This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This COPG antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 721-750 amino acids from the C-terminal region of human COPG.
COPG
Reactivity: Human
WB, ELISA
Host: Rabbit
Polyclonal
Biotin
Application Notes
WB: 1:1000
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Expiry Date
6 months
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: "Large-scale mapping of human protein-protein interactions by mass spectrometry. ..." in: Molecular systems biology, Vol. 3, pp. 89, (2007) (PubMed).
Rohde, Cheong, Konrad, Paiha, Mayinger, Boehmelt: "The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex." in: The Journal of biological chemistry, Vol. 278, Issue 52, pp. 52689-99, (2003) (PubMed).
Target
COPG
(Coatomer Protein Complex, Subunit gamma (COPG))
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).