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Anti-HSPD1 Antibody N/A
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Also for HSPD1 (NM_002156)
|Human Hsp60 produced through recombinant DNA methods in E.coli|
|Human, Mouse, Rat, Bovine, Canine, Chicken, Rabbit
|PBS with 50% glycerol and 0.09% sodium azide|
|Protein A Purified
|Recognizes a ~60kDa protein, corresponding to the molecular mass of hsp60 on SDS-PAGE blots.
|Homo sapiens heat shock 60kDa protein 1 (chaperonin) (HSPD1), transcript variant 1|
|CPN60; GROEL; HLD4; HSP-60; HSP60; HSP65; HuCHA60; SPG13|
Entrez Gene 3329 Human
Entrez Gene 15510 Mouse
Entrez Gene 63868 Rat
|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 . 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) inductionwith 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 . 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 . Hsp60 has however been linked to a number of autoimmune diseases, as well as Alzheimers, coronary artery diseases, MS, and diabetes .|
|Stem cell - PluripotencyDruggable Genome RNA degradationType I diabetes mellitus|
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Western blot analysis of Hsp60 using a 1:1000 dilution of the antibody