In closed communities such as the Amish in North America, rare genetic disorders occur more frequently. In children from this community, a condition has been described that affects the development of the nervous system and manifests, for example, as muscle weakness or epileptic seizures. The disorder is linked to a small change in a single protein, but for a long time it was unclear which cellular process this change disrupts. This question has now been answered by researchers from CEITEC Masaryk University, who show that the disease is caused by a disruption of a key mechanism required for the proper processing of genetic information in the cell.Every cell must first transcribe genetic information and then modify it before it can be used. From the original “working transcript,” unnecessary parts are removed and the remaining pieces are precisely joined together. This process, known as RNA splicing, consists of many consecutive steps and is tightly regulated. If the process does not proceed correctly or stops at any point, the cell cannot properly convert the copied genetic information into a usable form and therefore cannot function as it should.Researchers from CEITEC Masaryk University have now described one of the key steps in this process – a specific signal inside the cell. This signal acts as a checkpoint: only once it is fulfilled, the entire mechanism is activated and the process can continue.“We showed that during RNA splicing, a chemical modification of the protein SF3B1 is required at a precisely timed step. This modification allows another protein, SNIP1, to bind. If this signal is not transmitted correctly, the cell cannot proceed with the splicing process,” explains first author <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/pavla-gajduskova-ph-d/u26136?page=publication">Pavla Gajdušková</a>.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_4_79e003984a.jpeg" alt="CEITEC: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Pavla Gajdušková" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_4_79e003984a.jpeg 235w," sizes="100vw" width="1600" height="1067">This is where the research connects to patients in the Amish community. In affected children, a small genetic change in the SNIP1 protein disrupts its ability to respond properly to the signal mediated by the modified SF3B1 protein, making RNA splicing less efficient than in healthy individuals. As a result, errors occur during RNA splicing that the cell cannot correct, impairing its function – especially in the nervous system.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_44a7e2ef17.jpg" alt="CEITEC/Blažek Lab: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Interaction between SF3B1 and SNIP1 proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_44a7e2ef17.jpg 156w," sizes="100vw" width="1600" height="1600"><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_2_85826d711e.jpg" alt="CEITEC/Blažek Lab: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: The effect of mutations in SNIP1 on cell proliferation." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_2_85826d711e.jpg 235w," sizes="100vw" width="1600" height="1067">The researchers were thus able to clarify the cause of this rare neurodevelopmental disorder. “Additionally, the cause of this disease also confirms the correctness of the checkpoint we described. It shows that even a small change in one of the proteins involved can disrupt the RNA splicing mechanism on which the cell depends,” adds group leader <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/dalibor-blazek-ph-d/u25918">Dalibor Blažek</a>.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_3_f95cfd68eb.jpeg" alt="CEITEC/Martin Indruch: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Dalibor Blažek." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_3_f95cfd68eb.jpeg 235w," sizes="100vw" width="1600" height="1067">Although the study focuses on basic research, its implications are broader. It suggests that the same mechanism may also play a role in regulating cell division – a process that is often disrupted in cancer.<blockquote>The research was carried out by scientists from CEITEC Masaryk University in collaboration with researchers from Spain and Germany. The study was published in the journal <a target="_blank" rel="noopener noreferrer" href="https://www.nature.com/articles/s41467-026-71119-2">Nature Communications</a>.</blockquote>

