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Digital PCR assays for lung cancer gene variants

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Revolutionizing lung cancer research with precision dPCR assays

Lung cancer presents significant challenges to oncology researchers due to its genetic complexity and mutation diversity. The development of personalized therapies relies on accurately detecting and understanding these gene variants. Digital PCR (dPCR) technology, known for its precision and sensitivity, can play a pivotal role in identifying these markers and advancing research, in particular where precise identification of low prevalence biomarkers is required.

Our leading portfolio of dPCR LNA Mutation Assays offers unmatched accuracy, sensitivity and reproducibility, enabling precise detection and quantification of key gene variants. These capabilities are essential for advancing targeted research and therapies, facilitating the development of more personalized treatment approaches.

Explore lung cancer related dPCR assays by gene

Lung cancer's complexity is underscored by its subtypes, each characterized by unique genetic markers and treatment responses. The most common subtype, non-small cell lung cancer (NSCLC), represents about 85% of cases and includes adenocarcinoma, squamous cell carcinoma and large cell carcinoma. Small cell lung cancer (SCLC) comprises most of the remaining cases.

Specific mutations in genes such as EGFR, KRAS, BRAF and others are pivotal in advancing our understanding of lung cancer progression and identifying potential therapeutic targets. These genetic variations also play a crucial role in studying the mechanisms of treatment resistance, informing the development of more effective targeted therapies. Our assay collection provides a robust toolkit for advanced oncology research, facilitating precise genetic analysis and insights. 

