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You are here:Home » Antibodies » Antibodies-Heat Shock Proteins » Anti -GroES

Anti -GroES


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Clone Host Grade Applications
Polyclonal Rabbit B IP
GroEL and GroES are E.coli chaperonins, which are homologs of mitochondrial chaperonins Hsp60 and Hsp10. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding with an ATP-dependent mechanism. A proposed nested model for cooperatively in ATP binding by GroEL suggests that each ring of GroEL is in equilibrium between a tense protein-acceptor (T) state and a relaxed protein-release (R) state. The T state has low affinity for ATP and high affinity for unfolded polypeptide substrates whereas the R state has a high affinity for ATP and low affinity for unfolded polypeptides substrates (2). Recent electron cryomicroscopy data demonstrates that the GroEL double-ring particle is in equilibrium between three allosteric states TT, TR and RR (3). Non-native conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroidís central cavity. It has been proposed that binding of ATP and GroES to a polypeptide substrate-bound GroEL ring creates a GroES-GroEL cis (ìbulletí) complex triggering release of the polypeptide into the space sequestered underneath GroES where it can fold. Negative cooperatively between rings with respect to ATP, helps to ensure that binding of an unfolded protein to the trans ring of an ADP bullet precedes binding of the encapsulated GroES molecule thereby allowing a new reaction cycle to begin. Recent data demonstrates that optimization of the allosteric properties of GroEL reflect the cellís need to handle a wide range of substrates with different folding rates, propensities to aggregate and affinities for the T state of GroEL (4). In addition to their roles in protein folding and translocation GroEL and GroES participa in protein degradation of most proteins requires ATP but the biochemical basis for this energy requirement is unclear. It has been suggested that GroEL and GroES may function together with proteases during the degradation process by preventing aggregation of the unfolded substrates and promoting their unfolding or helping to maintain them in a conformation which can be readily digested by cellular proteases (5).
Western Blot (Colorimetric) (7): 1:5,000
Western Blot (ECL) (6): 1:500
Immunoprecipitation: 1:200
Optimal dilutions to be determined by researcher.
Positive Controls:
Recombinant E. coli GroES Protein
Catalog #G8980-25
Clone TypePolyclonal
SourceE. coli
ImmunogenPurified chromatographically from an E. coli strain overexpressing GroES
SpecificityDetects a ~10kD protein, corresponding to the apparent molecular mass of GroES on SDS-PAGE immunoblots, in samples from E. coli. This antibody has not been tested for crossreactivity to other bacterial species.
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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