A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism

This study investigates the pathogenesis of neurosyphilis through cerebrospinal fluid proteomics using LC–MS/MS and ELISA validation. Comparative analysis identified 234 differentially expressed proteins, with major alterations linked to lysosomal dysfunction, axon guidance, and neurodegeneration pathways.Key lysosomal proteins, including PSAP and DNASE2, together with the axonal protein EPHA4, were significantly downregulated in neurosyphilis patients. These proteins showed potential as biomarkers for neurodegeneration and may provide new insights into disease mechanisms, diagnostics, and therapeutic targets.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689">Cerebrospinal Fluid Proteome Reveals Dysregulation of Lysosomal and Axonal Proteins in Neurosyphilis</a></h4>Huayang Tang*, Junjie Hu, Yifan Wu, Jinping Gao, Wenjun Wang, Xiaodong Zheng, Ran Zhang, Bo Liang, Fusheng Zhou, Ze Guo*J. Proteome Res. 2026, 25, 2, 713–722<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.jproteome.5c00689">https://doi.org/10.1021/acs.jproteome.5c00689</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.<div>Neurosyphilis (NS) is a group of clinical syndromes characterized by neuroinflammation caused by Treponema pallidum (T. pallidum), which occurs in all stages of syphilis. <a href="javascript:void(0);">(1,2)</a> NS is classified based on clinical presentation as either asymptomatic (ANS) or symptomatic (SNS), and based on disease stage as either early (occurring 1–2 years after primary infection) or late. <a href="javascript:void(0);">(1)</a> T. pallidum can cause local nonspecific and central nervous system (CNS) inflammation, leading to possible degenerative changes. <a href="javascript:void(0);">(3)</a> The immune response of CNS in neurosyphilis is comparable to that observed in other neuroinflammatory diseases. Consequently, the presence of neurological symptoms may not reliably indicate active CNS inflammation in syphilis patients. <a href="javascript:void(0);">(3)</a> A cerebrospinal fluid (CSF) proteomic study identified three biomarkers (SEMA7A, SERPINA3, and ITIH4) that contribute to NS and have potential implications for diagnosis and therapeutic strategies. <a href="javascript:void(0);">(4)</a> Through integrated proteomics and single-cell transcriptomics analyses, Toll-like/NF-κB signaling was identified as the key pathway involved in CNS damage caused by T. pallidum. <a href="javascript:void(0);">(5)</a> Despite an increasing understanding of the biomarkers and possible neuroinflammatory damage mechanisms of neurosyphilis, the mechanisms of neurodegeneration caused by T. pallidum infection remain elusive. <a href="javascript:void(0);">(6)</a>Patients with neurosyphilis exhibit stage-specific profiles of soluble factors in their CSF, which are linked to both immune status and the extent of neuronal damage. <a href="javascript:void(0);">(7)</a> In this study, we analyzed differentially expressed proteins (DEPs) in the CSF proteomes from 28 individuals, including neurosyphilis (NS), suspected neurosyphilis (spNS) and non-neurosyphilis (nNS) individuals, by LC–MS/MS and analyzed a public data set of the neurosyphilis CSF proteome. Validation was then performed by ELISA in an independent group comprising 110 samples. The results revealed that neuroinflammation by T. pallidum infection results in dysregulation of the key proteins in lysosomal and axonal pathway, which suggesting a potential contribution to neurodegeneration in neurosyphilis.