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Rabbit anti-Human COPB1 Polyclonal Antibody

The antibody against COPB1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 460-740 of human COPB1 (NP_057535.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IF/ICC, ELISA.

ADA-01561A

The antibody against COPB1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 460-740 of human COPB1 (NP_057535.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IF/ICC, ELISA.

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Specifications


Cat.No ADA-01561A ClonalityPolyclonal
Host SpeciesRabbitTarget NameCOPB1
Target SynonymsCOPB; BARMACS; COPB1FormLiquid
Species ReactivityHuman, Mouse, RatIsotypeIgG
Storage Buffer50% Glycerol, PBS with 0.02% sodium azide, pH7.3.Purification MethodAffinity purification
Positive SamplesNIH/3T3, A549ApplicationELISA, WB, IF/ICC

Immunogen Information


Immunogen DescriptionRecombinant fusion protein containing a sequence corresponding to amino acids 460-740 of human COPB1 (NP_057535.1).Target SpeciesHuman
Uniprot IDP53618Immunogen Sequence
Background Information
  • Uniprot Id

    P53618

  • Target Species

    Human

  • Target Name

    COPB1

  • Target Full Name

    Coatomer subunit beta

  • Target 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. 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.

  • Target Subcellular 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.

  • Target Synonyms

    Beta-coat protein; Beta-COP; betacop; Coatomer beta subunit; Coatomer protein complex subunit beta 1; Coatomer protein complex subunit beta; Coatomer subunit beta; COPB; COPB_HUMAN; Copb1; DKFZp761K102; FLJ10341

  • Target Background

    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.

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