|Other Names||Coatomer subunit beta', Beta'-coat protein, Beta'-COP, p102, COPB2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).|
|Cellular Location||Cytoplasm, cytosol. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi.|
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Provided below are standard protocols that you may find useful for product applications.
The Golgi coatomer complex (see MIM 601924) constitutesthe coat of nonclathrin-coated vesicles and is essential for Golgibudding and vesicular trafficking. It consists of 7 proteinsubunits, including COPB2.
Kim, E., et al. Biochem. Biophys. Res. Commun. 395(2):244-250(2010)Guo, Y., et al. Mol. Biol. Cell 19(7):2830-2843(2008)Rikova, K., et al. Cell 131(6):1190-1203(2007)Tu, L.C., et al. Mol. Cell Proteomics 6(4):575-588(2007)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :
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