Abcam, ab78431, Recombinant human Hsc70 protein

Size: 50µg / 100µg
Recombinant human Hsc70 protein is a Human Full Length protein, in the 1 to 646 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS, ELISA.
Key facts
Purity:>90%,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:SDS-PAGE, ELISA, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:ATPase active.,
Accession:P11142,
Animal free:No,
Carrier free:Yes,
Species:Human,
Storage buffer:pH: 8Constituents: 1.753% Sodium chloride, 0.788% Tris HCl

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Stable for 12 months at -20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The heat shock cognate 70 (Hsc70) protein also known as HSPA8 plays an important role in chaperone-mediated cellular processes. It exhibits a molecular weight of approximately 70 kDa. Hsc70 is abundantly expressed in various tissues and organs including the brain muscle and liver. As a member of the heat shock protein family Hsc70 maintains protein homeostasis by preventing protein aggregation and assisting in protein folding.
Biological function summary
Hsc70 participates in several processes beyond protein folding. This includes its involvement in the transport of proteins across cellular membranes and the degradation of misfolded proteins. Hsc70 often works in conjunction with co-chaperones and forms part of large protein complexes such as the chaperone machinery involved in clathrin-mediated endocytosis. It also plays a part in cellular stress responses supporting cell survival under various stress conditions.
Pathways
Hsc70 integrates into fundamental cellular pathways such as the ubiquitin-proteasome system and the ER-associated degradation pathway. These pathways are important for protein quality control where Hsc70 collaborates with other heat shock proteins like Hsp40 to facilitate the correct folding and clearance of proteins. In the context of autophagy Hsc70 mediates the recognition and trafficking of specific substrates to lysosomes for degradation demonstrating its importance in maintaining cellular health through these pathways.
Hsc70 shows a strong connection to neurodegenerative diseases and cancer. Misregulation of Hsc70 activity can result in protein aggregation seen in disorders such as Parkinson's disease. This situation often links Hsc70 to proteins like alpha-synuclein which accumulate abnormally in these diseases. In cancer altered expression of Hsc70 can promote tumor development by hyper-accommodating the stress conditions within the tumor microenvironment. Hsc70's interplay with proteins such as p53 highlights its role in the pathology of tumorigenesis.