This polyclonal antibody recognizes the inner membrane protein SbmA of Gram-negative bacteria. The SbmA protein is a homodimeric secondary transporter protein, that is involved in the transport of microcins B17 and J25, glycopeptide antibiotic bleomycin, proline-rich antimicrobial peptides of prokaryotic and eukaryotic origin, antisense peptide phosphodiamidate morpholino oligomers and peptide nucleic acids (PNA) into the E.coli cytoplasm. This protein is found in a large number of Gram-negative and also Gram-positive microorganisms, including plant and animal pathogens. The monomeric SbmA protein contains 406 amino acids (about 50 kDa) and has 8 transmembrane regions. The homodimeric complex present in the membrane closely resembles the membrane-spanning region of the ATP-binding cassette transporter family. Peptide transport mediated by SmbA is driven by a electrochemical gradient. SbmA-mediated internalization of peptide substrates suggest that the transport of an unknown substrate(s) represents the function of this protein.
Immuno precipitation, Western blot
W: The band size to be expected is ~37 kDa under reducing conditions.
For Western blotting dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:50.
Recombinant SbmA or E.coli lysate