Human ARCN1 protein (Recombinant) (N-His) (STJP008169)

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STJP008169
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Host: E. coli
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description : Recombinant-Human ARCN1-N-His protein was developed from e. coli and has a target region of N-His. For use in research applications.
Formulation: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol: ARCN1
Gene ID: 372
Uniprot ID: COPD_HUMAN
Immunogen Region: Ser273-Leu511
Immunogen: Homo sapiens (Human)
Function Component of the coatomer, 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. The 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.
Protein Name Coatomer Subunit Delta
Archain
Delta-Coat Protein
Delta-Cop
Database Links Reactome: R-HSA-6807878
Reactome: R-HSA-6811434
Cellular Localisation Cytoplasm
Golgi Apparatus Membrane
Peripheral Membrane Protein
Cytoplasmic Side
Cytoplasmic Vesicle
Copi-Coated Vesicle Membrane
The Coatomer Is Cytoplasmic Or Polymerized On The Cytoplasmic Side Of The Golgi
As Well As On The Vesicles/Buds Originating From It
Alternative Protein Names Coatomer Subunit Delta protein
Archain protein
Delta-Coat Protein protein
Delta-Cop protein
ARCN1 protein
COPD protein

Information sourced from Uniprot.org

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