Abcam, ab266344, Human DNAJB1 (Hsp40) knockout HEK-293T cell line

Size: 2 x 1000000Cells / vial / 1000000Cells / vial
DNAJB1 KO cell line available to order. KO validated by Western blot. Free of charge wild type control available. Knockout achieved by using CRISPR/Cas9, Homozygous: 29 bp deletion in exon 1. To order both knockout and wild-type control cells: select 2 x 1000000Cells/vial. To order only knockout cells: select 1000000Cells/vial.
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 29 bp deletion in exon 1

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-DNAJB1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Zygosity-Homozygous, 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.
Hsp40 also known as DnaJB1 is a member of the heat shock protein family that acts mechanically as a molecular chaperone. This protein with a mass of approximately 41 kDa assists in protein folding and stabilization preventing aggregation under stress conditions. Hsp40 proteins are widely expressed in various tissues and are important in maintaining cellular homeostasis. In addition to DnaJB1 other aliases include 3b9 and 2a7 which emphasize its variety within the Hsp40 family.
Biological function summary
Hsp40 proteins participate in cell signaling and stress response by modulating the activity of Hsp70 forming a functional complex with it to guide protein folding processes. This process is essential for protein quality control and cellular protection. It interacts with unfolded proteins and delivers them to Hsp70 enhancing its ATPase activity necessary for the proper functioning of these molecular chaperones. The expression of Hsp40 in stress conditions highlights its importance in the protein quality control system.
Pathways
Hsp40 is involved in important cellular mechanisms like the unfolded protein response and protein catabolism pathways. It works closely with Hsp70 playing a pivotal role in managing protein misfolding and aggregation vital for cellular stress response and recovery. In these pathways Hsp40's function ensures the proper folding and degradation of damaged proteins maintaining proteostasis in the cell.
Hsp40 influences the development of neurodegenerative diseases and certain cancers. Mutations or altered expression of Hsp40 can lead to disrupted protein homeostasis contributing to conditions like Alzheimer's disease and tumor progression. In Alzheimer's disease besides interacting with Hsp70 Hsp40 affects the accumulation of amyloid-beta peptides. In cancer contexts it may interact with other chaperone proteins affecting their function and therefore promoting tumor aggressiveness and resistance to stress.