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 deletion in exon 1 and 2 bp deletion in exon 1,
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 and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-HSPB8, 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.
Hsp22 also known as HSPB8 is a small heat shock protein with a molecular weight of approximately 22 kDa. Expressed in various tissues including heart skeletal muscle and brain Hsp22 functions as a chaperone in cellular conditions. It prevents aggregation and aids in the refolding of misfolded proteins matching its role among the heat shock family proteins known for stress response.
Biological function summary
Hsp22 plays a critical role in maintaining protein homeostasis as part of a larger chaperone complex. It forms hetero-oligomers with other small heat shock proteins like HSPB1 and HSPB6 enhancing its protein-protective functions. These interactions allow Hsp22 to stabilize cytoskeletal elements and partake in autophagic pathways highlighting its importance during cellular stress conditions.
Pathways
Hsp22 integrates into cellular processes of autophagy and proteostasis. It participates in the chaperone-assisted selective autophagy (CASA) pathway. Here it associates with the cochaperone BAG3 facilitating the degradation of damaged proteins. Hsp22 also plays a role in the heat shock response pathway cooperating with other heat shock proteins like HSP70 to protect cells from damage induced by increased temperatures.
Hsp22 has associations with diseases like myopathy and neurodegeneration. In myopathies mutations in Hsp22 can disrupt normal muscular functions leading to muscle weakness and degeneration. In neurodegenerative conditions such as amyotrophic lateral sclerosis (ALS) abnormalities in the function or expression of Hsp22 together with its interaction with proteins such as HSPB1 can contribute to the disease's pathogenic mechanisms highlighting its clinical relevance.
