Abcam, ab163575, Recombinant Human SERINC1 protein

Size: 10µg
Recombinant Human SERINC1 protein is a Human Full Length protein, in the 1 to 453 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:Q9NRX5,
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.
SERINC1 also known as Serine Incorporator 1 is a membrane protein involved in the incorporation of serine into lipids. It has a molecular mass of approximately 53 kDa. Scientists have identified SERINC1 as highly expressed in several tissues including the brain testis and liver. The protein localizes largely at the plasma membrane and participates actively in lipid biosynthesis.
Biological function summary
SERINC1 modulates the synthesis of phosphatidylserine and sphingolipids which are critical for cellular functions. It acts as part of a larger complex playing a role in the folding and trafficking of proteins to the membrane. SERINC1's activity influences membrane-related processes which include vesicle trafficking and cell signaling. In particular the protein impacts cellular processes through the regulation of membrane composition.
Pathways
Researchers have placed SERINC1 within the lipid metabolism and serine biosynthesis pathways. SERINC1 regulates the distribution of serine into pathways necessary for lipid and nucleotide synthesis. Other proteins related to these pathways include CDP-diacylglycerol—serine O-phosphate phosphatidyltransferase 1 which is key in the phosphatidylserine biosynthetic process. The interaction between these proteins ensures proper cellular lipid composition and function.
Studies have linked SERINC1 to neurological and metabolic conditions. Dysregulation of SERINC1 is observed in some cases of schizophrenia suggesting its involvement in neurological pathways. Furthermore disturbances in lipid metabolism such as those found in metabolic syndrome may involve altered SERINC1 function. Its relationship with proteins like phosphatidylserine decarboxylase central to the production of phosphatidylethanolamine highlights its relevance in disease contexts where lipid imbalances are pronounced.