The table below includes COSMIC Variant IDs (COSV), as they provide a unique identifier for each distinct gene mutation and ensure precise reference to your variant of interest.
Gene
Mutation Type
Gene
Mutation Type
Mutation (CDS)
Mutation (AA)
COSMIC ID (COSV)
COSMIC ID (COSM)
Codon
dPCR Mutation Assay
BRAF Substitution - Missensec.1406G>Cp.G469ACOSV56061424COSM460469 DMH0000047
BRAF Substitution - Missensec.1798G>Ap.V600MCOSV56075762COSM1130600 DMH0000218
BRAF Substitution - Missensec.1798_1799delinsAAp.V600KCOSV56057713COSM473600 DMH0000001
BRAF Substitution - Missensec.1798_1799delinsAGp.V600RCOSV56058419COSM474600 DMH0000002
BRAF Substitution - Missensec.1799T>Ap.V600ECOSV56056643COSM476600 DMH0000004
BRAF Substitution - Missensec.1799T>Gp.V600GCOSV56080151COSM6137600 DMH0000068
BRAF Substitution - Missensec.1799_1800delinsAAp.V600ECOSV56059110COSM475600 DMH0000003
BRAF Substitution - Missensec.1799_1800delinsATp.V600DCOSV56059623COSM477600 DMH0000039
EGFR Substitution - Missensec.2125G>Ap.E709KCOSV51767260COSM12988709 DMH0000041
EGFR Substitution - Missensec.2126A>Cp.E709ACOSV51772956COSM13427709 DMH0000271
EGFR Substitution - Missensec.2126A>Tp.E709VCOSV51766584COSM12371709 DMH0000397
EGFR Substitution - Missensec.2155G>Ap.G719SCOSV51767289COSM6252719 DMH0000055
EGFR Substitution - Missensec.2155G>Tp.G719CCOSV51766606COSM6253719 DMH0000280
EGFR Substitution - Missensec.2156G>Cp.G719ACOSV51769339COSM6239719 DMH0000057
EGFR Deletion - In framec.2233_2247delp.K745_E749delCOSV51769442COSM26038745-749 DMH0000082
EGFR Deletion - In framec.2235_2249delp.E746_A750delCOSV51765119COSM6223746-750 DMH0000276
EGFR Deletion - In framec.2236_2250delp.E746_A750delCOSV51765066COSM6225746-750 DMH0000240
EGFR Deletion - In framec.2236_2253delp.E746_T751delCOSV51811139COSM12728746-751 DMH0000250
EGFR Deletion - In framec.2237_2251delp.E746_T751delinsACOSV51769364COSM12678746-751 DMH0000258
EGFR Deletion - In framec.2237_2254delp.E746_S752delinsACOSV51769704COSM12367746-752 DMH0000072
EGFR Deletion - In framec.2238_2255delp.E746_S752delinsDCOSV51772418COSM6220746-752 DMH0000232
EGFR Deletion - In framec.2239_2247delp.L747_E749delCOSV51780076COSM6218747-749 DMH0000262
EGFR Deletion - In framec.2239_2256delp.L747_S752delCOSV51767308COSM6255747-752 DMH0000076
EGFR Deletion - In framec.2240_2254delp.L747_T751delCOSV51766247COSM12369747-751 DMH0000275
EGFR Deletion - In framec.2240_2257delp.L747_P753delinsSCOSV51767961COSM12370747-753 DMH0000266
EGFR Deletion - In framec.2253_2276delp.S752_I759delCOSV51766231COSM13556752-759 DMH0000078
EGFR Substitution - Missensec.2303G>Tp.S768ICOSV51768106COSM6241768 DMH0000308
EGFR Insertion - In framec.2310_2311insGGTp.D770_N771insGCOSV51769298COSM12378770-771 DMH0000248
EGFR Substitution - Missensec.2369C>Tp.T790MCOSV51765492COSM6240790 DMH0000085
EGFR Substitution - Missensec.2389T>Ap.C797SCOSV51766493COSM6493937797 DMH0000007
EGFR Substitution - Missensec.2390G>Cp.C797SCOSV51766509COSM5945664797 DMH0000052
EGFR Substitution - Missensec.2573T>Gp.L858RCOSV51765161COSM6224858 DMH0000386
EGFR Substitution - Missensec.2582T>Ap.L861QCOSV51766344COSM6213861 DMH0000006
KRAS Substitution - Missensec.34G>Ap.G12SCOSV55497461COSM51712 DMH0000519
KRAS Substitution - Missensec.34G>Cp.G12RCOSV55497582COSM51812 DMH0000284
KRAS Substitution - Missensec.34G>Tp.G12CCOSV55497469COSM51612 DMH0000309
KRAS Substitution - Missensec.35G>Ap.G12DCOSV55497369COSM52112 DMH0000286
KRAS Substitution - Missensec.35G>Cp.G12ACOSV55497479COSM52212 DMH0001055
KRAS Substitution - Missensec.35G>Tp.G12VCOSV55497419COSM52012 DMH0000285
KRAS Substitution - Missensec.37G>Ap.G13SCOSV55509530COSM52813 DMH0000331
