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Hsp60 is a member of the chaperonin family of heat shock proteins, with homologs functioning in the cytosol and mitochondria to fold nascent and aggregated proteins. Hsp60 is the eukaryotic homolog of the E. coli GroEL protein, and forms a multimeric complex in the mitochondria with Hsp10 (Cpn10) to form a large central cavity in which ATP-dependent protein folding takes place. TRiC/CCT, a eukaryotic relative of Hsp60, is expressed in the cytosol and participates in the folding of actin and tubulin substrates, but lacks any association with an Hsp10-like co-factor.
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Western Blot Analysis of ADI-SPA-829: Lane 1: HSP60 protein(Human)(recombinant) (ADI-NSP-540), Lane 2: HeLa (Heat Shocked) Cell Lysate (ADI-LYC-HL101), Lane 3: PC-12 (Heat Shocked) Cell Lysate (ADI-LYC-PC101), Lane 4: 3T3 (Heat Shocked) Cell Lysate (ADI-LYC-3T101), Lane 5: GPC-16 (Heat Shocked) Cell Lysate
Immunohistochemistry analysis of human spleen tissue stained with HSP60, mAb (Mab11-13) at 5µg/ml.
| Regulatory Status |
RUO – Research Use Only |
|---|
Related Products
| Alternative Name | Chaperonin 60, CPN60, HspD1, Heat shock protein 60 |
|---|---|
| Purity | ≥90% (SDS-PAGE; Western blot) |
| Source | Produced in E. coli. |
| Application | ELISA, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Mouse |