Product Description
HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress. Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner. HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23. The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments. When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome. The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules. They also play a role in vesicle formation and protein trafficking.
Biovision | 4859 | Heat Shock Protein 70 human recombinant DataSheet
Biomolecule/Target: N/A
Synonyms: Human Heat Shock Protein 70, Heat Shock Protein 70
Alternates names: FS, activin-binding protein, FSH-suppressing protein (FSP)
Taglines: A chaperone protein that assists protein folding
NCBI Gene ID #: 14313
NCBI Gene Symbol: FST
Gene Source: Human
Accession #: P47931
Recombinant: Yes
Source: E. coli
Purity by SDS-PAGEs: 90%
Assay: SDS-PAGE
Purity: 98%
Assay #2: HPLC
Endotoxin Level: <0.1 ng/g
Activity (Specifications/test method): N/A
Biological activity: The activity is determined by the dose-dependent neutralization of 7.5 ng/mL human Activin A. Complete neutralization is typically reached at less than 0.3 ug/mL.
Results: 0.3 ug/mL
Binding Capacity: N/A
Unit Definition: N/A
Molecular Weight: 31.6 kDa
Concentration: N/A
Appearance: Lyophilized protein
Physical form description: Lyophilized from 41 mM Tris, pH 8 containing 81 mM NaCl.
Reconstitution Instructions: Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with sterile water at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions.
Amino acid sequence: MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS