Home
Protein
Recombinant Protein
Recombinant Escherichia coli Copper-exporting P-type ATPase A (copA), partial

Recombinant Escherichia coli Copper-exporting P-type ATPase A (copA), partial

Code	CSB-YP710518ENV
MSDS	MSDS
Size	Pls inquire
Source	Yeast
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-EP710518ENV
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-EP710518ENV-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-BP710518ENV
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-MP710518ENV
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
Have Questions?	Leave a Message or Start an on-line Chat

Product Details
Related Products
Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

copA

Uniprot No.

Q59385

Alternative Names

copA; atcU; f834; ybaR; b0484; JW0473Copper-exporting P-type ATPase; EC 7.2.2.8; Copper-exporting P-type ATPase A; Cu(+)-exporting ATPase; Soluble copper chaperone CopA(Z)

Species

Escherichia coli (strain K12)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

■ Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function

Exports Cu(+) from the cytoplasm to the periplasm. Binds 2 Cu(+) ions per monomer, which are transferred to periplasmic copper chaperone CusF upon ATP hydrolysis. In vitro an excess of CusF over CopA is required for efficient transfer. May also be involved in silver export.; mRNA is subject to programmed ribosomal frameshifting which produces a cytoplasmic copper chaperone CopA(Z) that corresponds to the first HMA domain. The soluble form is essential for cell survivial in the presence of CuSO(4); in growth competition experiments between wild-type and a version that prevents expression of CopA(Z) after 50 generations the non-CopA(Z) version is nearly extinct. The first HMA domain (residues 1-70) can be replaced by B.subtilis Cu chaperone CopZ.

Gene References into Functions

CopA chaperone is expressed in E. coli from the same gene that encodes the transporter. Some ribosomes translating copA undergo programmed frameshifting, terminate translation in the -1 frame, and generate the 70 aa-long polypeptide CopA(Z), which helps cells survive toxic copper concentrations. The high efficiency of frameshifting is achieved by the combined stimulatory action of a "slippery" sequence, an mRNA pseudoknot PMID: 28107647
The distal N-terminal metal-binding domain transfers copper to the membrane-integral ion-binding sites of CopA, while the proximal metal-binding domain has a regulatory role by suppressing the catalytic activity of CopA in absence of copper. PMID: 25899340
copper-transporting ATPases, CopA and ATP7A, in both bacteria and macrophage are unique determinants of bacteria survival and identify an unexpected role for copper at the host-pathogen interface PMID: 19808669

Subcellular Location

[Copper-exporting P-type ATPase]: Cell inner membrane; Multi-pass membrane protein.; [Isoform Soluble copper chaperone CopA(Z)]: Cytoplasm.

Protein Families

Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily

Database Links

KEGG: ecj:JW0473

STRING: 316385.ECDH10B_0441

Promotions