HSP60 recombinant protein

HSP60 (low endotoxin) (mouse), (recombinant)

Cat. Num. AAA565883

• Gene Names: Hspd1; 60kDa; CPN60; Hsp60; HSP-60; HSP-65
• Applications: ELISA, Western Blot
• Purity: >=90% (SDS-PAGE; Western blot); Purified by multi-step chromatography
• Synonyms: HSP60; HSP60 (low endotoxin) (mouse); (recombinant); HSP60 recombinant protein

• Host: E Coli
• Purity/Purification: >=90% (SDS-PAGE; Western blot); Purified by multi-step chromatography
• Form/Format: Liquid. In 10mM TRIS, pH7.5, containing 150mM sodium chloride, 1mM EDTA, and 1mM DTT

• Applicable Applications for HSP60 recombinant protein: ELISA (EIA), Western Blot (WB), Activity assay
• Endotoxin: <50EU/mg purified protein (LAL test)
• Preparation and Storage: For long term storage, store at -80 degree C; Shipping: Shipped on Dry Ice

Related Product Information for HSP60 recombinant protein

Mouse Hsp60 belongs to a highly conserved family that includes molecular chaperones from a variety of species such as plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60, and the 65kDa major antigen of mycobacteria. Hsp60 is localized in the mitochondrial matrix of eukaryotes, and in the chloroplast of plants. Hsp60s from divergent species share a number of common characteristics: high abundance; induction with environmental stress such as heat shock; homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg²⁺ and ATP; ATPase activity; and a role in folding and assembly of oligomeric protein structures. These similarities correspond with studies in which the single-ring human mitochondrial homolog Hsp60 and its co-chaperonin Hsp10 were expressed in an E Coli strain engineered to keep the groE operon under strict regulatory control. The findings demonstrate that expression of Hsp60-Hsp10 enabled successful performance of all essential in vivo functions of GroEL and its cochaperonin, GroES. Several studies reveal a possible link between members of the Hsp60 family and a number of autoimmune diseases, atherosclerosis, and chlamydial disease. Overexpression of self Hsp60 is seen in the synovial tissue of rheumatoid arthritic (RA) patients, and can accompany both cellular and humoral reactivity against Hsp60 in RA. Chlamydial heat shock protein Hsp60, a homolog of E Coli GroEL, appears capable of eliciting macrophage activation, and several studies reveal a correlation between Hsp60 responses and the immunopathologic manifestations of human chlamydial disease.

Product Categories/Family for HSP60 recombinant protein

Proteostasis; Protein Synthesis & Folding

NCBI and Uniprot Product Information

• NCBI GI #: 183396771
• NCBI GeneID: 15510
• NCBI Accession #: NP_034607.3
• NCBI GenBank Nucleotide #: NM_010477.4
• UniProt Accession #: P63038; P19226; P19227; P97602; Q3KQP2; Q3UIP0; Q8C2C7; Q8VEF4
• Molecular Weight: 27,015 Da
• NCBI Official Full Name: 60 kDa heat shock protein, mitochondrial
• NCBI Official Synonym Full Names: heat shock protein 1 (chaperonin)
• NCBI Official Symbol: Hspd1
• NCBI Official Synonym Symbols: 60kDa; CPN60; Hsp60; HSP-60; HSP-65
• NCBI Protein Information: 60 kDa heat shock protein, mitochondrial
• UniProt Protein Name: 60 kDa heat shock protein, mitochondrial
• Protein Family: Hydrogenosomal chaperonin
• UniProt Gene Name: Hspd1
• UniProt Synonym Gene Names: Hsp60; CPN60; HSP-60; Hsp60

Uniprot Description

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates 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. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.