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COPG Antibody (C-term)

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - COPG Antibody (C-term) AP19908b
    All lanes : Anti-COPG Antibody (C-term) at 1:1000 dilution Lane 1: A2058 whole cell lysate Lane 2: K562 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 98 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
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, E
Primary Accession Q9Y678
Other Accession NP_057212.1
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 97718 Da
Additional info
Gene ID 22820
Other Names Coatomer subunit gamma-1, Gamma-1-coat protein, Gamma-1-COP, COPG1, COPG
Target/Specificity 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.
Dilution WB~~1:1000
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.
StorageMaintain 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.
PrecautionsCOPG Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name COPG1
Synonyms COPG
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. 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 triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity).
Cellular Location Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=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.
Research Areas

BACKGROUND

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).

REFERENCES

Pinheiro, A.P., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. 153B (5), 1070-1080 (2010) :
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :
Lippincott-Schwartz, J., et al. Trends Cell Biol. 16 (10), E1-E4 (2006) :
Watson, P.J., et al. Traffic 5(2):79-88(2004)
Rohde, H.M., et al. J. Biol. Chem. 278(52):52689-52699(2003)

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