Abcam, ab163753, Recombinant Human FAM111A protein

Size: 10µg
Recombinant Human FAM111A protein is a Human Full Length protein, in the 1 to 611 aa range, expressed in Wheat germ, suitable for ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:WB, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q96PZ2,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.31% Glutathione

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
FAM111A also known as Family with Sequence Similarity 111 Member A is a protein with a molecular mass of approximately 66 kDa. It is expressed in various tissues including the spleen thymus and liver. FAM111A possesses a serine protease domain which links it to protease activity. Its expression is especially noted in actively proliferating cells suggesting a function in cell cycle regulation.
Biological function summary
FAM111A participates in DNA replication and cell division. It often associates with components of the DNA replication machinery acting to maintain genomic stability during the cell cycle. Researchers have identified FAM111A as an essential factor for proper DNA synthesis. The protein may also interact with other cellular factors to ensure accurate DNA replication although it does not appear to form part of a large stable complex.
Pathways
Studies connect FAM111A to the DNA replication and repair pathways. It interacts with proteins involved in maintaining the integrity of the genome such as those in the replication fork machinery. FAM111A participates alongside proteins like DNA polymerase and helicase where it contributes to their regulation and function. This involvement places FAM111A as an important component for effective DNA damage response and repair.
Mutations in FAM111A are linked to Kenny-Caffey Syndrome and Gracile Bone Dysplasia. These relate to abnormal growth and skeletal development. The protein's dysfunction disrupts normal cell cycle and growth regulator mechanisms. Alterations affecting FAM111A may also involve interactions with cyclins or cyclin-dependent kinases important for proper cell cycle progression. Understanding FAM111A's role can provide insights into therapeutic approaches for managing these conditions.