Form
Liquid
Buffer
Ascites
Preservative
0.1% Sodium azide
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Antigen Species
Bovine
Immunogen
AP-2 adaptor protein from bovine brain.
Purification
Unpurified
Conjugation
Unconjugated
RRID
AB_381316
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
adaptor related protein complex 1 subunit beta 1
Background
Coated vesicle populations contain, besides clathrin, the adaptor complexes AP1 and AP2, also known as HAI (HA1) adaptor and HAII (HA2) adaptor or Assembly Protein 1 (AP1) and Assembly Protein 2 (AP2), respectively. Interest has focused on adaptors because they are known to mediate the interaction between clathrin and components of the membrane. Their location between the clathrin shell and the membrane, as revealed by cryoelectron microscopy, is consistent with such a function. In the cell, clathrin-adaptor interactions proceed in a very controlled and specific manner, leading to coated structures each containing only one type of adaptor. Clathrin-coated membranes at or originating from the plasma membrane contain the AP2 adaptor, while the AP1 adaptor appears to be largely restricted to clathrin-coated membranes of the trans-Golgi network. AP1 adaptor consists of four subunits termed beta 1 (formerly beta prime, 110 kDa), gamma (100 kDa), μ1 (47 kDa, and omega 1 (20 kDa). AP2 is made up of two 100-110 kDa polypeptides, termed alpha and beta 2 (formerly beta) subunits, μ2 (50 kDa), and s2 (17 kDa) subunit. Alpha and beta 2 subunits (alpha and beta 2 adaptins) behave in standard SDS-PAGE like 100-112 kDa polypeptides. Four alpha isoforms (alpha a1, alpha a2, alpha c1 and alpha c2) which are highly homologous in sequence have been described. ?1 and ?2 adaptins are highly homologous which suggests that the beta type adaptor chains may mediate the interaction of their adaptors with the highly conserved clathrin molecule. The alpha and gamma adaptins share only 25% overall identity. The other adaptor subunits of the two adaptor complexes which appear to be unrelated, are believed to possess binding sites for different cargo molecules (receptors) and for proteins which might regulate the complex functions of the adaptors. Monoclonal antibodies reacting specifically against adaptor proteins are useful tools for studies on the intracellular distribution and structural relationship of adaptor complexes.
Database
Research Area
