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Western blot analysis of Adaptin γ on PC12 cell lysate. Lane 1: 1:5000, lane 2: 1:10000, lane 3: 1:20000 dilution of anti-Adaptin γ.
Immunofluorescent staining of Rat Neurons with anti-Adaptin γ antibody.
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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. Adaptin γ shows more homology with Adaptin α than with Adaptin β. The conserved regions between Adaptins γ and α could be important for binding to other components of the AP-1 and AP-2 complexes, respectively.
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Refer to manufacturer's instructions for use and related User Manuals and Technical Data Sheets before using this product as described.
Comparisons, where applicable, are made against older BD technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.