HSPD1 Protein (His tag)

Catalog No. ABIN1686673

Product Details

Target: HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: Escherichia coli (E. coli)

Purification tag / Conjugate: This HSPD1 protein is labelled with His tag.

Application: Western Blotting (WB), SDS-PAGE (SDS), ELISA, Functional Studies (Func), Activity Assay (AcA)

Specificity: ~60 kDa

Characteristics: The protein has ATPase activity at the time of manufacture of 3.6 µM phosphate liberated/hr/μg protein in a 200 µL reaction at 37 °C (pH 7.5) in the presence of 20 µL of 1 mM ATP using a Malachite Green assay.

Purification: Affinity Purified

Purity: >90%

Biological Activity Comment: ATPase active

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

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.

Restrictions: For Research Use only

Handling

Concentration: Lot specific

Buffer: 20 mM Phosphate Buffer, 150 mM NaCl, 10 % glycerol

Storage: -20 °C

References

Kaiser, Steptoe, Thompson, Henderson: "Monocyte cytokine synthesis in response to extracellular cell stress proteins suggests these proteins exhibit network behaviour." in: Cell stress & chaperones, Vol. 19, Issue 1, pp. 135-44, (2013) (PubMed).

Adamus, Bonnah, Brown, David: "Detection of autoantibodies against heat shock proteins and collapsin response mediator proteins in autoimmune retinopathy." in: BMC ophthalmology, Vol. 13, pp. 48, (2013) (PubMed).

Dieudé, Correa, Neville, Pineau, Levine, Subang, Landolt-Marticorena, Su, Kassis, Solymoss, Fortin, Rauch: "Association of autoantibodies to heat-shock protein 60 with arterial vascular events in patients with antiphospholipid antibodies." in: Arthritis and rheumatism, Vol. 63, Issue 8, pp. 2416-24, (2011) (PubMed).

Target Details

Target: HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))

Alternative Name: Hsp60 (HSPD1 Products)

Synonyms: CPN60 Protein, GROEL Protein, HLD4 Protein, HSP-60 Protein, HSP60 Protein, HSP65 Protein, HuCHA60 Protein, SPG13 Protein, chaperonin Protein, cpn60 Protein, groel Protein, hld4 Protein, hsp60 Protein, hsp65 Protein, spg13 Protein, 60kDa Protein, Hsp60 Protein, 12 Protein, BP5 Protein, CG12101 Protein, Cpn60 Protein, Dmel\\CG12101 Protein, Dmhsp60 Protein, G62 Protein, HSP60A Protein, Hsp60A Protein, IEF16 Protein, Mmp-P1 Protein, SSP 7506 Protein, d-hsp60 Protein, hsp60A Protein, l(1)10Ac Protein, l(1)BP5 Protein, l(1)G8 Protein, l(1)HM21 Protein, l(1)L12 Protein, l(1)dp025 Protein, cb863 Protein, fa04a05 Protein, fb22d10 Protein, fi27b05 Protein, id:ibd2197 Protein, sb:cb144 Protein, wu:fa04a05 Protein, wu:fb22d10 Protein, wu:fi04a12 Protein, wu:fi27b05 Protein, MIF4 Protein, MNA2 Protein, mopA Protein, groL Protein, crpA Protein, Hspd1-30p Protein, heat shock protein family D (Hsp60) member 1 Protein, heat shock protein family D (Hsp60) member 1 S homeolog Protein, 60 kDa heat shock protein, mitochondrial Protein, heat shock protein 1 (chaperonin) Protein, Heat shock protein 60A Protein, heat shock 60 protein 1 Protein, chaperone ATPase HSP60 Protein, molecular chaperone GroEL Protein, thermosome subunit Protein, chaperonin GroEL Protein, mitochondrial chaperonin Protein, heat shock protein family D member 1 Protein, HSPD1 Protein, hspd1.S Protein, hspd1 Protein, LOC100414401 Protein, Hspd1 Protein, Hsp60A Protein, HSP60 Protein, groEL Protein, MMP_RS07785 Protein, groEl Protein, LOC100136430 Protein

Background: 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).

Molecular Weight: approx. 60 kDa

Gene ID: 3329

UniProt: P10809

Pathways: Activation of Innate immune Response, Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process, Production of Molecular Mediator of Immune Response, Positive Regulation of Endopeptidase Activity