Adaptin δ Mouse anti-Human, Unlabeled, Clone: 18, BD

Descripción

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 through AP-4), which are associated with the vesicle coats. These coatomers contain two large adaptin proteins (γ, α, δ, ε and β1, β2, β3, 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. In the AP-3 complex, adaptin δ contains an N-terminal “head” domain that has 25% identity with adaptins α and γ, while its C-terminal “hinge” and “ear” domains are two-fold larger and more divergent as compared to the same domains in adaptins α and γ. Adaptin δ is widely expressed and its mutation results in protein storage deficiencies within lysosomal-related organelles in platelets, melansomes, and synaptic vesicles

Host Species: Mouse
Clone: 18
Isotype: IgG1
Species Reactivity: Human
Immunogen: Human Adaptin δ aa. 627-731
Formula Weight [Chemical]: 160kDa

Immunofluorescence, Western Blotting