cusF Antibody

Code CSB-PA304370XA01ENV
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Product Details

Full Product Name
Rabbit anti-Escherichia coli (strain K12) cusF Polyclonal antibody
Uniprot No.
Target Names
cusF
Alternative Names
cusF antibody; cusX antibody; ylcC antibody; b0573 antibody; JW0562Cation efflux system protein CusF antibody
Raised in
Rabbit
Species Reactivity
Escherichia coli (strain K12)
Immunogen
Recombinant Escherichia coli (strain K12) cusF 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
Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.
Gene References into Functions
  1. We therefore recommend the use of CusF as a viable alternative to MBP or GST as a fusion protein/affinity tag for the production of soluble recombinant proteins in E. coli. PMID: 26805756
  2. Arabidopsis with cell wall-, cytosol- and vacuole-targeted CusF had increased Cu accumulation; in particular, plants expressing CusF in the cytoplasm transport Cu from roots to shoots more efficiently than plants with cell wallor vacuole-targeted CusF. PMID: 24951313
  3. N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF. PMID: 22812620
  4. Data reveal that N-terminal region of CusB interacts with metal-binding face of CusF; these proteins transiently interact in a metal-dependent fashion. PMID: 21323389
  5. Electron paramagnetic resonance (EPR) spectroscopy has been used to structurally characterize the copper-binding site in CusF protein from Escherichia coli PMID: 15770503
  6. CusF has a topology and metal binding site that are unique among copper proteins and provide insight into its function. PMID: 16060662
  7. The binding of CuI and AgI to CusF using isotheromal titration calorimetry and NMR spectroscopy is reported. PMID: 16964970
  8. In the CusF-Ag(I) structure, Ag(I) is coordinated by two methionines and a histidine, with a nearby tryptophan capping the metal site. Measurements on the CusF-Cu(I) complex show a similar environment for Cu(I). PMID: 17893365
  9. CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan PMID: 18157124

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Subcellular Location
Periplasm.
Database Links
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