Recombinant Escherichia coli Chemotaxis protein CheA (cheA)

Code CSB-EP362114ENV
MSDS
Size $388
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
cheA
Uniprot No.
Research Area
Others
Species
Escherichia coli (strain K12)
Source
E.coli
Expression Region
1-654aa
Target Protein Sequence
MSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKQSQEPDAASFDYICQALRQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRSNESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQKMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSALQAINREQRMANTAA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
78.8 kDa
Protein Length
Full Length
Tag Info
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Form
Liquid or 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
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is 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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Function
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
Gene References into Functions
  1. Signaling complexes control CheA by altering its apparent rate constant of autophosphorylation. PMID: 28425142
  2. Differences were observed, however, in a keel-like density that we identify here as CheA kinase domains P1 and P2, the phosphorylation site domain and the binding domain for response regulator target proteins. PMID: 23802570
  3. Thus, these P1 phosphorylation domain mutants appear to define interaction determinants for P1-P4 docking during the CheA autophosphorylation reaction. PMID: 24163342
  4. crystal of CheA belonged to space group P1, with unit-cell parameters a = 59.271, b = 67.674, c = 82.815 A, alpha = 77.568, beta = 86.073, gamma = 64.436 degrees . The asymmetric unit may contain up to ten dimeric units of P3 four-helix bundles PMID: 21636905
  5. The fluorescence properties of CheA carrying a Phe455Trp replacement can be used to monitor ATP-binding events and a conformational change at the CheA protein histidine kinase active site. PMID: 15766267
  6. Results describe the ranges and kinetics of domain motions in the free CheA dimer. PMID: 19256549
  7. Specific CheA-short (CheA(S)) residues, L123 and L126, were identified as critical for CheZ binding. In the CheA(S) 'P1-CheZ nuclear magnetic resonance structure, these residues form an interaction surface on alpha-helix E in the 'P1 domain. PMID: 19581362

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Subcellular Location
Cytoplasm.
Database Links

KEGG: ecj:JW1877

STRING: 316407.1736547

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