PA1-061 detects Golgi beta-coatomer protein (beta-COP) from mouse, human and rat tissues.
PA1-061 has been successfully used in Western blot and immunofluorescence procedures. By Western blot, this antibody detects an ~110kDa protein which represents beta-COP from rat brain homogenate. Indirect immunofluorescence staining of beta-COP in NIH-3T3 cells with PA1-061 results in beta-COP localization to the Golgi complex and to distinct vesicular structures scattered throughout the cytoplasm. Golgi localization of beta-COP is sensitive to treatment with brefeldin A or ATP depletion.
The PA1-061 immunogen is a synthetic peptide corresponding to residues E(496) A G E L K P E E E I T V G P V Q K(513) of rat beta-COP. This sequence is completely conserved in human beta-COP.
Figure 1 illustrates immunolocalization of beta-COP in NIH-3T3 cells using PA1-061.
Figure 2 illustrates Western blot detection of beta-COP from rat brain homogenate using PA1-061. |
Coatomer proteins are involved in regulating transport between the endoplasmic reticulum (ER) and the Golgi complex and in intra-Golgi transport. There exist two coatomer-protein mechanisms (COPI and COPII) and although they have mechanistic parallels, they are molecularly distinct. The COPI coat is comprised of seven subunits (alpha-, beta-, beta'-, gamma-, delta-, epsilon-, and zeta-COP) in a complex called coatomer. Assembly of the coatomer (COPI) onto non-clathrin coated vesicles is regulated by ADP-ribosylation factor (ARF). Vesicle formation, budding, fusion, and disassembly is dependent on GDP-GTP exchange, COPI, and ARF. COPI has been shown to facilitate retrograde intracellular transport from the ER to the Golgi complex. By contrast, COPII facilitates anterograde transport between these subcellular organelles. COPII has been shown to be independently and selectively recruited to the ER relative to COPI subunits. |
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