Recombinant Escherichia coli Cation efflux system protein CusF (cusF)

Code CSB-YP304370ENV
MSDS
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Source Yeast
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Code CSB-EP304370ENV
MSDS
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Source E.coli
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Code CSB-EP304370ENV-B
MSDS
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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.
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Code CSB-BP304370ENV
MSDS
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Source Baculovirus
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Code CSB-MP304370ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
cusF
Uniprot No.
Alternative Names
cusF; cusX; ylcC; b0573; JW0562Cation efflux system protein CusF
Species
Escherichia coli (strain K12)
Expression Region
22-110
Target Protein Sequence
ANEHHHETM SEAQPQVISA TGVVKGIDLE SKKITIHHDP IAAVNWPEMT MRFTITPQTK MSEIKTGDKV AFNFVQQGNL SLLQDIKVSQ
Protein Length
Full Length of Mature Protein
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
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

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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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