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Stock availability
In Stock
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Scientific context
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 within 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 of 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 diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
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Protein target
HSP60
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Protein reactivity
Human
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Certificate of analysis
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.6µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
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Protein description
Active Human Recombinant HSP60 Protein
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Other name
60kDa chaperonin Protein, cb863 Protein, CPN60 Protein, GROEL Protein, GroEL Homolog Protein, HLD4 Protein, HSP65 Protein, HSPD1 Protein, HuCHA60 Protein, SPG13 Protein
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Primary research area
Cancer, Heat Shock
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Category
Protein
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Brand name
none
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Origin
Recombinant
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NCBI number
BC003030
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Gene number
3329
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Protein number
P10809
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Verified applications
WB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA
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Relevant bio activity
ATPase active
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Protein expression model
E. coli
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Protein charasterics
See included datasheet.
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Peptide sequence
See included datasheet.
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Protein purification
Affinity Purified
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Purity pourcentage
>90% High purity
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Recommended buffer for storage
20mM Phosphate Buffer, 150mM NaCl, 10% glycerol
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Protein concentration
Lot/batch specific. See included datasheet.
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Protein specificity
~60 kDa
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Protein tag
His tag
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Storage recommendations
-20°C
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Shipping recommendations
Blue Ice or 4°C
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Supplementary useful information
Please see included datasheet or contact us
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Protein cell localization
Mitochondrion Matrix
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Bibliography
1. Hartl F.U. (1996) Nature. 381: 571-579. 2. Bukau B. and Horwich A.L. (1998) Cell. 92: 351-366. 3.Hartl F.U. and Hayer-Hartl M. (2002) Science. 295: 1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biol. 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.
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Release date
1-Sep-2007
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PubMed number
23775284, 24066722, 21506099
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Tested applications
Functional Assay, Western Blot Control, ELISA
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Tested species reactivity
Human
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Representative figure legend
SDS-PAGE of 60kDa Hsp60 protein (SPR-104). SDS-Page of human HSP60 Protein (SPR-104)
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Warnings
Non-hazardous materials
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Protein origin
Canada
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Total weight kg
1.4
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Net weight g
0.2
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Properties
Human proteins, cDNA and human recombinants are used in human reactive ELISA kits and to produce anti-human mono and polyclonal antibodies. Modern humans (Homo sapiens, primarily ssp. Homo sapiens sapiens). Depending on the epitopes used human ELISA kits can be cross reactive to many other species. Mainly analyzed are human serum, plasma, urine, saliva, human cell culture supernatants and biological samples.
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Source
Recombinants or rec. proteins
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Group
recombinants