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HSP60 (low endotoxin) (human), (recombinant)

 
ADI-ESP-540-D 50 µg 385.00 USD
 
ADI-ESP-540-F 200 µg 834.00 USD
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Product Specification

Alternative Name:Chaperonin 60, CPN60, HspD1, Heat shock protein 60
 
Recommended Dilutions/Conditions:Western Blot (100ng, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
MW:~60kDa
 
Source:Produced in E. coli.
 
UniProt ID:P10809
 
Formulation:Liquid. In Dulbecco’s PBS.
 
Purity:≥90% (SDS-PAGE; Western blot)
 
Purity Detail:Purified by multi-step chromatography.
 
Endotoxin Content:<50EU/mg purified protein (LAL test)
 
Applications:WB
Activity assay, in vitro Assay
 
Application Notes:ATPase activity assay (positive). Western blot control.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background:The human Hsp60 is a member of a highly conserved family which includes molecular chaperones from several species including plant Hsp60 (known as Rubisco binding protein), and bacterial GroEL, a major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix while plant Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria have a common ancestry (>1 billion years). This fact combined with the high degree of homology between the divergent Hsp60s would indicate that these proteins carry out a primitive but important function which is conserved in divergent species. The common characteristics of the Hsp60s include i) high abundance, ii) induction upon environmental stress such as heat shock, iii) homo -oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures. These similarities are supported by studies where the single-ring human mitochondrial homolog, Hsp60 with its cochaperonin, Hsp10 were expressed in an E. coli strain, engineered so that the GroE operon is under strict regulatory control. This study has demonstrated that expressed Hsp60- Hsp10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES. Consistent with their function as chaperones, Hsp60 and Hsp10 have been suggested to act as docking molecules with a passive role in the maturation of caspase processing. Recombinant Hsp60 and Hsp10 have been shown to accelerate the activation of procaspase-3 by cytochrome c and dATP in an ATP-dependent manner. Hsps are intracellular proteins which are thought to serve protective functions against infection and cellular stress, however several studies indicate that members of the Hsp60 family are linked to a number of autoimmune diseases, artherosclerosis and chlamydial disease.
 
ADI-ESP-540 SDS-PAGE
SDS-PAGE Analysis: Lane 1: MW marker, Lane 2: 0.5ug, Lane 3: 1.0ug, Lane 4: 2.0ug, Lane 5: 5.0ug of purified HSP60 (low endotoxin) (human), (recombinant).
ADI-ESP-540 WB
Western Blot analysis: Lane 1: MW Marker, Lane 2: 100ng of HSP60 (low endotoxin) (human), (recombinant) (Prod. No. ADI-ESP-540), Lane 3: 50ng E. coli GroEL (Prod. No. ADI-SPP-610); Left: Probed with HSP60 mAb (Prod. No. ADI-SPA-806); Right: Probed with GroEL mAb (Prod. No. ADI-SPS-870).
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ADI-ESP-540 SDS-PAGE ADI-ESP-540 WB

Product Literature References

Intrathecal heat shock protein 60 mediates neurodegeneration and demyelination in the CNS through a TLR4- and MyD88-dependent pathway: K. Rosenberger, et al.; Molec. Neurodegen. 10, 5 (2015), Application(s): Injection, Abstract; Full Text
Inhibition of experimental Sjogren's syndrome through immunization with Hsp60 and its peptide amino acids 437-460: N. Delaleu, et al. ; Arthritis Rheum. 58, 2318 (2008), Application(s): Other using mouse Other, Abstract;
Different efficiency of heat shock proteins (HSP) to activate human monocytes and dendritic cells: superiority of HSP60: M. Heike, et al. ; J. Immunol. 169, 6141 (2002), Application(s): In Vitro Assay using human samples, Abstract;

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