COPE Human

Coatomer Protein Complex Subunit Epsilon Human Recombinant
Cat. No.
BT1261
Source
Escherichia Coli.
Synonyms
Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

COPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 36.9kDa.
COPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Coatomer Protein Complex Subunit Epsilon, also known as COPE, is an epsilon subunit of the coatomer protein complex. Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly interacts with Golgi non-clathrin-coated vesicles. COPE is essential for vesicle budding from Golgi membranes and the retrograde transport of dilysine-tagged proteins from the Golgi to the ER. The coatomer complex comprises at least seven subunits: alpha, beta, beta', gamma, delta, epsilon, and zeta. Several alternatively spliced transcript variants encoding different isoforms of COPE have been identified.
Description
Recombinant human COPE protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 331 amino acids (residues 1-308) and having a molecular mass of 36.9 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The COPE protein solution is provided at a concentration of 0.25 mg/ml and contains phosphate-buffered saline (pH 7.4), 20% glycerol, and 1 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is recommended. Multiple freeze-thaw cycles should be avoided.
Purity
The purity of the COPE protein is greater than 90.0% as determined by SDS-PAGE analysis.
Synonyms
Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.
Source
Escherichia Coli.
Amino Acid 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.

Product Science Overview

Structure and Function

The coatomer complex is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles . It is essential for the budding of vesicles from Golgi membranes and is involved in the retrograde transport of dilysine-tagged proteins from the Golgi to the ER . The coatomer complex consists of at least seven subunits: alpha, beta, beta’, gamma, delta, epsilon, and zeta .

Gene and Protein Information

The COPE gene, located on chromosome 19 (19p13.11), encodes the epsilon subunit of the coatomer complex . This gene is expressed in various tissues, including the anterior pituitary, adrenal glands, thyroid gland, stomach, pancreas, and salivary glands . The protein encoded by the COPE gene is involved in several biological processes, including vesicle-mediated transport, protein transport, and maintaining Golgi structural integrity .

Biological Significance

The coatomer complex, including the epsilon subunit, is crucial for the proper functioning of the secretory pathway. It influences the processing, activity, and endocytic recycling of LDL receptors and other proteins . In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins .

Clinical Relevance

Mutations or dysregulation of the COPE gene can lead to various diseases. For instance, COPE has been associated with Cepacia Syndrome . Understanding the function and regulation of the COPE gene and its protein product is essential for developing therapeutic strategies for diseases related to vesicle transport and protein trafficking.

Research and Applications

Recombinant human COPE protein is used in research to study its role in intracellular transport and its interactions with other proteins. It is also used to investigate the mechanisms underlying diseases associated with coatomer complex dysfunction.

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