<h4>Materials and Methods</h4><h5>LC–MS/MS</h5>The tryptic peptides were dissolved in 0.1% formic acid (solvent A) and loaded onto a custom-made reversed-phase column (15 cm × 75 μm). Using an EASY-nLC 1000 UPLC system, a gradient was run at 400 nL/min as follows: 6% to 23% solvent B (0.1% formic acid in 98% acetonitrile) over 26 min, 23% to 35% in 8 min, up to 80% in 3 min, and held at 80% for 3 min. Peptides were ionized via an NSI source at 2.0 kV and analyzed online by a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/559">Q Exactive Plus mass spectrometer</a>. Full scans (m/z 350–1800) were acquired in the Orbitrap at 70,000 resolution. The top precursors were selected for MS/MS with an NCE of 28, and fragments were detected at 17,500 resolution. A data-dependent method cycled between one MS scan and 20 MS/MS scans with a 15.0 s dynamic exclusion. AGC was set at 5E4. MS/MS data were processed with MaxQuant (v.1.5.2.8) using Trypsin/P as the enzyme (up to 2 missed cleavages). Precursor mass tolerance was 20 ppm (first search) and 5 ppm (main search); fragment mass tolerance was 0.02 Da. Fixed modification: carbamidomethyl (C); variable modification: oxidation (M). The FDR threshold was &lt;1%, and the minimum peptide score was &gt;40.<h5>ELISA</h5>CSF levels of host proteins were quantified using commercial ELISA kits according to the manufacturers’ protocols. Proteins analyzed included PSAP (OKEH07124, Aviva, USA), CTSL (abx150963, Abbexa, UK), NPC2 (A-QEK07857, Biogradetech, USA), and DNASE2 (abx386953, Abbexa, UK). Briefly, 100 μL of CSF was added to precoated plates and incubated at 37 °C for 2 h. After washing, 100 μL of detection antibody was added to each well and incubated at 37 °C for another 2 h. Following a wash, 100 μL of streptavidin-HRP working solution was added and incubated at room temperature for 20 min in the dark. The reaction was stopped with 50 μL of stop solution, and the optical density was measured at 450 nm.<h4>Results</h4><h5>Downregulation of Key Lysosomal Proteins in CSF from Patients With Neurosyphilis</h5>By analyzing the DEPs in NS vs nNS, we observed a significant enrichment of downregulated proteins in the lysosome pathway (P = 0.007) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>A), with 9 lysosomal proteins showing significant downregulation (Padj &lt; 0.05) in the NS group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S4</a>). To validate this finding, we examined the public CSF proteomics data set of neurosyphilis (PXD033034) and identified 18 proteins in the lysosomal pathway that were significantly downregulated in patients with NS (Padj &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S4</a>). PPI network analysis determined the top 10 hub genes within the lysosome pathway (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>B). A Venn diagram revealed 3 proteins (PSAP, CTSL, and NPC2) shared across our current data, the public data set (PXD033034) and the top 10 hub genes (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>C). The mass spectrometry results indicated that the levels of PSAP (Padj = 0.043), CTSL (Padj = 0.028) and NPC2 (Padj = 0.013) were significantly lower in the NS group compared to the nNS group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D). The PXD033034 data set revealed consistent changes in the PSAP, CTSL, and NPC2 levels in the NS group (Padj &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S1 and Table S4</a>). In addition, associations between the lysosomal protein DNASE2 and NS were observed in both the present study (Padj = 0.003) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D) and the PXD033034 data set (Padj &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S1 and Table S4</a>), with subgroup analysis revealing a significantly lower expression level of DNASE2 in the SNS group compared to the ANS group (P = 0.035) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D and <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S3</a>). Further validation by ELISA (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S5</a>) in an independent group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#tbl1">Table 1</a>) confirmed significantly downregulated