Recombinant humaan HSP60-eiwit

HSP60 is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60's bacterial homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Recombinant human HSP60 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

60 kDa heat shock protein mitochondrial, 60 kDa heat shock protein, mitochondrial, CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13

E.coli

Human

His-Tag

SDS-PAGE

0.5 mg/mL (determined by Bradford assay)

> 90% by SDS-PAGE

60 kDa (572aa)

HSP60, 60 kDa heat shock protein mitochondrial, 60 kDa heat shock protein, mitochondrial, CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13, ATGP2027-10 µg, ATGP2027-20 µg, ATGP2027-50 µg, ATGP2027-100 µg, ATGP2027-250 µg, ATGP2027-500 µg, ATGP2027-1 mg, ATGP2027-10, ATGP2027-20, ATGP2027-50, ATGP2027-100, ATGP2027-250, ATGP2027-500, ATGP2027-1

Cappello F, Di Stefano A, et al. (2006) . Cancer. 107 (10) :2417-24.

Vilasi S, et al. Human Hsp60 with its mitochondrial import signal occurs in solution as heptamers and tetradecamers remarkably stable over a wide range of concentrations. (PLoS One. 2014) {https://pubmed.ncbi.nlm.nih.gov/24830947/}; ; Ricci C, et al. Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins. (Biophys Chem. 2016) {https://pubmed.ncbi.nlm.nih.gov/26259786/}; ; Ricci C, et al. Investigation on different chemical stability of mitochondrial Hsp60 and its precursor. (Biophys Chem. 2017) {https://pubmed.ncbi.nlm.nih.gov/28774748/}; ; Kaiser F, et al. Association between circulating levels of heat-shock protein 27 and aggressive periodontitis. (Cell Stress Chaperones. 2018) {https://pubmed.ncbi.nlm.nih.gov/29766408/}; ; Marino C, et al. Hsp60 Protects against Amyloid β Oligomer Synaptic Toxicity via Modification of Toxic Oligomer Conformation. (ACS Chem Neurosci. 2019) {https://pubmed.ncbi.nlm.nih.gov/31091411/}; ; Vilasi S, et al. Inhibition of Aβ 1-42 Fibrillation by Chaperonins: Human Hsp60 Is a Stronger Inhibitor than Its Bacterial Homologue GroEL. ACS Chem Neurosci. 2019) {https://pubmed.ncbi.nlm.nih.gov/31298838/}

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 0.1M NaCl, 10% glycerol

Heat Shock Proteins

NP_955472

P10809

Human

AKDVK FGADARALML QGVDLLADAV AVTMGPKGRT VIIEQSWGSP KVTKDGVTVA KSIDLKDKYK NIGAKLVQDV ANNTNEEAGD GTTTATVLAR SIAKEGFEKI SKGANPVEIR RGVMLAVDAV IAELKKQSKP VTTPEEIAQV ATISANGDKE IGNIISDAMK KVGRKGVITV KDGKTLNDEL EIIEGMKFDR GYISPYFINT SKGQKCEFQD AYVLLSEKKI SSIQSIVPAL EIANAHRKPL VIIAEDVDGE ALSTLVLNRL KVGLQVVAVK APGFGDNRKN QLKDMAIATG GAVFGEEGLT LNLEDVQPHD LGKVGEVIVT KDDAMLLKGK GDKAQIEKRI QEIIEQLDVT TSEYEKEKLN ERLAKLSDGV AVLKVGGTSD VEVNEKKDRV TDALNATRAA VEEGIVLGGG CALLRCIPAL DSLTPANEDQ KIGIEIIKRT LKIPAMTIAK NAGVEGSLIV EKIMQSSSEV GYDAMAGDFV NMVEKGIIDP TKVVRTALLD AAGVASLLTT AEVVVTEIPK EEKDPGMGAM GGMGGGMGGG MF