|Application ||WB, E|
|Other Accession||P62944, Q9DBG3, P63009, Q08DS7, NP_001025177.1, NP_001273.1|
|Predicted||Bovine, Mouse, Rat|
|Calculated MW||104553 Da|
|Antigen Region||517-546 aa|
|Other Names||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, AP2B1, ADTB2, CLAPB1|
|Target/Specificity||This AP2B1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 517-546 amino acids from the Central region of human AP2B1.|
|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||AP2B1 Antibody (Center) 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 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.|
|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|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is one of two large chain components of the assembly protein complex 2, which serves to link clathrin to receptors in coated vesicles. The encoded protein is found on the cytoplasmic face of coated vesicles in the plasma membrane. Two transcript variants encoding different isoforms have been found for this gene.
Kahlfeldt, N., et al. J. Biol. Chem. 285(4):2734-2749(2010)
Hood, F.E., et al. J. Cell. Sci. 122 (PT 13), 2185-2190 (2009) :
Grass, B., et al. Histopathology 54(7):873-879(2009)
Keyel, P.A., et al. Mol. Biol. Cell 19(12):5309-5326(2008)
Rikova, K., et al. Cell 131(6):1190-1203(2007)
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