aer Antibody

Code CSB-PA342683XA01ENV
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Product Details

Full Product Name
Rabbit anti-Escherichia coli (strain K12) aer Polyclonal antibody
Uniprot No.
Target Names
aer
Alternative Names
aer; air; yqjJ; b3072; JW3043; Aerotaxis receptor
Raised in
Rabbit
Species Reactivity
Escherichia coli (strain K12)
Immunogen
Recombinant Escherichia coli (strain K12) aer protein
Immunogen Species
Escherichia coli (strain K12)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
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
Troubleshooting and 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

Function
Signal transducer for aerotaxis. The aerotactic response is the accumulation of cells around air bubbles. The nature of the sensory stimulus detected by this protein is the proton motive force or cellular redox state. It uses a FAD prosthetic group as a redox sensor to monitor oxygen levels.
Gene References into Functions
  1. Oxidized Aer activates CheA, whereas ASQ Aer reversibly inhibits CheA. PMID: 27803157
  2. These studies demonstrated trigonal interactions among the F1 linkers from three Aer monomers, presumably within trimer-of-dimer units, as well as binary interactions between subunits. PMID: 21097634
  3. Gain-of-function mutations are associated with the signalling pathway in the PAS domain of Aer. PMID: 20545849
  4. functional interactions between the PAS domain and the HAMP AS-2 helix are required for FAD binding and aerotactic signaling by Aer. PMID: 15489456
  5. Dimers also formed in mutants that did not bind flavin adenine dinucleotide and in truncated peptides without a signaling domain and part of the HAMP domain. PMID: 15489458
  6. Either the PAS or signalling domains could be deleted from the non-signalling subunit of the Aer heterodimer, but removing 16 residues from the C-terminus of the signalling subunit abolished aerotaxis. PMID: 16430703
  7. Mutations and truncations in the sequence encoding residues 15 to 21 introduced a range of phenotypes, including defects in FAD binding, constant tumbling motility, and an inverse response in which E. coli cells migrated away from oxygen concentrations PMID: 16513745
  8. EilA activates the genetically linked high molecular weight bacterial surface protein Air PMID: 16762026
  9. strong Aer responses to oxygen are associated with redox changes in NADH dehydrogenase I PMID: 16995896
  10. the overall membrane organization of Aer included a maximum of three Aer dimers, did not swap neighbors over time, and appeared to be constrained by interactions in the cytosolic signaling domain. PMID: 17693513
  11. Data confirmed that the Aer HAMP domain is composed of two alpha-helices separated by a structured loop and significance of the HAMP and proximal signaling domain structure for signal transduction is discussed. PMID: 18203838
  12. The aer mutant exhibited a decreased ability to colonize the intestine when compared to wild-type cells. PMID: 19130287

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Subcellular Location
Cell inner membrane; Multi-pass membrane protein. Note=Predominantly localized to one cell pole in mid-to-late exponential phase, with a few smaller foci elsewhere in the cell.
Database Links
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