Hu, Mu, Rt, Ha, Pm, Bv, ChApplications:
WB, Simple Western, Flow, ICC/IF, IHC, IHC-PHost:
Species: Hu, Mu, Rt, Ha, Pm, Bv
Applications: WB, Simple Western, ICC/IF, IHC, IHC-P
Host: Rabbit Polyclonal
Hu, Mu, Rt, Po, Bv, Ca, Ch, Dr, Ha, Pm, Rb, Sh, XpApplications:
WB, Simple Western, Flow, ICC/IF, IHC-Fr, IHC-P, IPHost:
Applications: WB, IP
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.
|Product By Gene ID
- Heat shock protein 60
- P60 lymphocyte protein
- short heat shock protein 60 Hsp60s1
- heat shock protein 65
- 60 kDa chaperonin
- Mitochondrial matrix protein P1,60 kDa heat shock protein, mitochondrial
- spastic paraplegia 13 (autosomal dominant)
- Chaperonin 60
- heat shock 60kD protein 1 (chaperonin)
- heat shock 60kDa protein 1 (chaperonin)
Bioinformatics Tool for HSP60
Discover related pathways, diseases and genes to HSP60. Need help? Read the Bioinformatics Tool Guide
for instructions on using this tool.
Related HSP60 Blog Posts
Check out the latest blog posts on HSP60.
Read more HSP60 related blogs.
|TLR4 - A Guardian of Innate Immunity
Toll-like receptor 4 (TLR4) belongs to the family of Toll-like receptors (TLR), and plays a main role in pathogen recognition and innate immunity system activation. The TLR family members are highly conserved proteins that all contain a high degree of... Read more.
|Customer Experience using HSP60 Antibody
I began using the HSP60 antibody (NB110-57063) in June of 2010 and it worked well. I do not like to buy antibodies that have not been tested in the species for which I will use them, so I picked this antibody because it had already been tested in rat... Read more.
|Heat Shock Proteins: An Overview
Heat Shock Proteins (HSPs) are a ubiquitous group of molecular chaperone proteins that have evolved unique mechanisms, within their host cells, to facilitate survival in hostile environments such as heat, oxidative (hypoxia), pH and cold. Under permis... Read more.
|The Heat is On: Heat Shock Proteins and the Link to Cancer
Novus Biologicals offers an extensive antibody catalog targeting heat shock proteins (HSPs). A large protein group covering a number of families, the HSPs are functionally related by their dramatic upregulation in response to stress. Stress triggers m... Read more.