Recombinant E.Coli Methyl-Accepting Chemotaxis Protein I (TSR) Protein (His)

Name: Recombinant E.Coli Methyl-Accepting Chemotaxis Protein I (TSR) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10556P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant E.Coli Methyl-Accepting Chemotaxis Protein I (TSR) Protein (His) is produced by our Yeast expression system. This is a cytoplasmic protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P02942
Target Symbol	TSR
Synonyms	tsr; cheD; b4355; JW4318Methyl-accepting chemotaxis protein I; MCP-I; Serine chemoreceptor protein
Species	Escherichia coli (strain K12)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	WFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF
Expression Range	211-551aa
Protein Length	Cytoplasmic Domain
Mol. Weight	38.0kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cell inner membrane; Multi-pass membrane protein. Note=Found predominantly at cell poles.
Database References	KEGG: ecj:JW4318 STRING: 316407.85677095

Gene Functions References

this study shows that Tsr interacts with IL-8 provoking E. coli transmigration across human lung epithelial cells PMID: 27506372
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
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
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
Phe396 governs conformational changes of tsr. PMID: 24335957
Alterations in the symmetry of the two branches of the cytoplasmic hairpin of tsr seriously compromise chemoreceptor function. PMID: 22111959
Mutant Tsr molecules with a charged amino acid or proline replacement exhibited the most severe trimer formation defects. PMID: 21965562
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
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
serine ligand binding increased rate of methylation PMID: 15516567
Tsr responds to changes in proton motive force PMID: 16995896
Architecture of receptor assemblies is in intact Escherichia coli is described. PMID: 17327165
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
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
Expansion of polyQ to 13Q in Tsr has no significant effect on chemotaxis. PMID: 18667570
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
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
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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.