Hsp60 Antibody
Référence OASE00017
Conditionnement : 50ug
Marque : Aviva Systems Biology
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| Datasheets/Manuals | Printable datasheet for OASE00017 |
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| Predicted Species Reactivity | Human, Mouse, Rat, Bovine, Dog, Chicken, Guinea Pig, Hamster, Monkey, Pig, Rabbit, Plant, Bacteria, Trichinella spiralis, Yeast, Insect, Fish |
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| Product Format | Liquid PBS with 50% glycerol and 0.09% sodium azide |
| Clonality | Monoclonal |
| Clone | LK2 |
| Isotype | IgG1 |
| Host | Mouse |
| Conjugation | Unconjugated |
| Application | FC, IHC-Fr, IP |
| :: | Certificate of Analysis: 0.25ug/mL was sufficient for detection of Hsp60 in10ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using goat anti-mouse IgG as the secondary antibody. |
| Reconstitution and Storage | Store at -20°C for one year. Avoid freeze/thaw cycles. |
| Immunogen | Recombinant human HSP60 |
| Purification | Protein G Purified |
| Concentration | 1 mg/ml |
| Specificity | Detects ~60kDa. |
| Dilution | WB (1:4000), IHC (1:100); optimal dilutions for assays should be determined by the user. |
| Description | 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). |
| Reference | 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 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. 10. Gao, Y.L., et al (1995) J. of Immunology 154: 3548-3556. 11. Neuer, A., et al (1997) European Society for Human Reproduction and Embryology 12(5):925-929. 12. Bason, C., et al (2003) Lancet 362(9400): 1971-1977. |
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| Gene Symbol | HSP60 |
| Gene Full Name | heat shock 60kDa protein 1 (chaperonin) |
| Alias Symbols | CPN60, GROEL, HLD4, HSP 60, HSP65, HSPD1, HuCHA60, SPG 13 |
| NCBI Gene Id | 3329 |
| Description of Target | 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). |
| Uniprot ID | P10809 |
| Protein Accession # | NP_002147.2 |
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What is the species homology for "Hsp60 Antibody (OASE00017)"?
The tested species reactivity for this item is "". This antibody is predicted to have homology to "Human, Mouse, Rat, Bovine, Dog, Chicken, Guinea Pig, Hamster, Monkey, Pig, Rabbit, Plant, Bacteria, Trichinella spiralis, Yeast, Insect, Fish ".
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How long will it take to receive "Hsp60 Antibody (OASE00017)"?
This item is available "Domestic: within 1-2 weeks delivery | International: 1-2 weeks".
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What buffer format is "Hsp60 Antibody (OASE00017)" provided in?
This item is provided in "Liquid PBS with 50% glycerol and 0.09% sodium azide".
Additional format options may be available. For more information please contact info@avivasysbio.com. -
What are other names for "Hsp60 Antibody (OASE00017)"?
This target may also be called "CPN60, GROEL, HLD4, HSP 60, HSP65, HSPD1, HuCHA60, SPG 13" in publications.
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What is the shipping cost for "Hsp60 Antibody (OASE00017)"?
The shipping cost for this item is within the US. Please contact us for specific shipping for international orders.
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What is the guarantee for "Hsp60 Antibody (OASE00017)"?
All Aviva products have been through rigorous validations and carry 100% satisfaction guarantee.
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Can I get bulk pricing for "Hsp60 Antibody (OASE00017)"?
You can get bulk pricing for this item by going here.
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What is the molecular weight of the protein?
The molecular weight reported by Uniprot for this item is "".
Please note observed molecular weights in western blot applications may differ depending on a variety of protein characteristics. -
What protocols are available for "Hsp60 Antibody (OASE00017)"?
We may have detailed protocol data avaialble for this item. To learn more, please view the "Protocols & Data" tab on the product page.
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What are positive controls for "HSP60"?
We have listed RNA Seq and gene expression data in the "Target Info" tab. You may be able to find adequate positive controls there.
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What are negative controls for "HSP60"?
We have listed RNA Seq and gene expression data in the "Target Info" tab. You may be able to find adequate positive controls there.
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What other proteins interact with "HSP60"?
This protein has been reported to interact with "Protein Interactions". Please view the "Related Categories" tab on the product page for more information.
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What biological processes are associated with "HSP60"?
This protein has been associated with "Biological Processes". Please view the "Related Categories" tab on the product page for more information.
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What cellular components are associated with "HSP60"?
This protein has been associated with "Cellular Components". Please view the "Related Categories" tab on the product page for more information.
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What protein functions are associated with "HSP60"?
This protein has been associated with "Protein Functions". Please view the "Related Categories" tab on the product page for more information.