Human Recombinant HSP60 Protein
#
-
Catalog numberSPR-104B
-
Price:
-
Size100 µg
-
-
Stock availabilityIn Stock
-
Scientific contextIn 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 targetHSP60
-
Protein reactivityHuman
-
Certificate of analysisThis 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 descriptionActive Human Recombinant HSP60 Protein
-
Other name60kDa chaperonin Protein, cb863 Protein, CPN60 Protein, GROEL Protein, GroEL Homolog Protein, HLD4 Protein, HSP65 Protein, HSPD1 Protein, HuCHA60 Protein, SPG13 Protein
-
Primary research areaCancer, Heat Shock
-
CategoryProtein
-
Brand namenone
-
OriginRecombinant
-
NCBI numberBC003030
-
Gene number3329
-
Protein numberP10809
-
Verified applicationsWB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA
-
Relevant bio activityATPase active
-
Protein expression modelE. coli
-
Protein charastericsSee included datasheet.
-
Peptide sequenceSee included datasheet.
-
Protein purificationAffinity Purified
-
Purity pourcentage>90% High purity
-
Recommended buffer for storage20mM Phosphate Buffer, 150mM NaCl, 10% glycerol
-
Protein concentrationLot/batch specific. See included datasheet.
-
Protein specificity~60 kDa
-
Protein tagHis tag
-
Storage recommendations-20°C
-
Shipping recommendationsBlue Ice or 4°C
-
Supplementary useful informationPlease see included datasheet or contact us
-
Protein cell localizationMitochondrion Matrix
-
Bibliography1. 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 date1-Sep-2007
-
PubMed number23775284, 24066722, 21506099
-
Tested applicationsFunctional Assay, Western Blot Control, ELISA
-
Tested species reactivityHuman
-
Representative figure legendSDS-PAGE of 60kDa Hsp60 protein (SPR-104). SDS-Page of human HSP60 Protein (SPR-104)
-
WarningsNon-hazardous materials
-
Protein originCanada
-
Total weight kg1.4
-
Net weight g0.1
-
PropertiesHuman 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.
-
SourceRecombinants or rec. proteins
-
Grouprecombinants
-
Gene target
-
Gene symbolHSPD1
-
Short nameRecombinant HSP60 Protein
-
TechniqueRecombinant, 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.
-
SpeciesHuman, Humans
-
Alternative nameH. sapiens Rec. HSP60 Protein
-
Alternative techniquerec
-
Gene info
-
Identity
-
Gene
-
Long gene nameheat 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 year1991-07-19
-
Entrez gene record
-
Pubmed identfication
-
RefSeq identity
-
Classification
- Chaperonins
-
VEGA ID
MeSH Data
-
Name
-
ConceptScope 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
-
Qualifiersethics, trends, veterinary, history, classification, economics, instrumentation, methods, standards, statistics & numerical data