Hsp70
N-Terminal c-Myc and 6His-tagged, recombinant, human Hsp70, full length, expressed by baculovirus in Sf21 insect cells.
Biological information
Background
Hsp70 (heat shock protein 70) is a chaperone protein that plays a critical role in maintaining protein homeostasis within cells. While Hsp70 itself is not subject to ubiquitination, it can interact with other proteins that are ubiquitinated, and play a role in their degradation and clearance.
Hsp70 interacts with several co-chaperones, including CHIP (C-terminus of Hsc70-interacting protein), which is a ubiquitin ligase that catalyzes the transfer of ubiquitin molecules to target proteins. Hsp70 can promote the ubiquitination and degradation of misfolded or damaged proteins by recruiting them to CHIP, which then ubiquitinates them and targets them for proteasomal degradation.
In addition to its role in promoting protein degradation, Hsp70 can also prevent protein aggregation and promote protein folding and stability.
Target class
Ubiquitin
Family
Substrate
Accession number
GenBank BC002453
Target Name
Hsp70
Target Alias
APG-2, HEL-S-5a, HS24/P52, HSPH2, RY, hsp70, hsp70RY
Origin
Human
Theori. MW
75 kDa
Affinity tag
N-terminal c-Myc, 6His-tag
Product specifications
Expression system
expressed in insect cells
Purity
78%
Purification method
Immobilized metal affinity chromatography
Sample Buffer
1.50 mg/ml of enzyme in 50 mM Tris/HCl pH 7.5, 150 mM NaCl, 0.1 mM EGTA, 0.03% Brij-35, 270 mM sucrose, 1 mM benzamidine, 0.2 mM PMSF, 0.1% 2-mercaptoethanol. Frozen solution.
Specified activity
Refer to CoA
Application
For Research Only
Storage conditions
1 year at -70°C
Usage disclaimer
For Research Only
Chemical data
Background
Hsp70 (heat shock protein 70) is a chaperone protein that plays a critical role in maintaining protein homeostasis within cells. While Hsp70 itself is not subject to ubiquitination, it can interact with other proteins that are ubiquitinated, and play a role in their degradation and clearance.
Hsp70 interacts with several co-chaperones, including CHIP (C-terminus of Hsc70-interacting protein), which is a ubiquitin ligase that catalyzes the transfer of ubiquitin molecules to target proteins. Hsp70 can promote the ubiquitination and degradation of misfolded or damaged proteins by recruiting them to CHIP, which then ubiquitinates them and targets them for proteasomal degradation.
In addition to its role in promoting protein degradation, Hsp70 can also prevent protein aggregation and promote protein folding and stability.
Compound name
Ubiquitin
Catalog number
23-052
Molecular formula
CAS
MW
Ka
Percent composition
Product specifications
Physical state
Purity (HPLC 214nm)
Retention time (RP18 HPLC)
CMC
Exact mass
Stability
For Research Only
Solubility structure
Datasheets
23-052
Datasheet