Abcam, ab258607, Human PSAT1 (Phosphoserine Aminotransferase) knockout HEK-293T cell lysate

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PSAT1 KO cell lysate available now. KO validated by. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon 1 and 4 bp deletion in exon 1 and Insertion of the selection cassette in exon 1.
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon 1 and 4 bp deletion in exon 1 and Insertion of the selection cassette in exon 1.

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-PSAT1, 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.
Phosphoserine Aminotransferase (PSAT1) is an enzyme that actively participates in amino acid metabolism. It is also known by alternate names like O-phospho-L-serine:2-oxoglutarate aminotransferase. With a molecular mass of approximately 39 kDa PSAT1 facilitates the conversion of 3-phosphohydroxypyruvate to phosphoserine. You can find its expression across various tissues including liver brain and kidney. This widespread presence suggests its essential role in cellular functions and metabolism.
Biological function summary
PSAT1 plays an important role in the biosynthesis of the amino acid serine. It is part of a multi-step serine biosynthesis complex involving other enzymes like 3-phosphoglycerate dehydrogenase and phosphoserine phosphatase. PSAT1 works in conjunction with these enzymes to ensure the proper synthesis of serine which is vital for nucleotide synthesis and cell proliferation. This function establishes PSAT1 as an important regulator of cellular growth and division.
Pathways
PSAT1 is a significant component of the serine biosynthesis pathway which is linked to the folate cycle. This metabolic pathway is important for one-carbon metabolism affecting thymidine and purine synthesis. PSAT1 interacts with proteins such as 3-phosphoglycerate dehydrogenase highlighting its involvement in these interconnected metabolic processes. This connection indicates the critical position that PSAT1 holds in facilitating the production of biomolecules essential for cell survival and function.
PSAT1 has been associated with conditions such as Neu-Laxova syndrome and certain cancer types. Neu-Laxova syndrome linked to defects in serine biosynthesis involves abnormal neurological and physical development. Additionally PSAT1's role in cell proliferation pathways associates it with oncogenic processes where its altered expression can lead to tumor growth. Dysregulation of related proteins like phosphoserine phosphatase further ties PSAT1 to the pathogenesis of these conditions making it a target of interest in therapeutic research.