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AP2S1 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P53680 |
| Other Accession | P62744, P62743, Q17QC5, NP_004060.2, NP_067586.1 |
| Reactivity | Human |
| Predicted | Bovine, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 17018 Da |
| Antigen Region | 36-64 aa |
| Gene ID | 1175 |
|---|---|
| Other Names | AP-2 complex subunit sigma, Adaptor protein complex AP-2 subunit sigma, Adaptor-related protein complex 2 subunit sigma, Clathrin assembly protein 2 sigma small chain, Clathrin coat assembly protein AP17, Clathrin coat-associated protein AP17, HA2 17 kDa subunit, Plasma membrane adaptor AP-2 17 kDa protein, Sigma2-adaptin, AP2S1, AP17, CLAPS2 |
| Target/Specificity | This AP2S1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 36-64 amino acids from the Central region of human AP2S1. |
| Dilution | WB~~1:1000 |
| 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 | AP2S1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | AP2S1 (HGNC:565) |
|---|---|
| Synonyms | AP17, CLAPS2 |
| 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 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). May also play a role in extracellular calcium homeostasis. |
| Cellular Location | Cell membrane {ECO:0000250|UniProtKB:P63010}. 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 {ECO:0000250|UniProtKB:P63010} |
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Provided below are standard protocols that you may find useful for product applications.
Background
One of two major clathrin-associated adaptor complexes, AP-2, is a heterotetramer which is associated with the plasma membrane. This complex is composed of two large chains, a medium chain, and a small chain. This gene encodes the small chain of this complex. Alternative splicing has been observed in this gene and results in two known transcripts.
References
Stove, V., et al. J. Virol. 79(17):11422-11433(2005)
Lu, W., et al. Neuron 47(3):407-421(2005)
Collins, B.M., et al. Cell 109(4):523-535(2002)
Yano, H., et al. J. Neurosci. 21 (3), RC125 (2001) :
Pearse, B.M., et al. Curr. Opin. Struct. Biol. 10(2):220-228(2000)
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