CSF levels of PSAP (P &lt; 0.0001), CTSL (P &lt; 0.0001), NPC2 (P = 0.0024) and DNASE2 (P &lt; 0.0001) in patients with NS (n = 21) than in nNS individuals (n = 56) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>E) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S6</a>), as well as decreased in the SNS subgroup (P &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S2 and Table S6</a>). Receiver operating characteristic (ROC) curve analysis supported PSAP (AUC = 0.91, 95% CI: 0.83–0.99) and DNASE2 (AUC = 0.95, 95% CI: 0.91–0.99) for distinguishing NS from nNS and as potential biomarkers for assessing neurodegeneration in NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>F). These results indicate that T. pallidum infection may lead to lysosomal dysfunction in CNS.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/J_Proteome_Res_2026_25_2_713_722_Figure_2_Downregulation_of_key_lysosomal_proteins_in_the_cerebrospinal_fluid_of_neurosyphilis_patients_bbccd95f44.jpg" alt="J. Proteome Res. 2026, 25, 2, 713–722: Figure 2. Downregulation of key lysosomal proteins in the cerebrospinal fluid of neurosyphilis patients. (a) KEGG pathway analysis demonstrated that downregulated proteins in patients with NS were significantly enriched in the lysosome pathway, as well as in axon guidance and neurodegeneration. (b) The top 10 hub genes involved in the lysosome pathway were identified using the STRING network data set and PPI analysis. (c) A Venn diagram revealed 3 proteins (PSAP, CTSL, and NPC2) shared across our current data, the public data set (PXD033034) and the top 10 hub genes. (d) The CSF levels of PSAP (Padj = 0.043), CTSL (Padj = 0.028), DNASE2 (Padj = 0.003) and NPC2 (Padj = 0.013) were significantly decreased in the NS group than in the nNS group. Subgroup analysis found a significantly lower expression level of DNASE2 in the SNS group than in the ANS group (P = 0.035). (e) PSAP, DNASE2, CTSL and NPC2 levels in CSF were tested by ELISA in the nNS (n = 56) and NS (n = 21) groups. Compared with those in the nNS group, significantly lower PSAP (P &lt; 0.0001), CTSL (P &lt; 0.0001), DNASE2 (P &lt; 0.0001) and NPC2 (P = 0.0024) levels were detected in the NS group. (f) ROC curve analysis for NS revealed that PSAP had an AUC = 0.91 (95% CI: 0.83–0.99), DNASE2 had an AUC = 0.95 (95% CI: 0.91–0.99), CTSL had an AUC = 0.85 (95% CI: 0.76–0.95), and NPC2 had an AUC = 0.72 (95% CI: 0.59–0.85). NS: neurosyphilis; nNS: non-neurosyphilis; ANS: asymptomatic neurosyphilis; SNS: symptomatic neurosyphilis. ROC: receiver operating characteristic; AUC: area under the curve. * P &lt; 0.05, ** P &lt; 0.01, ****P &lt; 0.0001." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_J_Proteome_Res_2026_25_2_713_722_Figure_2_Downregulation_of_key_lysosomal_proteins_in_the_cerebrospinal_fluid_of_neurosyphilis_patients_bbccd95f44.jpg 140w," sizes="100vw" width="2100" height="2339"><h5>Downregulation of Key Axonal Proteins Correlated with Lysosomal Protein Reduction in Neurosyphilis CSF</h5>Lysosomes play crucial roles in neuronal health by maintaining axonostasis. <a href="javascript:void(0);">(10)</a> The enrichment analysis indicated that the downregulated proteins in NS were implicated in the biological processes of axonostasis (such as axon development and axonogenesis) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig1">Figure 1</a>F) and the pathway of axon guidance (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>A). Our proteomic data revealed a total of 24 downregulated (Padj &lt; 0.05) axonal proteins and 1 upregulated (Padj &lt; 0.05) axonal protein in the CSF of patients with NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S9</a>). Furthermore, the PXD033034 data set revealed 55 downregulated (Padj &lt; 0.05) and 4 upregulated (Padj &lt; 0.05) axonal proteins in NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S9</a>). The