tsr Antibody

Code CSB-PA355908XA01ENV
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Product Details

Full Product Name Rabbit anti-Escherichia coli (strain K12) tsr Polyclonal antibody
Uniprot No. P02942
Target Names tsr
Alternative Names tsr antibody; cheD antibody; b4355 antibody; JW4318Methyl-accepting chemotaxis protein I antibody; MCP-I antibody; Serine chemoreceptor protein antibody
Raised in Rabbit
Species Reactivity Escherichia coli (strain K12)
Immunogen Recombinant Escherichia coli (strain K12) tsr protein
Immunogen Species Escherichia coli (strain K12)
Conjugate Non-conjugated
Clonality Polyclonal
Isotype IgG
Purification Method Protein A/G
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 ELISA Protocol
Troubleshooting and FAQs Antibody 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

(From Uniprot)
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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