Aliases
Peptidyl-prolyl cis-trans isomerase SurA, PPIase SurA, Rotamase SurA, Survival protein A, b0053, JW0052, surA
Antibody Type
Polyclonal Antibody
Species
Escherichia coli
Uniprot ID
P0ABZ6
Immunogen
Recombinant Escherichia coli Chaperone SurA protein (21-428AA)
Raised In
Rabbit
Species Reactivity
Escherichia coli
Tested Applications
ELISA, WB;Not yet tested in other applications.
Background / Function
Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.
Isotype
IgG
Conjugate
Unconjugated
Storage Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze.
Purity
Caprylic Acid Ammonium Sulfate Precipitation purified
Modification
Chaperone SurA
Literature
[1]”The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.” Bitto E., McKay D.B. J. Biol. Chem. 278:49316-49322(2003). [2]”The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.” Behrens S., Maier R., de Cock H., Schmid F.X., Gross C.A. EMBO J. 20:285-294(2001). [3]”SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.” Rouviere P.E., Gross C.A. Genes Dev. 10:3170-3182(1996).
