RPN1 Recombinant Monoclonal Antibody

RPN1, also known as Ribophorin I, serves as an essential subunit of the oligosaccharyltransferase complex responsible for N-linked glycosylation of nascent polypeptides in the endoplasmic reticulum. This fundamental post-translational modification pathway influences protein folding, stability, and trafficking, making RPN1 a valuable target for researchers investigating ER function, glycoprotein biosynthesis, and cellular stress responses.

This recombinant monoclonal antibody, clone 21F2, offers the reproducibility and consistency that demanding experimental workflows require. Because the antibody sequence is defined and produced recombinantly in rabbit host cells, researchers can expect uniform performance across experiments and between lots, eliminating the variability concerns often associated with traditional hybridoma-derived antibodies. The affinity-chromatography purification ensures high specificity for your target.

Validation studies demonstrate reliable performance across multiple experimental platforms. In western blot applications, this antibody detects RPN1 at the expected molecular weight of approximately 70 kDa, closely matching the predicted size of 69 kDa. The slight difference likely reflects post-translational modifications consistent with RPN1's role in the glycosylation machinery. Detection has been confirmed across diverse human cell lines including A431, HT29, HL-60, K562, and HeLa whole cell lysates at dilutions ranging from 1:500 to 1:2000. For flow cytometry applications, the antibody has been validated in HeLa cells using intracellular staining protocols, with recommended dilutions of 1:50 to 1:200.

This antibody supports investigations into ER biology, protein quality control mechanisms, and glycosylation-related disease pathways, providing researchers with a dependable tool for characterizing RPN1 expression and function in human samples.