Recombinant Escherichia coli Methyl-accepting chemotaxis protein I (tsr)

Code CSB-EP355908ENV
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Source E.coli
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Code CSB-EP355908ENV-B
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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-BP355908ENV
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Source Baculovirus
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Code CSB-MP355908ENV
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
tsr
Uniprot No.
Research Area
Others
Alternative Names
tsr; cheD; b4355; JW4318Methyl-accepting chemotaxis protein I; MCP-I; Serine chemoreceptor protein
Species
Escherichia coli (strain K12)
Expression Region
211-551aa
Target Protein Sequence
WFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF
Mol. Weight
37.9kD
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
Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids.; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
Gene References into Functions
  1. this study shows that Tsr interacts with IL-8 provoking E. coli transmigration across human lung epithelial cells PMID: 27506372
  2. results indicate that, rather than being essential for proper receptor-receptor interaction, the "glycine hinge" residues are involved in the ability of the receptor to switch between different signaling states. Mainly, the C-helix residue G439 has a key role in shifting the equilibrium toward a kinase-activating conformation. PMID: 28664727
  3. These results indicate that the E402 and R404 residues of Tsr play their most critical signaling roles at their inner locations near the trimer axis where they likely participate in stabilizing the trimer-of-dimer packing and the kinase-ON state of core signaling complexes. PMID: 28215934
  4. The authors suggest that the Tsr control cable transmits input signals to a four-helix HAMP bundle by modulating the intensity of structural clashes between out-of-register transmembrane helix and AS1 helix of HAMP. PMID: 27019297
  5. Phe396 governs conformational changes of tsr. PMID: 24335957
  6. Alterations in the symmetry of the two branches of the cytoplasmic hairpin of tsr seriously compromise chemoreceptor function. PMID: 22111959
  7. Mutant Tsr molecules with a charged amino acid or proline replacement exhibited the most severe trimer formation defects. PMID: 21965562
  8. The results suggest a helix extension mechanism of Tsr transmembrane signaling in which TM2 piston motions influence HAMP stability by modulating the helicity of the control cable segment. PMID: 21803986
  9. The findings of this study provide strong support for a three-state dynamic bundle model of HAMP domain signalling in Tsr, and possibly in other bacterial transducers as well. PMID: 21306449
  10. serine ligand binding increased rate of methylation PMID: 15516567
  11. Tsr responds to changes in proton motive force PMID: 16995896
  12. Architecture of receptor assemblies is in intact Escherichia coli is described. PMID: 17327165
  13. Most I241 lesions locked Tsr signal output in the kinase-on mode, implying that this residue is responsible mainly for stabilizing the kinase-off signaling state. PMID: 18621896
  14. The current study, utilizing a Tsr-GFP fusion protein and time-lapse fluorescence microscopy of individual cell lineages, demonstrates that Tsr accumulates approximately linearly with time at the cell poles PMID: 18647166
  15. Expansion of polyQ to 13Q in Tsr has no significant effect on chemotaxis. PMID: 18667570
  16. Amino acid replacements of two conserved residues at the tip of the trimer contact region of Tsr caused differing interactions with CheA and CheW. PMID: 18931127
  17. chemoreceptors are organized as trimers of receptor dimers and display two distinct conformations that differ principally in arrangement of the HAMP domains within each trimer PMID: 18940922
  18. The authors propose that Tsr HAMP controls output signals by modulating destabilizing phase clashes between the AS2 helices and the adjoining kinase control helices. PMID: 19656294

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Subcellular Location
Cell inner membrane; Multi-pass membrane protein. Note=Found predominantly at cell poles.
Database Links

KEGG: ecj:JW4318

STRING: 316407.85677095

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