Product Name	COPE
Chinese Name	外壳蛋白COPE单克隆抗体
Alias	COPE_HUMAN; Coatomer subunit epsilon; Epsilon-coat protein (Epsilon-COP); COPI coat complex subunit epsilon;
Immunogen Species	Mouse
Clonality	Monoclonal
Clone NO.	H12B9
React Species	Human
Applications	WB=1:2000-5000,ICC/IF=1:100-500 not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user.
Theoretical molecular weight	34kDa
Cellular localization	cytoplasmic The cell membrane
Form	Liquid
Concentration	1mg/ml
Lsotype	IgG1/Kappa
Purification	Affinity purified by Protein G
Buffer Solution	1M TBS(pH7.4) with 1% BSA, 3% Proclin300 and 50% Glycerol.
Storage	Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Attention	This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
PubMed	PubMed
Product Detail	The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles. It is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Coatomer complex consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] SWISS: O14579 Gene ID: 11316 Copine is a type of cytosolic protein complex that binds to dilysine motifs and reversibly associates with non-clathrin-coated vesicles of the Golgi apparatus, which further mediates the transport of biosynthetic proteins from the endoplasmic reticulum through the Golgi apparatus to the trans-Golgi network. The copine complex is essential for the budding of Golgi membranes and for the retrograde transport of dilysine-tagged proteins from the Golgi apparatus to the endoplasmic reticulum. In mammals, only membranes associated with ADP-ribosylation factors (ARFs) can recruit copines. ARFs are small GTP-binding proteins. This complex also affects the structural integrity of the Golgi apparatus, as well as the processing, activity, and endocytic recycling of the low-density lipoprotein receptor.

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