Thanks, Sujal. Good morning, everyone. Q2 marked a major inflection point in our scientific journey. As Sujal mentioned, this quarter, we shared a preprint of a manuscript illustrating how our iterative mapping method enables a unique capability on the Nautilus platform, resolution of proteoforms at the single molecule level at scale. In traditional proteomic techniques, a protein is often treated as a single entity. But the reality is that proteins exist in many modified forms, each with their own distinct structure and function. These different variants are called proteoforms. Just like a single gene may have thousands of variants defined by mutations, a single protein may have thousands of different proteoforms defined by a combination of alternative splicing and multiple post-translational modifications. The prevalence of different proteoforms may ultimately influence the role a protein plays in disease and how best to therapeutically target it. Before I dive in, I'd like to clarify one important point. You'll hear from others that they are measuring proteoforms. However, the reality is that only platforms that look at intact protein molecules and are able to interrogate multiple positions on those molecules are capable of examining proteoforms with the necessary resolution. Existing affinity-based methods such as Olink, SomaScan or LMR are able to report the relative amount of a protein, but they typically do not measure modifications of those proteins and certainly not the co-occurrence of those modifications on individual protein molecules. Likewise, peptide-based methods, such as employed by Shotgun mass spectrometry or even single molecule peptide sequencing methods entirely lose the contextual information required to know that multiple modifications are co-occurring on a single protein molecule. Any peptide-based measurement method cannot measure proteoforms. Consequently, we believe that the Nautilus platform is the only platform that has been designed to readily quantify the thousands of distinct proteoforms of key proteins at scale. With the release of our manuscript, we publicly demonstrated the remarkable real- world capabilities of our iterative mapping method. This is notable for 2 distinct reasons. First, the manuscript represents an end-to- end validation of our core platform, which is shared between our targeted proteoform assays and our forthcoming broadscale assay. Second, the manuscript demonstrates that the tau assay built upon our platform has the ability to drive powerful biological insight into Alzheimer's disease and related disorders. Diving in, the first part of the manuscript shows that the platform is able to go end-to-end from sample to answer by taking individual protein molecules from complex samples, attaching them to DNA origami nanoparticles, depositing those nanoparticles on nanofabricated arrays, iteratively probing them and then applying our machine learning-based engine to quantify the proteoforms in the sample. When we began the company 8 years ago, each of these challenges represented its own complex scientific frontier. Consequently, demonstrating them fully integrated is an important proof point regarding the scientific foundations of our approach. After introducing the method and how that method is applied to assay the Alzheimer's disease-associated protein tau, we performed extensive assay characterization that serves as external confirmation of the platform scientific rigor and technical maturity. I'd like to call out 2 specific aspects of the platform characterization data that will have concrete impacts to our customers. First is the reproducibility data. It is extremely uncommon for first introductions of a new method to perform such a rigorous and extensive characterization of reproducibility. However, we've heard from our future customers that reproducibility is top of mind for them. This is natural as high reproducibility allows researchers to trust their results and know that they are more likely to be able to be replicated by researchers in other labs. We measure the within experiment reproducibility of our platform as having a median CV of 1.5%. Even across multiple instruments, reagent lots, operators, sample preparations and runs, our median CVs were approximately 5%. To put that in perspective, studies of the reproducibility of existing, mature, affinity-based and mass spectrometry-based proteomics platforms that look solely at total protein abundances, not proteoforms, have found median coefficiency variation of nearly 40% from run-to-run and up to 80% across labs and operators. The reproducibility of our platform, even at this earliest stage is a direct consequence of our single molecule methodology, which determines protein abundance not from a single measurement, but instead from the aggregate of independent measurements of many, many individual molecules. Our reproducibility is also a consequence of our incredible team's steadfast commitment to quality. As I mentioned, reproducibility of this type would be considered exceptional for a mature platform. to have demonstrated such world-leading reproducibility at the first introduction of a novel method is astonishing. We additionally demonstrated that the assay is extremely sensitive and able to accurately measure changes to proteoforms abundance across a wide range of physiologically relevant concentrations. For reference, mass spectrometric methods such as tandem mass tagging, lose quantitative accuracy when comparing samples in which a protein's abundance changes by more than a factor of 10. Our analysis revealed that our assay could reliably measure how much a proteoform changes even for changes of over a factor of 1,000. Furthermore, the assay is able to accurately quantify extremely low abundances of proteoforms. Forms of tau present in samples at levels approximately 0.1% of total tau can be reliably quantified. This is critical as we know that low abundance forms of proteins like tau can still be tremendously impactful in disease progression. Beyond demonstrating the technical capabilities of our platform, the studies we presented are already providing unique biological insight into Alzheimer's disease and related disorders. Before discussing the paper specifically, I'd like to give a bit of context as to why the findings are potentially so significant. The link between tau and Alzheimer's disease has been established for nearly 40 years. In that time, a huge number of potential biomarker tests and therapeutics targeting tau were developed with the goal of diagnosing AD early and stopping or reversing its progression. Unfortunately, these assays and therapeutics have failed in clinical trials. Retrospective analysis suggests these failures may have stem from targeting the wrong proteoform of tau. Unfortunately, prior to the introduction of the Nautilus platform, measuring these proteoforms was out of reach. The proteoform resolution offered by the Nautilus platform gives researchers actionable biological insights that aren't otherwise attainable. With the Nautilus platform, researchers will be able to observe not just how much of a protein is present, but which forms are increasing, decreasing or appearing uniquely in specific states, knowledge that is critical for understanding mechanisms of disease and for identifying precise therapeutic targets. In our study, we examined a diversity of model systems that are used by researchers around the world to develop the next generation of therapeutics and biomarkers. For the first time, we were able to measure more than 130 different forms of tau that were present, some of which had as many as 6 co-occurring phosphorylation events. Existing platforms would have mushed all those forms together, providing a low-resolution readout of total tau that obscures the critical proteoform information. In addition to looking at model systems, we applied our method to a small human cohort. Within that cohort was a patient with aggressive AD. This patient was clearly delineated from healthy controls and even other patients with less advanced AD by a form of tau that was quadruply phosphorylated. Moreover, the pattern of forms of doubly and triply phosphorylated tau strongly suggests an order and a timing to how the proteoform came to be formed, an observation that previously had not been possible. This combination of technical rigor and biological insight is why the reaction from researchers with whom we've shared the manuscript has been so strong. They recognize that this isn't just a new measurement method. It's a fundamentally different way of understanding biology. They see that iterative mapping represents an entirely new class of measurement modalities distinct from either mass spectrometry-based approaches or the affinity reagent profiling methods. Scientists are already asking how they can start integrating the method into their workflows. As we continue to expand our reagent panels and data analysis capabilities, we're confident this core capability will remain a major driver of scientific adoption. For an easier-to-understand synopsis of the manuscript, I encourage you to check out our blog where we've tried to distill the manuscript into a form that is more broadly accessible. We believe that these findings validate the full Nautilus platform, not just for tau, but as a generalizable engine for proteomic insight. The core platform and iterative mapping method used in the tau studies is also used for broad scale analysis, and we anticipate the exceptional performance we've observed will translate across applications. Looking ahead, our road map for the remainder of 2025 includes continuing to refine and scale our broadscale assay configuration, advancing multiple external collaborations for tau and non-tau targets, publishing additional data sets and technical white papers to support adoption. With the release of this manuscript and the strong momentum across our platform development and collaborations, we're confident that Nautilus is on track to deliver on its mission to transform how biology is measured and understood. Back to you, Sujal.