AP2m1 (Adaptor-related Protein Complex 2 mu 1, Clathrin Assembly Protein Complex 2) Recombinant, Human

AP2M1 is a subunit of the heterotetrameric coat assembly protein complex 2 (AP2), which belongs to the adaptor complexes medium subunits family. This protein is required for the activity of a vacuolar ATPase, which is responsible for proton pumping occurring in the acidification of endosomes and lysosomes. It may also play an important role in regulating the intracellular trafficking and function of CTLA-4 protein.\n\nDescription: \nRecombinant Human AP2M1 produced in E.Coli is a non-glycosylated, polypeptide chain containing amino acids (1-435) and having a total molecular mass of 50kD. Recombinant AP2M1 contains T7 tag at N-terminus and is purified by proprietary chromatographic techniques.\n\nApplications: \n

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SPECIFICATIONS

Catalog Number

A2298-51H

Size

2ug

Form

Supplied as a liquid in 10mM Tris, pH 8.0, 0.1% Triton X-100 and 0.002% sodium azide.

Purity

(same/more than) 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. Endocytosis of the glucose transporter GLUT8 is mediated by interaction of a dileucine motif with the {beta}2-adaptin subunit of the AP-2 adaptor complex. J Cell Sci 2006 Jun 1;119(Pt 11):2321-31 2. Analysis of the AP-2 adaptor complex and cargo during clathrin-mediated endocytosis. Traffic 2005 Jul;6(7):539-47 3. Binding of AP-2 adaptor complex to brain membrane is regulated by phosphorylation of proteins. Biochem Biophys Res Commun 2005 May 13;330(3):695-700 4. The small G-protein Arf6GTP recruits the AP-2 adaptor complex to membranes. J Biol Chem 2005 Jun 3;280(22):21661-6 5. Internalization of pseudorabies virus glycoprotein B is mediated by an interaction between the YQRL motif in its cytoplasmic domain and the clathrin-associated AP-2 adaptor complex. J Virol 2004 Aug;78(16):8852- 9 6. Human reticulon 1-A and 1-B interact with a medium chain of the AP-2 adaptor complex. Cell Mol Biol (Noisy-le-grand) 2003;49 Online Pub:OL467-71