KRAS Substitution - Missensec.37G>Cp.G13RCOSV55502117COSM52913 DMH0000332
KRAS Substitution - Missensec.37G>Tp.G13CCOSV55497378COSM52713 DMH0000195
KRAS Substitution - Missensec.38G>Ap.G13DCOSV55497388COSM53213 DMH0000289
KRAS Substitution - Missensec.38G>Cp.G13ACOSV55497357COSM53313 DMH0000334
KRAS Substitution - Missensec.38G>Tp.G13VCOSV55522580COSM53413 DMH0000527
KRAS Substitution - Missensec.38_39delinsATp.G13DCOSV55508630COSM53113 DMH0000525
KRAS Substitution - Missensec.181C>Ap.Q61KCOSV55502066COSM54961 DMH0000290
KRAS Substitution - Missensec.181C>Gp.Q61ECOSV55502677COSM55061 DMH0000044
KRAS Substitution - Missensec.182A>Cp.Q61PCOSV55508574COSM55161 DMH0000022
KRAS Substitution - Missensec.182A>Gp.Q61RCOSV55498739COSM55261 DMH0000023
KRAS Substitution - Missensec.182A>Tp.Q61LCOSV55504296COSM55361 DMH0000198
KRAS Substitution - Missensec.183A>Cp.Q61HCOSV55498802COSM55461 DMH0000024
KRAS Substitution - Missensec.183A>Tp.Q61HCOSV55499223COSM55561 DMH0000025
NRAS Substitution - Missensec.34G>Ap.G12SCOSV54736621COSM56312 DMH0000188
NRAS Substitution - Missensec.34G>Cp.G12RCOSV54736940COSM56112 DMH0000336
NRAS Substitution - Missensec.34G>Tp.G12CCOSV54736487COSM56212 DMH0000186
NRAS Substitution - Missensec.35G>Cp.G12ACOSV54736555COSM56512 DMH0000339
NRAS Substitution - Missensec.35G>Tp.G12VCOSV54736974COSM56612 DMH0000340
NRAS Substitution - Missensec.37G>Ap.G13SCOSV54736476COSM57113 DMH0000510
NRAS Substitution - Missensec.37G>Cp.G13RCOSV54736550COSM56913 DMH0000341
NRAS Substitution - Missensec.37G>Tp.G13CCOSV54736386COSM57013 DMH0000342
NRAS Substitution - Missensec.38G>Ap.G13DCOSV54736416COSM57313 DMH0000343
NRAS Substitution - Missensec.38G>Cp.G13ACOSV54736793COSM57513 DMH0000345
NRAS Substitution - Missensec.38G>Tp.G13VCOSV54736480COSM57413 DMH0000344
NRAS Substitution - Missensec.181C>Ap.Q61KCOSV54736310COSM58061 DMH0000505
NRAS Substitution - Missensec.181C>Gp.Q61ECOSV54743343COSM58161 DMH0000347
NRAS Substitution - Missensec.182A>Gp.Q61RCOSV54736340COSM58461 DMH0000183
NRAS Substitution - Missensec.182A>Tp.Q61LCOSV54736624COSM58361 DMH0000190
NRAS Substitution - Missensec.183A>Cp.Q61HCOSV54736320COSM58661 DMH0000180
NRAS Substitution - Missensec.183A>Tp.Q61HCOSV54736991COSM58561 DMH0000349
PIK3CA Substitution - Missensec.1633G>Ap.E545KCOSV55873239COSM763545 DMH0000292
PIK3CA Substitution - Missensec.1634A>Gp.E545GCOSV55873220COSM764545 DMH0000033
PIK3CA Substitution - Missensec.3129G>Tp.M1043ICOSV55878974COSM7731043 DMH0000034
PIK3CA Substitution - Missensec.3139C>Tp.H1047YCOSV55876499COSM7741047 DMH0000209
PIK3CA Substitution - Missensec.3140A>Gp.H1047RCOSV55873195COSM7751047 DMH0000036
PIK3CA Substitution - Missensec.3140A>Tp.H1047LCOSV55873401COSM7761047 DMH0000062
PTEN Substitution - Missensec.388C>Gp.R130GCOSV64288384COSM5219130 DMH0000296
PTEN Substitution - Nonsensec.388C>Tp.R130*COSV64288463COSM5152130 DMH0000294
PTEN Substitution - Nonsensec.697C>Tp.R233*COSV64288653COSM5154233 DMH0000295
TP53 Substitution - Missensec.488A>Gp.Y163CCOSV52663142COSM10808163 DMH0000112
TP53 Substitution - Missensec.517G>Tp.V173LCOSV52676535COSM43559173 DMH0000126
TP53 Substitution - Missensec.578A>Gp.H193RCOSV52662414COSM10742193 DMH0000108
TP53 Substitution - Missensec.659A>Gp.Y220CCOSV52661282COSM10758220 DMH0000440
TP53 Substitution - Missensec.743G>Tp.R248LCOSV52675468COSM6549248 DMH0000381
TP53 Substitution - Missensec.818G>Ap.R273HCOSV52660980COSM10660273 DMH0000094
TP53 Substitution - Missensec.818G>Tp.R273LCOSV52664805COSM10779273 DMH0000114
TP53 Substitution - Missensec.856G>Ap.E286KCOSV52664318COSM10726286 DMH0000364
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Discover the QIAcuity family of dPCR instruments

