Description
Key facts
Cell type:A549,
Species or organism:Human,
Tissue:Lung,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon6.,
Disease:Carcinoma
Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
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-TGM2, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Transglutaminase 2 also known as TG2 or tissue transglutaminase is an enzyme with a mass of approximately 74 kDa. It catalyzes the formation of covalent bonds by crosslinking glutamine residues and lysine residues in proteins. This enzyme is widely expressed in various tissues including the liver heart and lungs. It can act as a GTPase a kinase and a protein disulfide isomerase highlighting its multifunctional nature. Additionally transglutaminase 2 associates with cell membranes cytoskeleton and extracellular matrix indicating its versatile involvement in cellular processes.
Biological function summary
Transglutaminase 2 plays roles in cell adhesion wound healing and the immune response. It mediates extracellular matrix stabilization through crosslinking structural proteins which is critical for tissue repair. The enzyme does not typically form a stable part of a large complex but interacts with fibronectin as a binding partner highlighting its role in cellular adhesion and migration. The enzymatic activity of transglutaminase 2 helps maintain tissue integrity by modifying extracellular and intracellular proteins.
Pathways
Transglutaminase 2 contributes significantly to the integrin-mediated signaling pathway and the apoptosis pathway. It assists in the modulation of cell-matrix interactions by crosslinking matrix proteins which is important for integrin signaling. During apoptosis transglutaminase 2 promotes cellular processes that lead to cell death via its involvement in nuclear condensation and DNA fragmentation. In these pathways proteins such as fibronectin and integrins interact with transglutaminase 2 facilitating its regulatory functions.
Transglutaminase 2 is associated with celiac disease and neurodegenerative disorders like Huntington's disease. Its autoantigenic properties make it a target in celiac disease where antibodies against transglutaminase 2 play a role in the pathology by affecting intestinal tissue. In Huntington's disease transglutaminase 2 contributes to the formation of protein aggregates which are toxic to neurons. This enzyme's interactions with proteins such as gliadin in celiac disease and huntingtin in Huntington's disease are central to its pathogenic mechanism.
