Human Recombinant HSP60 Protein

  • Catalog number
    SPR-104C
  • Price
    Please ask
  • Size
    2x100 µg
  • Stock availability
    In Stock
  • Scientific context
    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 (1-3). 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) 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 (4). 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 (5). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
  • Protein target
    HSP60
  • Protein reactivity
    Human
  • Certificate of analysis
    This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.6µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
  • Protein description
    Active Human Recombinant HSP60 Protein
  • Other name
    60kDa chaperonin Protein, cb863 Protein, CPN60 Protein, GROEL Protein, GroEL Homolog Protein, HLD4 Protein, HSP65 Protein, HSPD1 Protein, HuCHA60 Protein, SPG13 Protein
  • Primary research area
    Cancer, Heat Shock
  • Category
    Protein
  • Brand name
    none
  • Origin
    Recombinant
  • NCBI number
    BC003030
  • Gene number
    3329
  • Protein number
    P10809
  • Verified applications
    WB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA
  • Relevant bio activity
    ATPase active
  • Protein expression model
    E. coli
  • Protein charasterics
    See included datasheet.
  • Peptide sequence
    See included datasheet.
  • Protein purification
    Affinity Purified
  • Purity pourcentage
    >90% High purity
  • Recommended buffer for storage
    20mM Phosphate Buffer, 150mM NaCl, 10% glycerol
  • Protein concentration
    Lot/batch specific. See included datasheet.
  • Protein specificity
    ~60 kDa
  • Protein tag
    His tag
  • Storage recommendations
    -20°C
  • Shipping recommendations
    Blue Ice or 4°C
  • Supplementary useful information
    Please see included datasheet or contact us
  • Protein cell localization
    Mitochondrion Matrix
  • Bibliography
    1. Hartl F.U. (1996) Nature. 381: 571-579. 2. Bukau B. and Horwich A.L. (1998) Cell. 92: 351-366. 3.Hartl F.U. and Hayer-Hartl M. (2002) Science. 295: 1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biol. 9: 2279-2283. 5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh H., et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7.Gupta S. and Knowlton A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris C.C. et al. (2006) Cell Stress Chaperones. 11: 116-128. 9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297.
  • Release date
    1-Sep-2007
  • PubMed number
    23775284, 24066722, 21506099
  • Tested applications
    Functional Assay, Western Blot Control, ELISA
  • Tested species reactivity
    Human
  • Representative figure legend
    SDS-PAGE of 60kDa Hsp60 protein (SPR-104). SDS-Page of human HSP60 Protein (SPR-104)
  • Warnings
    Non-hazardous materials
  • Protein origin
    Canada
  • Total weight kg
    1.4
  • Net weight g
    0.2
  • Properties
    Human proteins, cDNA and human recombinants are used in human reactive ELISA kits and to produce anti-human mono and polyclonal antibodies. Modern humans (Homo sapiens, primarily ssp. Homo sapiens sapiens). Depending on the epitopes used human ELISA kits can be cross reactive to many other species. Mainly analyzed are human serum, plasma, urine, saliva, human cell culture supernatants and biological samples.
  • Source
    Recombinants or rec. proteins
  • Group
    recombinants
  • Gene target
    HSP60   Protein  
  • Gene symbol
    HSPD1
  • Short name
    Recombinant HSP60 Protein
  • Technique
    Recombinant, E. coli recombinant proteins are genetic recombinations in Escherichia coli, supplied as white sterile powder lyopillized. StressMark proteins advises they will be reconstituted in a buffer soluion or culture medium for cell culture.
  • Species
    Human, Humans
  • Alternative name
    H. sapiens Rec. HSP60 Protein
  • Alternative technique
    rec
Gene info
  • Identity
  • Gene
  • Long gene name
    heat shock protein family D (Hsp60) member 1
  • Synonyms gene
  • Synonyms gene name
    • heat shock 60kD protein 1 (chaperonin)
    • spastic paraplegia 13 (autosomal dominant)
    • heat shock 60kDa protein 1 (chaperonin)
  • Synonyms
  • GenBank acession
  • Locus
  • Discovery year
    1991-07-19
  • Entrez gene record
  • Pubmed identfication
  • RefSeq identity
  • Classification
    • Chaperonins
  • VEGA ID
MeSH Data
  • Name
  • Concept
    Scope note: The initial culturing of cells derived directly from fresh TISSUES.
  • Tree numbers
    • E01.370.225.500.223.500
    • E05.200.500.265.500
    • E05.242.223.500
    • E05.481.500.249.500
  • Qualifiers
    ethics, trends, veterinary, history, classification, economics, instrumentation, methods, standards, statistics & numerical data
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