top 10 hub genes involved in the biological processes of axon development and axonogenesis were identified by PPI network analysis (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>A). Considering the overlap of our current data, the PXD033034 data set and the top 10 hub genes (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>B), one key protein, EPHA4, was identified across 3 data sets, with significant downregulation in our current data (Padj = 0.011) and in the PXD033034 data set (Padj = 0.028) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>C). Correlation analysis further revealed a positive correlation between the levels of PSAP and EPHA4 (r = i 0.83, P &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>D). Reduced levels of PSAP and EPHA4 in CSF have been implicated in neurodegenerative diseases, including Alzheimer’s disease (AD) and Parkinson’s disease (PD). <a href="javascript:void(0);">(11,12)</a> Our findings suggest that coordinated dysregulation of lysosomal and axonal proteins may contribute to neurodegeneration in NS.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/J_Proteome_Res_2026_25_2_713_722_Figure_4_Key_axonal_protein_downregulated_in_CSF_from_patients_with_neurosyphilis_66f5533e94.jpg" alt="J. Proteome Res. 2026, 25, 2, 713–722: Figure 4. Key axonal protein downregulated in CSF from patients with neurosyphilis. (a) The top 10 hub genes involved in axonostasis were identified by the STRING network data set and PPI analysis. (b) A Venn diagram revealed 1 protein (EPHA4) shared across DEPs related to axonostasis in our current data and in the public data set (PXD033034) and the top 10 hub genes. (c) EPHA4 was significantly downregulated both in our present study (Padj = 0.011) and in the PXD033034 data set (Padj = 0.028). (d) Correlation analysis demonstrated that the EPHA4 level was significantly positively correlated (P &lt; 0.05) with the levels of PSAP (r = 0.83), CTSL (r = 0.6), NPC2 (r = 0.69), DNASE2 (r = 0.61) and SEMA7A (r = 0.83). NS: neurosyphilis; nNS: non-neurosyphilis. * P &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_J_Proteome_Res_2026_25_2_713_722_Figure_4_Key_axonal_protein_downregulated_in_CSF_from_patients_with_neurosyphilis_66f5533e94.jpg 178w," sizes="100vw" width="1250" height="1096"><h4>Conclusions</h4>The present study reveals the associations of dysregulated proteins in lysosomal and axonal pathways with neurosyphilis, and potential evidence of shared pathophysiological mechanisms between neuroinflammation caused by T. pallidum infection and neurodegenerative diseases.However, this study has certain limitations. First, the use of ELISA to validate a limited number of proteins has certain limitations, such as the inherent cross-reactivity of ELISA. In the future, we can optimize the validation experiments by adding techniques such as Western blotting for verification. Second, this study uses a cross-sectional sampling method for research, which limits our ability to infer disease progression and treatment responses. In the future, we will conduct follow-up on the subjects, continue collecting cerebrospinal fluid samples after treatment, and observe whether the protein dysregulation is reversible after treatment. For spNS patients, follow-up should also be conducted to determine if they have transformed into NS, which will be very valuable for validating the predictive utility of our biomarkers. Finally, although multiple discovery and validation cohort studies have been conducted, we currently lack direct mechanistic evidence. Future work will investigate whether exposing neural cell coculture models to outer-membrane antigens of T. pallidum reproduces the lysosome and axon alterations observed in CSF, clarifying their role in neural damage of neurosyphilis and potential biomarkers for diagnosis and treatment of neurodegeneration in neurosyphilis.</div>

