathrin-coated vesicles (PubMed:23529131). Interacts with P2RX4 (via internalization motif) (By similarity). Together with AP2A1 or AP2A2 and AP2B1, it interacts with ADAM10; this interaction facilitates ADAM10 endocytosis from the plasma membrane during long-term potentiation in hippocampal neurons (PubMed:23676497). Probably interacts with ACE2 (via endocytic sorting signal motif); the interaction is inhibited by ACE2 phosphorylation (PubMed:33436498). Interacts with RALBP1; the interaction is direct (PubMed:10910768). Interacts with TMEM106B (via N-terminus) (PubMed:25066864)
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SwissProt ID
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Synonyms
AP-2 complex subunit mu; AP-2 mu chain; Adapter-related protein complex 2 subunit mu; Adaptin-mu2; Clathrin assembly protein complex 2 mu medium chain; Clathrin coat assembly protein AP50
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Research Field
Signal Transduction
Documentation
References
[1]. Fraile-Ramos A, et al. Endocytosis of the viral chemokine receptor US28 does not require beta-arrestins but is dependent on the clathrin-mediated pathway. Traffic. 2003 Apr;4(4):243-53. [Content Brief]
[2]. Motley A, et al. Clathrin-mediated endocytosis in AP-2-depleted cells. J Cell Biol. 2003 Sep 1;162(5):909-18. [Content Brief]
[3]. Nakatsu F, et al. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct Funct. 2003 Oct;28(5):419-29. [Content Brief]
[4]. Huang F, et al. Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference. J Biol Chem. 2004 Apr 16;279(16):16657-61. [Content Brief]
[5]. Owen DJ, et al. Adaptors for clathrin coats: structure and function. Annu Rev Cell Dev Biol. 2004;20:153-91. [Content Brief]
[6]. Helbig I, et al. A Recurrent Missense Variant in AP2M1 Impairs Clathrin-Mediated Endocytosis and Causes Developmental and Epileptic Encephalopathy. Am J Hum Genet. 2019 Jun 6;104(6):1060-1072. [Content Brief]
[7]. Paing MM, et al. Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization. Mol Cell Biol. 2006 Apr;26(8):3231-42. [Content Brief]
[8]. Lau AW, et al. The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway. J Cell Sci. 2008 Dec 15;121(Pt 24):4008-17. [Content Brief]
[9]. Marcello E, et al. Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease. J Clin Invest. 2013 Jun;123(6):2523-38. [Content Brief]
[10]. Ricotta D, et al. Phosphorylation of the AP2 mu subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. J Cell Biol. 2002 Mar 4;156(5):791-5. [Content Brief]
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