Human AP2B1 protein (Recombinant) (N-His) (STJP006636)

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STJP006636
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Host: E. coli
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description : Recombinant-Human AP2B1-N-His protein was developed from e. coli and has a target region of N-His. For use in research applications.
Formulation: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol: AP2B1
Gene ID: 163
Uniprot ID: AP2B1_HUMAN
Immunogen Region: Met1-Phe266
Immunogen: Homo sapiens (Human)
Post Translational Modifications Phosphorylation at Tyr-737 by SRC occurs at the plasma membrane in clathrin-coated vesicles (CCVs).
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. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins.at least some clathrin-associated sorting proteins (CLASPs) are recognized by their DE-X(1,2)-F-X-X-FL-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly.clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly.
Protein Name Ap-2 Complex Subunit Beta
Ap105b
Adaptor Protein Complex Ap-2 Subunit Beta
Adaptor-Related Protein Complex 2 Subunit Beta
Beta-2-Adaptin
Beta-Adaptin
Clathrin Assembly Protein Complex 2 Beta Large Chain
Plasma Membrane Adaptor Ha2/Ap2 Adaptin Beta Subunit
Database Links Reactome: R-HSA-167590
Reactome: R-HSA-177504
Reactome: R-HSA-182218
Reactome: R-HSA-2132295
Reactome: R-HSA-3928665
Reactome: R-HSA-416993 P63010-1
Reactome: R-HSA-437239
Reactome: R-HSA-5099900
Reactome: R-HSA-5140745
Reactome: R-HSA-8856825
Reactome: R-HSA-8856828
Reactome: R-HSA-8866427
Reactome: R-HSA-8964038
Reactome: R-HSA-9679191
Cellular Localisation Cell Membrane
Membrane
Coated Pit
Peripheral Membrane Protein
Cytoplasmic Side
Ap-2 Appears To Be Excluded From Internalizing Ccvs And To Disengage From Sites Of Endocytosis Seconds Before Internalization Of The Nascent Ccv
Alternative Protein Names Ap-2 Complex Subunit Beta protein
Ap105b protein
Adaptor Protein Complex Ap-2 Subunit Beta protein
Adaptor-Related Protein Complex 2 Subunit Beta protein
Beta-2-Adaptin protein
Beta-Adaptin protein
Clathrin Assembly Protein Complex 2 Beta Large Chain protein
Plasma Membrane Adaptor Ha2/Ap2 Adaptin Beta Subunit protein
AP2B1 protein
ADTB2 protein
CLAPB1 protein

Information sourced from Uniprot.org