Anti-GroEL antibody produced in rabbit

GroEL protein belongs to the folding chaperonin family. It is a 58.3 kDa protein with apical, intermediate and equatorial functional domains.

purified recombinant GroEL produced in E. coli.

Anti-GroEL antibody produced in rabbit has been used as positive control in histology and immunohistochemistry of Dirofilaria immitis, nematode worms and in the western blot analysis of the HeLa cells.

GroEL, together with GroES, in the presence of ATP, assists in protein folding. Co-expression of aldehyde dehydrogenase with GroEL/GroES promotes folding and higher production of protein in soluble form. GroES and GroEL bind to the protein substrate, enclosing it in a cage like fold. The target protein after folding gets dissociated from the cage and is accompanied with hydrolysis of adenosine triphosphate (ATP) to adenosine diphosphate (ADP).

The antibody does not cross-react with GroES and bovine HSP 70.

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

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