Heat Shock Protein 60 Recombinant Protein | HSP60 recombinant protein

Heat Shock Protein 60, Recombinant, Human (HSP60, GroEL, Chaperonin 60, cpn60) (Low Endotoxin)

Cat. Num. AAA635700

• Gene Names: HSP60; heat shock protein 60; HEAT SHOCK PROTEIN 60-3B; HSP60; HSP60-3B
• Applications: Western Blot
• Purity: >90% (SDS-PAGE; Western Blot)
• Synonyms: Heat Shock Protein 60; Recombinant; Human (HSP60; GroEL; Chaperonin 60; cpn60) (Low Endotoxin); HSP60 recombinant protein

• Host: E. coli
• Purity/Purification: >90% (SDS-PAGE; Western Blot)
• Form/Format: Supplied as a liquid in 1X Dulbecco's PBS.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for HSP60 recombinant protein: Western Blot (WB)
• Application Notes: Recommended Dilutions: Western Blot (Colometric): 100ng; ; Optimal dilutions to be determined by the researcher. Other applications not tested.
• Grade: Purified
• Endotoxin: < 50 EU/mg (LAL)
• Functional Activity Assay: This protein has tested positive for ATPase activity.
• Preparation and Storage: Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Related Product Information for HSP60 recombinant protein

Human 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 65kD, a major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix and the plant 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 Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (1). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, Hsp60 with its co-chaperonin, Hsp10 were expressed in an 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 (2). 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 (3). 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, artherosclerosis and chlamydial disease.

Product Categories/Family for HSP60 recombinant protein

Molecular Biology; MB-Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 15229559
• NCBI GeneID: 821983
• NCBI Accession #: NP_189041.1
• NCBI GenBank Nucleotide #: NM_113304.4
• UniProt Accession #: P29197; Q9LIQ8
• Molecular Weight: ~60kD
• NCBI Official Full Name: heat shock protein 60
• NCBI Official Symbol: HSP60
• NCBI Official Synonym Symbols: heat shock protein 60; HEAT SHOCK PROTEIN 60-3B; HSP60; HSP60-3B
• NCBI Protein Information: heat shock protein 60
• UniProt Protein Name: Chaperonin CPN60, mitochondrial
• Protein Family: Heat shock protein
• UniProt Gene Name: CPN60
• UniProt Entry Name: CH60A_ARATH

NCBI Description

mitochondrial chaperonin HSP. assist in rapid assembly of the oligomeric protein structures in the mitochondria.

Uniprot Description

Function: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.

Subcellular location: Mitochondrion.

Induction: By heat shock.

Sequence similarities: Belongs to the chaperonin (HSP60) family.