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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.
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Western Blot analysis of ENZ-ABS714: Lane 1: MW Marker, Lane 2: GroEL (E. coli), (recombinant) (Prod. No. ADI-SPP-610), Lane 3: E. coli lysate.
| Regulatory Status |
RUO – Research Use Only |
|---|
Related Products
| Application | ELISA, IHC, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Mouse |
HSP60 (human), (recombinant)
ADI-SPP-540
Recombinant human HSP60 that functions as a mitochondrial chaperone for protein folding and assembly.
| Alternative Name | Chaperonin 60, CPN60, HspD1, Heat shock protein 60 |
|---|---|
| Purity | ≥90% (SDS-PAGE; Western blot) |
| Source | Produced in E. coli. |
GroEL (E. coli), (recombinant)
ADI-SPP-610
Recombinant GroEL (E. coli) that acts as a molecular chaperone, assisting protein folding and preventing aggregation.
| Alternative Name | Heat shock protein 60, 60kDa Chaperonin, Protein Cpn60 GroEL protein, HSP60 |
|---|---|
| Purity | ≥90% (SDS-PAGE; Western blot) |
| Source | Produced in E. coli. |
Last modified: May 29, 2024