copA Antibody

Code CSB-PA710518XA01ENV
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Product Details

Full Product Name
Rabbit anti-Escherichia coli (strain K12) copA Polyclonal antibody
Uniprot No.
Target Names
copA
Alternative Names
copA antibody; atcU antibody; f834 antibody; ybaR antibody; b0484 antibody; JW0473Copper-exporting P-type ATPase antibody; EC 7.2.2.8 antibody; Copper-exporting P-type ATPase A antibody; Cu(+)-exporting ATPase antibody; Soluble copper chaperone CopA(Z) antibody
Raised in
Rabbit
Species Reactivity
Escherichia coli (strain K12)
Immunogen
Recombinant Escherichia coli (strain K12) copA protein
Immunogen Species
Escherichia coli (strain K12)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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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
  1. 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
  2. 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
  3. 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
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