UAP1 Recombinant Monoclonal Antibody

UDP-N-acetylhexosamine pyrophosphorylase, encoded by the UAP1 gene, serves as a critical enzyme in the hexosamine biosynthetic pathway, catalyzing the formation of UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine. These nucleotide sugars are essential substrates for protein glycosylation, glycolipid synthesis, and proteoglycan assembly, positioning UAP1 at a metabolic intersection that influences cellular signaling, protein quality control, and nutrient sensing. Altered UAP1 expression has drawn research attention for its potential roles in metabolic reprogramming and cellular stress responses.

This recombinant monoclonal antibody, clone 1F2, offers the reproducibility and consistency that demanding experimental workflows require. Produced using recombinant technology with a defined sequence, this rabbit IgG eliminates the lot-to-lot variability that can complicate longitudinal studies or multi-site collaborations. The antibody was raised against a synthetic peptide derived from human UAP1 and purified by affinity chromatography, ensuring high specificity for your target.

Validation in western blot applications demonstrates reliable detection in K562 whole cell lysate, where the antibody identifies a band at the predicted molecular weight of 59 kDa. The recommended working dilution range of 1:500 to 1:5000 provides flexibility to optimize signal intensity based on your specific sample conditions and detection systems. The antibody is also validated for ELISA, expanding its utility across different experimental platforms.

Whether you are investigating hexosamine pathway regulation, exploring connections between metabolism and signal transduction, or characterizing UAP1 expression patterns in human cell models, this antibody provides a dependable tool for advancing your research objectives.