HSC70 Protein

Product Description

HSC70 Protein is available at Gentaur for Next week delivery.

Description:  Active Human Recombinant HSC70 Protein

Alternative Name(s):  Constitutive heat shock protein 70 Protein, HSC54 Protein, HSC71 Protein, HSC73 Protein, HSP71 Protein, HSP74 Protein, HSPA10 Protein, HSPA8 Protein, LAP1 Protein, NIP71 Protein

Research Area(s):  Cancer | Heat Shock

Nature:  Recombinant

Accession Number: AF352832

Gene ID:  3312

Swiss-Prot:  P11142 

Applications Species:  WB | SDS-PAGE | ATPase Activity Assay | Functional Assay | ELISA 

Biological Activity:  ATPase active

Expression System: E. coli

Protein Length: 

Amino Acid Sequence:

Purification:  Affinity Purified

Storage Buffer:  20mM Tris/HCl pH7.5, 1mM EDTA

Concentration:  Lot/batch specific. See included datasheet.

Shipping Temperature: Blue Ice or 4ºC

Other relevant information:

Certificate of Analysis: This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.2µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay. 

Cellular Localization:  Cytoplasm | Melanosome

Scientific Background:  HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).

References: 1. Brown C. L., et al. (1993) J.Cell Biol. 120(5): 1101-1112 2. Boorstein W. R., Ziegelhoffer T. & Craig E.A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell. 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 6. Brown C. L., et al. (1996) J. Biol. Chem. 271(2): 833-840.

Field of Use:  Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

PubMed ID:  28110910|28026090|26244546|25939977|25979775|23291500|20084527|19209902

Published Application:  Functional Assay|Western Blot|Functional Assay|Intrinsic fluorescence spectroscopy|Western Blot Control|Functional Assay|Functional Assay|Western Blot Control

Published Species Reactivity:  Rat|Human|Human|||Mouse|Photinus pyralis|