Adaptin β Mouse, Unlabeled, Clone: 74, BD

Description

• Sorting of integral membrane proteins at various stages of the endocytic and secretory pathways is mediated by vesicular trafficking between a variety of organelles
• Two sorting signals are tyrosine-based and dileucine-based signals that interact with heterotetrameric adaptor protein complexes (AP-1, AP-2, AP-3, and AP-4), which are associated with the vesicle coats
• These coatomers contain two large Adaptin proteins (γ, α,δ or ε and β1, β2, β3, or β4, respectively) that are noncovalently linked to one medium chain (μ1, μ2, μ3, or μ4) and one small chain (σ1, σ2, σ3, or σ4)
• The AP-1 and AP-3 complexes are involved in protein sorting from the TGN and endosomes, while AP-2 adaptor complexes are involved in clathrin-mediated endocytosis
• β Adaptin subunits (β1, β2, β3, β4) lack sequence homology to adaptins α, γ, δ and ε, but all of these subunits share a similar domain structure
• Adaptin β1 (also known as Adaptin β′) and β2 (also known as Adaptin β) have 83% amino acid identity and are found in the AP1 and AP2 complexes, respectively
• Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting