Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 8 bp deletion in exon7.,
Disease:Adenocarcinoma
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-EPHA1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, 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.
Eph receptor A1 also known by the alternative name EphA1 is a member of the ephrin receptor family part of the larger group of receptor tyrosine kinases. The EphA1 protein carries a molecular mass of approximately 108 kDa. Mechanically it functions as a cellular signaling molecule by binding ephrins its membrane-bound ligands which initiates bidirectional signaling pathways. This interaction typically occurs at cell-cell interfaces involving dynamic communication essential for cellular processes. EphA1 is expressed in a variety of tissues with a significant presence in epithelial tissues where it plays roles in maintaining tissue architecture.
Biological function summary
EphA1 contributes to cellular adhesion migration and positioning linking to ephrin ligands to form signaling complexes. These complexes aid in regulating developmental processes such as angiogenesis and neuronal development by transmitting signals that control cell shape and movement. The EphA1 receptor also influences cell proliferation and plays a role in the inhibition of cell migration by responding to concentration gradients of ephrin ligands. Its ability to control cellular boundaries and morphology highlights its importance in tissue patterning and organogenesis.
Pathways
EphA1 integrates into the Eph/ephrin signaling pathway a critical framework for developmental processes and cellular organization. This pathway involves cross-talk with the MAPK signaling cascade which further influences cell proliferation and differentiation. The interplay between EphA1 and other Eph receptors like EphB2 enhances bidirectional signaling that accommodates both forward and reverse signal transduction a feature that accommodates dynamic cellular responses in development and homeostasis.
EphA1 has significant connections to cancer progression and metastasis particularly in colorectal carcinoma and melanoma. Alterations in EphA1 expression can lead to deregulated cellular pathways contributing to tumor development and spread. EphA1's relationship with proteins like ephrin A1 and other Eph receptors such as EphA2 provides a link between its dysregulation and cancer pathology highlighting its potential as a therapeutic target in oncology.