Explore the QIAcuity family of dPCR instruments, designed to meet the rigorous demands of biomarker research, translational research and clinical applications. With unmatched precision and operational efficiency, these versatile platforms can transform your scientific and diagnostic efforts.

Transform your research capabilities with QIAcuity digital PCR

QIAcuity is a fully automated digital PCR system that combines precision, efficiency and ease of use. Experience unparalleled accuracy and save resources with high-throughput multiplexing, allowing for the simultaneous detection of up to five genetic targets. A seamless transition from existing qPCR workflows ensures minimal disruption while significantly enhancing data quality and throughput.

Streamline your clinical PCR workflows with QIAcuityDx

QIAcuityDx is tailored for IVD applications. This fully automated system enhances diagnostic precision and operational efficiency by reducing hands-on time and ensuring accurate detection and quantification of important genetic variations. Easily develop your own assay menu* by using QIAcuityDx utility mode and IVD medical device consumables, reagents and software.

*FDA ‘Medical Devices; Laboratory Developed Tests’ final rule, May 6, 2024 and European Union regulation requirements on ‘In-House Assays’ (Regulation (EU) 2017/746 -IVDR- Art. 5(5))

Frequently asked questions

Discover key insights into genes and variants critical for lung cancer research and how they can be detected using digital PCR
How do dPCR LNA Mutation Assays benefit cancer researchers?
dPCR LNA Mutation Assays offer significant advantages to cancer researchers working on precise and sensitive mutation detection. These assays are specifically designed for use with the QIAcuity Digital PCR System and are enhanced with Locked Nucleic Acid (LNA) technology. This enhancement greatly improves the specificity and sensitivity of mutation detection, making it possible to identify DNA sequence mutations at very low abundance, with a sensitivity as fine as 0.1% in a single nanoplate well.

The key benefits of dPCR LNA Mutation Assays for cancer researchers include:
  • High precision and sensitivity: The use of duplex, hydrolysis probe-based assays allows for highly precise detection of mutations. The presence of both mutant and wild-type probes in the same reaction ensures that researchers can detect and quantify minor genetic variations with great accuracy, crucial for studies in heterogeneous cancer samples where only a few cells may carry the mutation.
  • Enhanced specificity: The integration of LNA into the probes increases the binding affinity and specificity towards the target sequences, minimizing the risk of non-specific bindings and improving the overall reliability of the assays.
  • Multiplexing capability: Each assay is capable of detecting mutations using two different fluorescent dye combinations, allowing for the simultaneous analysis of mutant and wild-type alleles within the same reaction. This multiplexing ability is particularly useful in applications requiring the analysis of multiple targets, such as assessing co-occurring mutations in cancer.
  • Flexibility in sample analysis: By dividing the reaction across multiple wells, even greater sensitivity can be achieved, facilitating the detection of extremely rare mutations. This is especially valuable in cancer research, where detecting low-frequency mutations can inform prognosis and treatment strategies.
  • Streamlined workflow: Supplied in a single-tube format with ready-to-use primer pairs and probes, these assays simplify the experimental setup, enabling efficient and straightforward integration into existing research workflows.
What role does EGFR play in lung cancer?

EGFR (epidermal growth factor receptor) is a receptor tyrosine whose mutations are implicated in the uncontrolled cell proliferation characteristic of non-small cell lung cancer (NSCLC). These specific EGFR gene variants play a critical role in the cascade of signals that lead to cellular growth and division, marking them as prime targets for therapies tailored to halt this progression. The identification and targeting of these mutations have been pivotal in improving patient outcomes, as they are central to the development and advancement of the disease and respond well to targeted treatments that specifically inhibit the aberrant EGFR signaling in NSCLC.

  • EGFR Exon 19 Deletions: Deletions in exon 19 generally result in the loss of four amino acids from the EGFR kinase domain, which alters the configuration of the protein, enhancing tyrosine kinase activity. This increase in enzymatic activity leads to unchecked cell signaling pathways that drive tumorigenesis and tumor growth. Molecular models suggest that this deletion affects the dynamic equilibrium of the kinase domain, shifting it towards an active state.
  • EGFR c.2573T>G / L858R Point Mutation in Exon 21: The L858R mutation changes the hydrophobic core of the kinase domain, leading to a conformation that mimics the active state of the EGFR protein. This mutation stabilizes the active conformation even in the absence of ligand binding, promoting constant downstream signaling. Structural analysis reveals that the arginine residue at position 858 forms new stabilizing interactions that are absent in the wild-type kinase, which increases the affinity of the kinase domain for ATP.
  • EGFR c.2369C>T / T790M Point Mutation in Exon 20: The T790M mutation introduces a bulkier methionine residue into the ATP-binding pocket, which can affect drug binding. This mutation is associated with acquired resistance to first- and second-generation tyrosine kinase inhibitors (TKIs) because it increases the binding affinity for ATP, making it more competitive against these drugs. The steric hindrance caused by the methionine also interferes with the proper binding of some TKIs.
  • EGFR Exon 20 Insertions: Insertions in exon 20 lead to the addition of amino acids within or near the C-helix of the kinase domain, disrupting the normal kinase activity regulation and causing constitutive activation. These insertions can lead to unique structural changes that may affect the binding of ATP and TKIs differently compared to other EGFR mutations, explaining the resistance to certain therapies.
  • EGFR c.2155G>A / G719X Point Mutation in Exon 18: Mutations at codon 719, typically resulting in substitution of glycine by cysteine (G719C), alanine (G719A), or serine (G719S), alter the ATP-binding pocket of the EGFR kinase domain. These changes alter the charge and steric properties of the pocket, increasing the kinase's intrinsic activity. The G719X mutations are thought to affect the conformational dynamics of the kinase activation loop, enhancing its activity even without ligand stimulation.
How is KRAS involved in lung cancer?

