HSP60 Antibody [Alexa Fluor® 594]

Alexa Fluor (R) products are provided under an intellectual property license from Life Technologies Corporation. The purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: (i) in manufacturing; (ii) to provide a service, information, or data in return for payment; (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5791 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@lifetech.com. This conjugate is made on demand. Actual recovery may vary from the stated volume of this product. The volume will be greater than or equal to the unit size stated on the datasheet.

Hsp60 is a member of a highly conserved family which includes molecular chaperones from several species such as plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60 and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria have a common ancestry (>1 billion years) and this fact together with the high degree of homology between the divergent Hsp60s would indicate that these proteins carry out a primitive but important function which is similar to all of these 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 magnesium ions and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures. 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. Consistent with their functions as chaperones, Hsp60 and Hsp10 have been suggested to act as docking molecules with a passive role in the maturation of caspase processing. Data demonstrates that 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 recent studies indicate that members of the Hsp60 family are linked to a number of autoimmune diseases, arthrosclerosis and chlamydial disease.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Array NBP1-77397AF594

• HSP60 Antibodies
• HSP60 ELISA Kits
• HSP60 Lysates
• HSP60 Proteins
• HSP60 ELISA