Coatomer subunit gamma-2 (COPG2) Recombinant Protein | COPG2 recombinant protein

Recombinant Human Coatomer subunit gamma-2 (COPG2) , partial

• Gene Names: COPG2; 2-COP; gamma-2-COP
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Coatomer subunit gamma-2 (COPG2); Recombinant Human Coatomer subunit gamma-2 (COPG2); partial; COPG2 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Length: 726

• Species: Human
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

NCBI and Uniprot Product Information

• NCBI GI #: 585866346
• NCBI GeneID: 26958
• NCBI Accession #: NP_001276962.1
• NCBI GenBank Nucleotide #: NM_001290033.1
• UniProt Accession #: Q9UBF2; Q2NLA0; Q54AC3; Q8WVW8; A6NH74
• Molecular Weight: 81,483 Da
• NCBI Official Full Name: coatomer subunit gamma-2 isoform 2
• NCBI Official Synonym Full Names: coatomer protein complex subunit gamma 2
• NCBI Official Symbol: COPG2
• NCBI Official Synonym Symbols: 2-COP; gamma-2-COP
• NCBI Protein Information: coatomer subunit gamma-2
• UniProt Protein Name: Coatomer subunit gamma-2
• Protein Family: Coatomer
• UniProt Gene Name: COPG2
• UniProt Synonym Gene Names: Gamma-2-COP

Uniprot Description

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 ().