Description
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 16 bp deletion in exon 2.
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 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-UFC1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Zygosity-Homozygous, 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.
UFC1 also known as ubiquitin-fold modifier-conjugating enzyme 1 or UFM1-conjugating enzyme 1 functions mechanically by facilitating the conjugation of ubiquitin-fold modifier 1 (UFM1) to target substrates. It exhibits a molecular mass of approximately 20.8 kDa. UFC1 is expressed in a variety of tissues including liver kidney and heart indicating its widespread role in cellular processes. As an essential component in the UFM1 system UFC1 works closely with other proteins to regulate protein modification through UFMylation.
Biological function summary
UFC1 is involved in the process of UFMylation which modifies proteins through the attachment of UFM1 much like ubiquitination influences protein degradation and signaling. UFC1 forms part of a complex that also includes UBA5 and UFL1 the E1 activating enzyme and E3 ligase respectively. This UFMylation system is necessary for endoplasmic reticulum-associated degradation (ERAD) contributing to the maintenance of protein homeostasis within cells. The disruption of this modification process can impact cellular stress response and protein quality control mechanisms.
Pathways
UFC1 plays a critical role in the ER stress response and protein quality control pathways. Within these pathways UFC1 interacts with proteins such as UFM1 and UFL1 to mediate the UFMylation of target proteins during cellular stress. Additionally UFC1 has been linked to pathways regulating autophagy where it indirectly influences the degradation of defective proteins. This interaction ultimately affects the cellular response to misfolded proteins and is pivotal for maintaining cellular equilibrium.
UFC1 has implications in conditions such as cancer and neurological disorders. Abnormalities in UFMylation can contribute to the dysregulation of protein homeostasis which is frequently observed in cancerous cells. In the context of neurological disorders the dysfunctional UFM1 system involving UFC1 can result in impaired neuronal homeostasis. Additionally UFC1's relationship with proteins like UFM1 and UFL1 highlights its importance in the pathological processes of these diseases positioning it as a potential target for therapeutic intervention.
