Heat Shock Protein 60, P. falciparum (HSP60, HSP-60, 60kD Heat Shock Protein Mitochondrial, 60kD Chaperonin, Chaperonin 60, Cpn60, GroEL, HuCHA60, HLD4, HSP65, HSPD1, Mitochondrial Matrix Protein P1, P60 Lymphocyte Protein, SPG13)

In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. Hsp60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian Hsp60 (1-3). Whereas mammalian Hsp60 is localized \nwithin the mitochondria, plant Hsp60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that Hsp60 is present in so many different species. The common characteristics of the Hsp60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures \nof either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, Hsp60 with its co-chaperonin, Hsp10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of Hsp60 and Hsp10 is their protective functions against infection and cellular stress. Hsp60 has however been linked to a number of autoimmune \ndiseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9). \n\nApplications:\nSuitable for use in Immunofluorescence and Western Blot. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot:1:2000\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

H1830-70M

Size

25ug

Applications

IF, WB

Hosts

Rabbit

Form

Supplied as a liquid in PBS, pH7.4, 0.09% sodium azide and 50% glycerol.

P Type

Pab

Purity

Purified by Protein A affinity chromatography.

Isotype

IgG

References

1. Hartl F.U. (1996) Nature 381:571-579. 2. Bukau B., and Horwich A.L. (1998) Cell 92:351-366. \n3. Hartl F.U and Hayer-Hartl M. (2002) Science 295:1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biology 9:2279-2283. 5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7:64-71. 6. Itoh H., et al. (2002) Eur. J. Biochem. 269:5931-5938. 7. Gupta S. and Knowlton A.A. J. Cell Mol Med. 9:51-58. 8. Deocaris C.C., et al. (2006) Cell Stress Chaperones 11:116-128. 9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab 292:E292-E297.

Additional Info

Recognizes P. falciparum hsp60. Crossreactivity: E.coli Hsp60, GroEl.