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>   首页   >   产品   >   一抗   >   其他   >   COPB Recombinant Rabbit mAb   

COPB Recombinant Rabbit mAb

     
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, IHC-F, IF, E
Primary Accession P53618
Other Accession P53618
Reactivity Rat, Human, Mouse
Host Rabbit
Clonality Recombinant
Calculated MW 107142 Da
Isotype IgG
Purity affinity purified by Protein A
Buffer 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
SIMILARITY Contains 6 HEAT repeats.
SUBUNIT Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts (via C-terminus) with HIV-1 Nef; the interaction is direct. Interacts with SCYL1. Interacts with COPG1. Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct. Interacts with KCNK2/TREK (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2/TREK. Interacts with anthrax lethal factor (LF); this interaction may facilitate endosomal vesicle membrane translocation of LF and its release from the lumen of endosomal vesicles to external milieu. Interacts with CAPN8 and PRKCE (By similarity). Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes (By similarity).
Post-translational modifications Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.
Background Descriptions 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. [provided by RefSeq, Jan 2009],
Additional Information
Gene ID 1315
Other Names BARMACS; COPB; COPB_HUMAN; COPB1; Beta-coat protein (Beta-COP); Q6GTT7_HUMAN; COPB_RAT; coat protein complex I subunit beta 1; COPI coat complex subunit beta 1; coatomer protein complex, subunit beta; coatomer protein complex, subunit beta 1; Coatomer subunit beta (Beta-coat protein) (Beta-COP); Coatomer subunit beta; Beta-coat protein; Beta-COP
Dilution IHC-P=1:50-200,IHC-F=1:50-200,WB=1:500-2000,IF=1:50-200,ELISA=1:5000-10000
StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name COPB1 (HGNC:2231)
Synonyms COPB
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 {ECO:0000250|UniProtKB:Q9JIF7}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity) 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 (PubMed:20362547) {ECO:0000250|UniProtKB:P23514, ECO:0000269|PubMed:20362547}
Research Areas
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