Recombinant Escherichia coli Protein tonB (tonB), partial

Code CSB-YP360914ENV
MSDS
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Source Yeast
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Code CSB-EP360914ENV
MSDS
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Source E.coli
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Code CSB-EP360914ENV-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-BP360914ENV
MSDS
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Source Baculovirus
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Code CSB-MP360914ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
tonB
Uniprot No.
Alternative Names
tonB; exbA; b1252; JW5195; Protein TonB
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
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.

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Target Background

Function
Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment.
Gene References into Functions
  1. The TonB system embodies a novel means of active transport across the outer membrane for nutrients. PMID: 26283773
  2. Avian pathogenic Escherichia coli DeltatonB mutants are safe and protective live-attenuated vaccine candidates. PMID: 25205199
  3. This study has demonstrated that TonB is essential for virulence in avian pathogenic Escherichia coli. PMID: 22237011
  4. These observations supported the hypothesis that ExbD couples TonB to the protonmotive force, with concomitant transitions of ExbD and TonB periplasmic domains from unenergized to energized heterodimers. PMID: 22100395
  5. ExbD-TonB interactions required ExbD transmembrane domain residue D25. PMID: 21984795
  6. TonB with asparagine substitution for His20 is fulluy active. PMID: 21665976
  7. Taken together, these results indicate that the solved dimeric crystal structures of TonB do not exist in vivo. PMID: 21179522
  8. 92-residue C-terminal fragment of TonB from Escherichia coli structure shown by x-ray crystallography PMID: 15522863
  9. after input of protonmotive force mediated through ExbB/D and the TonB transmembrane domain, the TonB carboxy-terminus can form a meta-stable high-energy conformation that is not represented by the crystal structure of the carboxy-terminus. PMID: 15612934
  10. the TonB box binds to TonB-CTD along the beta3-strand PMID: 15644214
  11. Analyses of two recombinant TonB species in complex with FhuA reveals that TonB undergoes a kinetically limiting rearrangement upon initial interaction with FhuA: an intermediate TonB-FhuA complex of 1:1 stoichiometry is detected. PMID: 15736954
  12. Results indicate that TonB-CTD binding to the TonB box was interfered by FecA N-terminal domain and a loss of its secondary structure would expose TonB surface area for additional intermolecular interactions. PMID: 16718599
  13. In order to obtain additional information on the nature of TonB-dependent outer membrane active transport, we solved the structure of the C-terminal domain of TonB in complex with the cobalamin transporter BtuB PMID: 16741124
  14. A complex of BtuB and a fragment ofTonB was formed in the presence of the substrate cyanocobalamin and calcium and was crystallized. PMID: 16820681
  15. This study reports a novel mechanism in which TonB acts as a scaffold, directing FhuD to regions within the periplasm where it is poised to accept and deliver siderophore. PMID: 16928679
  16. interaction of TonB, an inner membrane protein, with an outer membrane transporter based upon a recent crystal structure of a TonB-transporter complex PMID: 17449669
  17. TonB Q160 region may be part of a large disordered region required to span the periplasm and contact an OM transporter. PMID: 17483231
  18. the role of the TonB-ExbB-ExbD complex, potentiated by the proton motive force, is to reduce the affinity of the Cbl-binding site, thus increasing the rate of Cbl release into the periplasmic space PMID: 17908684
  19. Proton-motive force is required for the interaction of ExbD and TonB periplasmic domains trapped by formaldehyde cross-linking. PMID: 19627500
  20. TonB interacts with BtuF, suppporting a model wherein TonB serves as a scaffold to optimally position BtuF for initial binding of cyanocobalamin and for its subsequent release. PMID: 19708689

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Subcellular Location
Cell inner membrane; Single-pass membrane protein; Periplasmic side.
Protein Families
TonB family
Database Links
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