Cerebrospinal Fluid Proteome Reveals Dysregulation of Lysosomal and Axonal Proteins in Neurosyphilis

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Phenomenex Biozen SEC-3 LC columns

High inertness and particle consistency of both Biozen™ SEC columns drives greater reproducibility from injection-to-injection. 

High inertness and particle consistency of both Biozen™ SEC columns drives greater reproducibility from injection-to-injection. Combine this with the bioinert BioTi hardware and good aggregate recovery is no longer something that you’re missing out on.Biozen SEC columns provide:<ul><li>High efficiency on both HPLC and UHPLC</li><li>Extreme inertness and robustness</li><li>Finely tuned high and low MS separation windows</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Biozen_SEC_3_3a6e232271.webp" alt="Phenomenex: Biozen SEC-3" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Biozen_SEC_3_3a6e232271.webp 245w," sizes="100vw" width="500" height="150"><ul><li>Separation Mode: Gel Filtration Chromatography (GFC)</li><li>Particle Size: 1.8</li><li>Recommended Use: High molecular weight (HMW) separation range of 10 k – 700 kDa</li></ul><h3>Phenomenex Biozen Biologics LC Columns</h3>With a new titanium BioTi™ biocompatible hardware to minimize priming, four particle platforms for optimal versatility and nine particle chemistries to maximize selectivity and sensitivity, Biozen UHPLC/HPLC columns for protein analysis are seamlessly designed to bring peace of mind to your analysis of biologics through:<ul><li>Charge Variant Analysis</li><li>Aggregate Analysis</li><li>Peptide Mapping</li><li>Intact Mass Analysis</li><li>Intact and Subunit Analysis</li><li>Glycan Analysis</li><li>Peptide Quantitation</li><li>Drug Antibody Ratio (DAR)</li><li>Oligonucleotide Characterization</li></ul><h3>Biocompatible Flow Path with BioTi™ Hardware</h3>Keep your mind at ease knowing that we’ve minimized the need for priming with a new titanium infused biocompatible hardware and frit that doesn’t interfere with protein or peptide integrity!<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Bio_Ti_Hardware_991fb53395.jpg" alt="Phenomenex: BioTi Hardware" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Bio_Ti_Hardware_991fb53395.jpg 245w," sizes="100vw" width="1378" height="426"><h3>4 Advanced Particle Platforms</h3>All four of the Biozen particle platforms were individually designed and built by Phenomenex to take advantage of integral levels of performance, ruggedness, and reproducibility for protein characterization applications. Individually, each platform differs in the proprietary processing techniques used to control particle size and morphology.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg" alt="Phenomenex: Advanced Particle Platforms" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg 245w," sizes="100vw" width="1439" height="868">

Phenomenex Biozen SEC-2 LC columns

Biozen SEC columns are extremely inert, high density fully porous particle with high efficiency and low molecular weight separation range.

Biozen SEC columns are extremely inert, high density fully porous particle with high efficiency and low molecular weight (LMW) separation range of 1 k – 450 kDa.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Biozen_SEC_3_3a6e232271.webp" alt="Phenomenex: Biozen SEC-2" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Biozen_SEC_3_3a6e232271.webp 245w," sizes="100vw" width="500" height="150"><ul><li>Separation Mode: Gel Filtration Chromatography (GFC)</li><li>Particle Size: 1.8</li><li>Recommended Use: Low molecular weight (LMW) separation range of 1 k – 450 kDa</li></ul><h3>Phenomenex Biozen Biologics LC Columns</h3>With a new titanium BioTi™ biocompatible hardware to minimize priming, four particle platforms for optimal versatility and nine particle chemistries to maximize selectivity and sensitivity, Biozen UHPLC/HPLC columns for protein analysis are seamlessly designed to bring peace of mind to your analysis of biologics through:<ul><li>Charge Variant Analysis</li><li>Aggregate Analysis</li><li>Peptide Mapping</li><li>Intact Mass Analysis</li><li>Intact and Subunit Analysis</li><li>Glycan Analysis</li><li>Peptide Quantitation</li><li>Drug Antibody Ratio (DAR)</li><li>Oligonucleotide Characterization</li></ul><h3>Biocompatible Flow Path with BioTi™ Hardware</h3>Keep your mind at ease knowing that we’ve minimized the need for priming with a new titanium infused biocompatible hardware and frit that doesn’t interfere with protein or peptide integrity!<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Bio_Ti_Hardware_991fb53395.jpg" alt="Phenomenex: BioTi Hardware" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Bio_Ti_Hardware_991fb53395.jpg 245w," sizes="100vw" width="1378" height="426"><h3>4 Advanced Particle Platforms</h3>All four of the Biozen particle platforms were individually designed and built by Phenomenex to take advantage of integral levels of performance, ruggedness, and reproducibility for protein characterization applications. Individually, each platform differs in the proprietary processing techniques used to control particle size and morphology.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg" alt="Phenomenex: Advanced Particle Platforms" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg 245w," sizes="100vw" width="1439" height="868">

Phenomenex Biozen dSEC-2 LC columns

Biozen dSEC columns use low-pore silica with a proprietary hydrophilic diol bond to prevent silica-protein interactions.

