COPE recombinant protein

COPE, 1-308aa, Human, His tag, E Coli

Cat. Num. AAA205926

• Gene Names: COPE; epsilon-COP
• Applications: SDS-Page
• Purity: > 90% by SDS-PAGE
• Synonyms: COPE; 1-308aa; Human; His tag; E Coli; Coatomer subunit epsilon; Coatomer protein complex; subunit epsilon; epsilon-COP; COPE recombinant protein

• Host: E Coli
• Purity/Purification: > 90% by SDS-PAGE
• Form/Format: Liquid, In Phosphate buffered saline (pH 7.4) containing 20% glycerol, 1mM DTT
• Concentration: 0.25 mg/ml (determined by Bradford assay) (varies by lot)
• Sequence: MGSSHHHHHH SSGLVPRGSH MGSMAPPAPG PASGGSGEVD ELFDVKNAFY IGSYQQCINE AQRVKLSSPE RDVERDVFLY RAYLAQRKFG VVLDEIKPSS APELQAVRMF ADYLAHESRR DSIVAELDRE MSRSVDVTNT TFLLMAASIY LHDQNPDAAL RALHQGDSLE CTAMTVQILL KLDRLDLARK ELKRMQDLDE DATLTQLATA WVSLATGGEK LQDAYYIFQE MADKCSPTLL LLNGQAACHM AQGRWEAAEG LLQEALDKDS GYPETLVNLI VLSQHLGKPP EVTNRYLSQL KDAHRSHPFI KEYQAKENDF DRLVLQYAPS A
• Sequence Length: 308

• Applicable Applications for COPE recombinant protein: SDS-PAGE
• Antigen Species: Human
• Tag Information: His-tag
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for COPE recombinant protein

COPE 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. Recombinant human COPE protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography techniques.

Product Categories/Family for COPE recombinant protein

Signal Transduction

References

Shima D.T., et al. (1999) Curr. Biol. 9:821-824

NCBI and Uniprot Product Information

• NCBI GI #: 31542319
• NCBI GeneID: 11316
• NCBI Accession #: NP_009194
• NCBI GenBank Nucleotide #: NM_007263.3
• UniProt Accession #: O14579; O76097; Q6IBB8; Q9UGP6; A6NE29; A6NKA3
• Molecular Weight: 36.9 kDa (331aa) confirmed by MALDI-TOF
• NCBI Official Full Name: coatomer subunit epsilon isoform a
• NCBI Official Synonym Full Names: coatomer protein complex subunit epsilon
• NCBI Official Symbol: COPE
• NCBI Official Synonym Symbols: epsilon-COP
• NCBI Protein Information: coatomer subunit epsilon
• UniProt Protein Name: Coatomer subunit epsilon
• Protein Family: Coatomer
• UniProt Gene Name: COPE
• UniProt Synonym Gene Names: Epsilon-COP

NCBI Description

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]

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. 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 with 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 ().