KRAS (Kirsten rat sarcoma viral oncogene homolog) is a gene encoding a GTPase that functions as a molecular switch within the RAS/MAPK signaling pathway, regulating cell division, differentiation and apoptosis. In lung cancer, particularly NSCLC, mutations in the KRAS gene represent a common oncogenic driver, resulting in constitutive activation of downstream signaling pathways that promote cellular proliferation and survival independent of external growth signals. These mutations are often associated with resistance to EGFR-targeted therapies and are considered a hallmark of poor prognosis. The identification of KRAS mutations provides critical insight into the pathophysiology of lung cancer and guides therapeutic decision-making, although direct targeting remains challenging.

  • KRAS c.34G>T / G12C Mutation: The G12C mutation results from a single nucleotide change, leading to the substitution of glycine with cysteine at codon 12 in the KRAS protein. This alteration disrupts the GTPase activity, locking KRAS in its active GTP-bound state, and perpetuates the growth signal. This specific variant is noteworthy because it is targetable by covalent inhibitors that bind to the cysteine residue, offering a therapeutic opportunity for patients with KRAS G12C-mutant lung cancer.
  • KRAS c.35G>A / G12D and KRAS c.35G>T / G12V Mutations: Both the G12D and G12V mutations involve the substitution of glycine at codon 12 with aspartic acid and valine, respectively. These changes further reduce the intrinsic GTPase activity of KRAS, leading to sustained activation of the protein. These mutations are less amenable to targeted therapy compared to G12C, but they remain important biomarkers for prognosis and are the subject of ongoing drug development efforts.
  • KRAS c.38G>A / G13 Mutations: Mutations at codon 13, most commonly resulting in a glycine-to-aspartic acid substitution (G13D), similarly impair the GTPase activity of KRAS, contributing to continuous activation of signaling pathways. The impact of G13 mutations on prognosis and treatment response is an active area of research, with some studies suggesting differential responses to certain chemotherapy agents.
How does BRAF mutation affect lung cancer?

BRAF (v-Raf murine sarcoma viral oncogene homolog B) is a proto-oncogene that encodes a protein kinase involved in the MAPK/ERK signaling pathway, which regulates cell growth, differentiation and survival. In lung cancer, mutations in the BRAF gene can lead to constitutive activation of the MAPK pathway, driving tumorigenesis and cancer progression. These mutations are less common than KRAS or EGFR mutations but are important because they represent another piece of the lung cancer genomic puzzle and are amenable to targeted therapy. The discovery of specific BRAF mutations has expanded the arsenal of molecularly targeted treatments, providing tailored options that can significantly impact clinical outcomes.