Advanced SEC Silica Particle Technology and Surface Chemistry for Characterizing BiomoleculesThe Biozen dSEC columns are packed with low pore volume silica coupled with a proprietary hydrophilic diol-type bonded surface chemistry that prevents the silica surface from interacting with protein samples.<ul><li>Exceptionally Robust, Pore Controlled SEC Particle</li><li>Extreme Stability and Exceptional Lifetime</li><li>Reproducible Separations</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Biozen_dsec_63af9af237.webp" alt="Phenomenex: Biozen-dSEC-2" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Biozen_dsec_63af9af237.webp 245w," sizes="100vw" width="500" height="150"><ul><li>Separation Mode: Gel Filtration Chromatography (GFC)</li><li>Pore size: 200</li><li>Particle Size: 1.8, 3</li><li>Recommended Use: Analysis of monoclonal antibodies, biosimilars and other biomolecules by using specific molecular weights with improved column lifetimes and recovery</li></ul><h4>Biozen SEC Proprietary Silica Particle Technology</h4>The Biozen dSEC columns are packed with low pore volume silica coupled with a proprietary hydrophilic diol-type bonded surface chemistry that prevents the silica surface from interacting with protein samples.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Biozen_SEC_Proprietary_Silica_Particle_Technology_502218b910.jpg" alt="Phenomenex: Biozen SEC Proprietary Silica Particle Technology" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Biozen_SEC_Proprietary_Silica_Particle_Technology_502218b910.jpg 245w," sizes="100vw" width="1448" height="469"><h4>Improved Column Lifetime and Performance Stability</h4>Phenomenex’s optimized SEC column loading technology has significantly improved the overall packing density and silica distribution of the columns leading to improved chromatographic lifetime and stability.<h4>New Standard for Platform SEC Methods</h4>Whether IgG2 or IgG4 isotypes, bispecifics, or Fc-Fusions, dSEC-2 provides excellent separation and sample recovery for many different classes of antibodies and related recombinant proteins.<h3>Phenomenex Biozen Biologics LC Columns</h3>With a new titanium BioTi™ biocompatible hardware to minimize priming, four particle platforms for optimal versatility and nine particle chemistries to maximize selectivity and sensitivity, Biozen UHPLC/HPLC columns for protein analysis are seamlessly designed to bring peace of mind to your analysis of biologics through:<ul><li>Charge Variant Analysis</li><li>Aggregate Analysis</li><li>Peptide Mapping</li><li>Intact Mass Analysis</li><li>Intact and Subunit Analysis</li><li>Glycan Analysis</li><li>Peptide Quantitation</li><li>Drug Antibody Ratio (DAR)</li><li>Oligonucleotide Characterization</li></ul><h3>Biocompatible Flow Path with BioTi™ Hardware</h3>Keep your mind at ease knowing that we’ve minimized the need for priming with a new titanium infused biocompatible hardware and frit that doesn’t interfere with protein or peptide integrity!<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Bio_Ti_Hardware_991fb53395.jpg" alt="Phenomenex: BioTi Hardware" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Bio_Ti_Hardware_991fb53395.jpg 245w," sizes="100vw" width="1378" height="426"><h3>4 Advanced Particle Platforms</h3>All four of the Biozen particle platforms were individually designed and built by Phenomenex to take advantage of integral levels of performance, ruggedness, and reproducibility for protein characterization applications. Individually, each platform differs in the proprietary processing techniques used to control particle size and morphology.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg" alt="Phenomenex: Advanced Particle Platforms" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg 245w," sizes="100vw" width="1439" height="868">

Phenomenex Biozen dSEC-7 LC columns

dSEC-7 optimizes dimensions to save sample, speed up runs, and enhance resolution for AAVs and large biomolecule separations.

