COPG1 rabbit pAb
ENT-A8851
Description
| REF | ENT-A8851 |
|---|---|
| Category | Antibody Polyclonal |
| Description | COPG1 rabbit pAb |
| Source | Rabbit |
| Applications | WB;ELISA |
| Reactivity | Human;Mouse;Rat |
| Reactivity | Human;Mouse;Rat |
| Dilution | WB 1:500-2000 ELISA 1:5000-20000 |
| Immunogen | Synthesized peptide derived from part region of human protein |
| Storage Stability | -20°C/1 year |
| Clonality | Polyclonal |
| Isotype | IgG |
| Concentration | 1 mg/ml |
| Observed Band KD | 96kD |
| Human Gene ID | 22820 |
| Human Swiss Prot Nº | Q9Y678 |
| Subcellular Location | Cytoplasm . Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasmic vesicle, COPI-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Predominantly located in the cis-Golgi apparatus. . |
Other Name:
Background: 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.,similarity:Belongs to the COPG family.,similarity:Contains 4 HEAT repeats.,subcellular location:The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.,subunit:Oligomeric complex that consists of at least the alpha, beta, beta’, gamma, delta, epsilon and zeta subunits. Interacts with ZNF289/ARFGAP2 through its C-terminal appendage domain.,