Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon 2 and Insertion of the selection cassette in exon 2,
Disease:Adenocarcinoma
Product details:
We will provide viable cells that proliferate on revival.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-HSPA8, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°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.
