Recombinant E.Coli Methyl-Accepting Chemotaxis Protein Ii (TAR) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-10101P

Greater than 90% as determined by SDS-PAGE.
Recombinant E.Coli Methyl-Accepting Chemotaxis Protein Ii (TAR) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-10101P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant E.Coli Methyl-Accepting Chemotaxis Protein Ii (TAR) Protein (His-SUMO) is produced by our E.coli expression system. This is a cytoplasmic protein. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | P07017 |
Target Symbol | TAR |
Synonyms | tar; cheM; b1886; JW1875Methyl-accepting chemotaxis protein II; MCP-II; Aspartate chemoreceptor protein |
Species | Escherichia coli (strain K12) |
Expression System | E.coli |
Tag | N-6His-SUMO |
Target Protein Sequence | IRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTNKPQTPSRPASEQPPAQPRLRIAEQDPNWETF |
Expression Range | 212-553aa |
Protein Length | Cytoplasmic Domain |
Mol. Weight | 52.0kDa |
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-aspartate and related amino and dicarboxylic acids. Tar also mediates taxis to the attractant maltose via an interaction with the periplasmic maltose binding protein. Tar mediates taxis away from the repellents cobalt and nickel.; 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:JW1875 STRING: 316385.ECDH10B_2027 |
Gene Functions References
- Thus, the proportion of polypeptide chain that is locally and presumably transiently disordered is a structural feature of cytoplasmic domain dynamics that varies with functional region and modification-induced signaling state. PMID: 27318193
- There is a differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues. PMID: 25445668
- the Tar(FO) modules demonstrate that trimerized signaling tips self-associate, bind CheA and CheW, and facilitate conversion of CheA to an active conformation. PMID: 25967982
- Residues at the cytoplasmic end of transmembrane helix 2 determine the signal output of the Tar chemoreceptor. PMID: 23495653
- Such inversion is enabled by opposing pH sensing by the two major chemoreceptors, Tar and Tsr, such that the relative strength of the response is modulated by adaptive receptor methylation. PMID: 23078189
- Here we report the overexpression system for aCB2 in Escherichia coli C43(DE3) facilitated by two fusion partners: Mistic and TarCF, a C-terminal fragment of the bacterial chemosensory transducer Tar at the C-terminal of the CB2 open reading frame region. PMID: 22406258
- characterization of structural features of carboxyl-terminal 40 residues of Tar; identifed carboxyl-terminal linker between receptor body and the pentapeptide is an unstructured, disordered segment that can serve as a flexible arm and enzyme tether PMID: 21858888
- Ligand specificity is determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar PMID: 21979954
- Tar molecules with the cytoplasmic methylation and kinase control domains of Tsr still sensed phenol as an attractant. PMID: 21965561
- The cytoplasmic domains of Tar and Tsr receptors are close to each other near the trimer contact region at the cytoplasmic tip. PMID: 21174433
- These results with Tar-EnvZ hybrid receptor mutants suggest that intersubunit interactions in the HAMP linker normally mediate signal transduction through both subunits in a sensor dimer. PMID: 15316026
- mutations in the protein motifs of Tar significantly reduced the ability of the transmembrane domains to dimerize PMID: 15330757
- The tryptophan residues flanking the second transmembrane helix of Tar, especially Trp-209, are crucial in setting the baseline activity and ligand sensitivity of this chemoreceptor. PMID: 15667220
- assisted adaptational modification (methylation, demthylation and deamidation) in vitro of Trg chemorecptor PMID: 15916610
- polar localization of Tar fused to green fluorescent protein is influenced by its own amidation (methylation) state and the expression of another chemoreceptor (Tsr) PMID: 16267289
- Data show that Tar can be readily mutated to respond to new chemical signals, but that the overall change in specificity depends on the target compound. PMID: 16359703
- The pentapeptide linker in Tar is important for chemotaxis because of its role in adaptational modification. PMID: 16573695
- The fundamental mechanism of transmembrane signaling is conserved between homodimeric sensor kinases (with NarX) and chemoreceptors. PMID: 16707686
- Data suggest that Tar()-Tsr* suppression most likely occurs through compensatory changes in the conformation or dynamics of a mixed receptor signaling complex, presumably based on trimer-of-dimer interactions. PMID: 16751275
- The organization of these receptor/signaling complexes is determined by conserved interactions between the constituent chemotaxis proteins and may represent the active form in vivo. PMID: 16973743
- A mutational analysis of Tar residues 505-548 reveals that the more of this region is deleted, the less sensitive Tar is to inhibition by aspartate. PMID: 19053273