Anti-GroES antibody produced in rabbit

GroES, also known as chaperonin 10 (cpn10), is a highly characterized member of a class of ubiquitous and conserved E. coli proteins known as chaperonins. GroES is a homoheptamer protein, composed of 10 kDa subunits forming a ring.

Does not cross-react with GroEL.

recombinant GroES produced in E. coli coupled to KLH.

Anti-GroES antibody produced in rabbit has been used in immunoblotting.

Anti-GroES antibody produced in rabbit is suitable for use as a primary antibody in immunoblotting using different cellular fractions of Vibrio parahaemolyticus strains grown under sub-lethal heat and osmotic stress. It is suitable for dot blot at a working dilution of 1:5000 using 100ng recombinant GroES/dot, for indirect ELISA at a working dilution of 1:15,000 using recombinant GroES protein and for indirect immunoblotting at a working dilution of 1:5000 using a heat shocked E. coli cell extract. It is also suitable for indirect ELISA at a working dilution of 1:5000 using recombinant GroES protein.

GroES is a belongs to a class of ubiquitous and conserved E. coli proteins known as chaperonins. These chaperonins are involved in ATP-dependent protein folding and they enhance the yield of properly folded proteins under unfavourable conditions of spontaneous folding. GroES is present in the form of a ring made up of homo-heptamer protein composed of 10kDa subunits. One ring of GroES binds to two rings of GroEL, a tetradecamer protein of 58kDa subunits with a K⁺ dependent ATPase activity. This binding occurs in the presence of adenine nucleotides to form an asymmetric complex of GroES7-ADP-GroEL7-GroEL7. The folding reaction by GroEL is due to the cycles of binding and release of the co-chaperone GroES, which in turn alternate with binding and release of unfolded protein substrate.

Solution in in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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