  • BRAF c.1799T>A / V600E Mutation: The V600E mutation involves the substitution of valine with glutamic acid at position 600, which is located in the activation segment of the BRAF kinase domain. This mutation leads to a high level of kinase activity that stimulates the MAPK/ERK pathway without the need for upstream activation. BRAF V600E is the most common BRAF mutation in lung cancer and is actionable with inhibitors that have demonstrated efficacy in treating melanoma, leading to interest in their use for lung cancer harboring the same mutation.
  • Non-V600 BRAF Mutations: Non-V600 BRAF mutations, such as BRAF c.1406G>C / G469A and BRAF c.1781A>G / D594G, occur in regions of the kinase domain other than the activation segment and result in intermediate to low kinase activity. While these mutations are less common and less well-understood than the V600E mutation, they can still contribute to oncogenesis through aberrant MAPK pathway signaling. Their therapeutic implications are currently an area of active investigation, with a potential for combination therapies to target the altered signaling cascade effectively.
What is the significance of ALK in lung cancer?
ALK (anaplastic lymphoma kinase) is a gene that encodes a transmembrane receptor tyrosine kinase. Under normal physiological conditions, ALK plays a crucial role in the development of the nervous system during embryogenesis. However, ALK can create fusion proteins through chromosomal rearrangements. These ALK fusion proteins, such as EML4-ALK, are oncogenic drivers in a subset of non-small cell lung cancer (NSCLC) and are important therapeutic targets.
How does TP53 contribute to lung cancer?
TP53 (tumor protein p53) is a gene that encodes a crucial tumor suppressor protein involved in regulating the cell cycle, DNA repair and apoptosis. In lung cancer, TP53 mutations are among the most common genetic alterations, occurring in approximately 50–60% of non-small cell lung cancers (NSCLC) and 90% of small cell lung cancers (SCLC). These mutations typically result in the loss of normal TP53 tumor suppressor functions and can also confer gain-of-function properties that promote tumor progression and resistance to therapy. TP53 mutations are associated with a worse prognosis and increased resistance to chemotherapy and radiation in lung cancer patients
What is the role of MET in lung cancer?
MET (mesenchymal-epithelial transition factor), or MET proto-oncogene, is a gene that encodes a transmembrane receptor tyrosine kinase known as the hepatocyte growth factor receptor (HGFR). In lung cancer, MET can be dysregulated through mechanisms such as gene amplification, mutations, overexpression or fusion/rearrangement. These alterations lead to aberrant MET signaling, which promotes oncogenic processes including proliferation, survival, migration and invasion of cancer cells. MET dysregulation is particularly significant in non-small cell lung cancer (NSCLC), where it can act as a primary oncogenic driver or contribute to acquired resistance to therapies targeting other pathways, such as EGFR inhibitors. Consequently, MET is a critical biomarker and therapeutic target in lung cancer, with MET inhibitors showing promise in clinical trials for patients with MET-altered tumors.
In what way is PIK3CA associated with lung cancer?
PIK3CA (phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha) is a gene that encodes the p110α catalytic subunit of the PI3K enzyme, which is involved in the PI3K/AKT signaling pathway. Under normal physiological conditions, PIK3CA plays a crucial role in regulating cell growth, proliferation, survival and metabolism. PIK3CA mutations are observed in a subset of non-small cell lung cancer (NSCLC). These mutations lead to constitutive activation of the PI3K/AKT pathway, promoting uncontrolled cell proliferation and survival and contributing to tumorigenesis.
How are ROS1 rearrangements important in lung cancer?

ROS1 (c-ros oncogene 1) is a gene that encodes a receptor tyrosine kinase involved in cell growth and differentiation. The function of ROS1 is not fully understood, but it is known to play a significant role in several cellular signaling pathways, including the PI3K/AKT/mTOR pathway, the RAS/RAF/MEK/ERK pathway, and the JAK/STAT pathway. These pathways are critical for regulating cell proliferation, survival, and apoptosis. ROS1 can create fusion proteins through chromosomal rearrangements, where the ROS1 gene fuses with other genes, such as CD74, SLC34A2, TPM3, and FIG. These ROS1 fusion proteins are potent oncogenic drivers and are implicated in a subset of non-small cell lung cancer (NSCLC). The most common fusion partner in NSCLC is CD74, forming the CD74-ROS1 fusion protein, which results in constitutive kinase activity leading to uncontrolled cell growth and survival.

What impact do RET rearrangements have on lung cancer?
RET (rearranged during transfection) is a gene that encodes a receptor tyrosine kinase involved in cell growth, differentiation and survival. Under normal physiological conditions, RET plays a crucial role in the development of the nervous system and kidneys. RET can create fusion proteins through chromosomal rearrangements. These RET fusion proteins are oncogenic drivers in a subset of non-small cell lung cancer (NSCLC).
How does the loss of RB1 function affect lung cancer?
RB1 (retinoblastoma 1) is a gene that encodes a tumor suppressor protein involved in regulating the cell cycle. Normally, RB1 plays a vital role in controlling cell proliferation by inhibiting the cell cycle progression from the G1 to the S phase. Mutations or deletions in RB1 are frequently observed in various cancers, including non-small cell lung cancer (NSCLC). These alterations disrupt the normal tumor suppressor functions of RB1, leading to uncontrolled cell proliferation and tumorigenesis.

Disclaimers

dPCR LNA Mutation Assays are intended for molecular biology applications. These products are not intended for the diagnosis, prevention, or treatment of a disease.

The QIAcuity is intended for molecular biology applications. This product is not intended for the diagnosis, prevention or treatment of a disease. Therefore, the performance characteristics of the product for clinical use (i.e., diagnostic, prognostic, therapeutic or blood banking) is unknown.

The QIAcuityDx dPCR System is intended for in vitro diagnostic use, using automated multiplex quantification dPCR technology, for the purpose of providing diagnostic information concerning pathological states.

QIAcuity and QIAcuityDx dPCR instruments are sold under license from Bio-Rad Laboratories, Inc. and exclude rights for use with pediatric applications. The QIAcuityDx medical device is currently under development and will be available in 20 countries in H2 2024.