|Application ||WB, E|
|Other Accession||P23514, D2SW95, Q9JIF7, A0JN39, NP_001137533.1, NP_001137534.1, NP_057535.1|
|Predicted||Bovine, Mouse, Pig, Rat|
|Calculated MW||107142 Da|
|Antigen Region||351-380 aa|
|Other Names||Coatomer subunit beta, Beta-coat protein, Beta-COP, COPB1, COPB|
|Target/Specificity||This COPB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 351-380 amino acids from the Central region of human COPB1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||COPB1 Antibody (Center) is for research use only and 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. Plays a functional role in facilitating the transport of kappa- type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments.|
|Cellular Location||Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane. Endoplasmic reticulum- Golgi intermediate compartment. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By similarity). Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity). Occasionally present at the trans-side of Golgi, but mainly present at the cis- Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity) Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity). Some association with high- density and low-density microsomes and mitochondria/nuclei fraction (By similarity). Very little found in plasma membrane fraction (By similarity).|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a protein subunit of the coatomer complex associated with non-clathrin coated vesicles. The coatomer complex, also known as the coat protein complex 1, forms in the cytoplasm and is recruited to the Golgi by activated guanosine triphosphatases. Once at the Golgi membrane, the coatomer complex may assist in the movement of protein and lipid components back to the endoplasmic reticulum. Alternatively spliced transcript variants have been described.
Burman, J.L., et al. J. Biol. Chem. 283(33):22774-22786(2008)
Lippincott-Schwartz, J., et al. Trends Cell Biol. 16 (10), E1-E4 (2006) :
Huang, L., et al. Mol. Biol. Rep. 29(3):317-323(2002)
Paulsson, K.M., et al. J. Biol. Chem. 277(21):18266-18271(2002)
Sullivan, B.M., et al. Mol. Biol. Cell 11(9):3155-3168(2000)
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