AAV and Large Biomolecule Aggregate Analysis​Biozen dSEC-7 columns are packed with 700 Å large pore silica coupled with a proprietary hydrophilic diol-type bonded surface chemistry that ensures silica surface interactions are mitigated. Designed with optimized column dimensions, dSEC-7 conserves valuable sample consumption, facilitates faster run times, and maximizes resolution for AAVs and large biomolecule separations.Robust and reliable aggregate analysis:<ul><li>Baseline resolution of monomer/aggregate species through 700 Å pore size</li><li>Reduction in sample consumption by up to 90 % compared to traditional SEC columns</li><li>Reduction in method times by up to 50 % when compared to traditional SEC columns</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Biozen_dsec_63af9af237.webp" alt="Phenomenex: Biozen-dSEC-7" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Biozen_dsec_63af9af237.webp 245w," sizes="100vw" width="500" height="150"><ul><li>Separation Mode: Gel Filtration Chromatography (GFC)</li><li>Pore size: 700</li><li>Recommended Use: Aggregate analysis of AAVs and other large biomolecules using specific molecular weights that conserves sample consumption, facilitates faster run times, and maximizes resolution.</li></ul><h4>An SEC Column for AAV Aggregate Analysis</h4><figure class="image"><img style="aspect-ratio:668/575;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Biozen_d_SEC_7_Column_b307c4217d.jpg" alt="Phenomenex: Biozen dSEC-7 Column" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Biozen_d_SEC_7_Column_b307c4217d.jpg 182w," sizes="100vw" width="668" height="575"></figure><h4>Biozen dSEC-7 Features</h4><h5>Improved Loading</h5><ul><li>dSEC-7 addresses the challenge of aggregate analysis by offering accurate detection and separation with injections as low as 0.5 µL. Unlike traditional methods that demand large sample volumes, dSEC-7 conserves valuable samples, allowing for replicate analyses and ensuring availability for other CQA tests.</li></ul><h5>Mobile Phase Flexibility</h5><ul><li>dSEC-7’s particle properties facilitate robust separation of monomer from aggregate species, regardless of which mobile phase best suits your sample. This ensures reproducible results while accommodating unique sample demands, easing the burden of method condition optimization during development.</li></ul><h5>Serotype Versatility</h5><ul><li>With its robust performance and 700 Å pore size, dSEC-7 effectively resolves monomer from aggregate peaks across various AAV serotypes. This capability is crucial for evaluating appropriate serotype candidates, each varying in its unique tissue and cell tropisms, to ensure desired therapeutic outcomes are achieved.</li></ul><h5>Instrument Agnostic Performance</h5><ul><li>Despite differences in dwell volume and dispersion across various sites and departments, dSEC-7 consistently delivers robust and reproducible performance across commercially available LC instrumentation. This ensures reliable results regardless of variations in equipment, setup, or location.</li></ul><h5>Outperforms Trending Solutions</h5><ul><li>dSEC-7 excels in providing superior resolution over market alternatives, particularly when characterizing higher-level aggregates in AAV analysis. Unlike current market solutions with insufficient particle pore size, dSEC-7 ensures accurate and reproducible separation of AAV monomer from aggregates.</li></ul><h5>Enhanced Detector Flexibility</h5><ul><li>Conquer sample limitations using SEC-FLR for heightened sensitivity, SEC-MALS for precise molecular weight determination, or SEC-UV for routine analysis. Achieving comprehensive AAV characterization insights by transferring methods across detector technologies with unique benefits is now seamless.</li></ul><h3>Phenomenex Biozen Biologics LC Columns</h3>With a new titanium BioTi™ biocompatible hardware to minimize priming, four particle platforms for optimal versatility and nine particle chemistries to maximize selectivity and sensitivity, Biozen UHPLC/HPLC columns for protein analysis are seamlessly designed to bring peace of mind to your analysis of biologics through:<ul><li>Charge Variant Analysis</li><li>Aggregate Analysis</li><li>Peptide Mapping</li><li>Intact Mass Analysis</li><li>Intact and Subunit Analysis</li><li>Glycan Analysis</li><li>Peptide Quantitation</li><li>Drug Antibody Ratio (DAR)</li><li>Oligonucleotide Characterization</li></ul><h3>Biocompatible Flow Path with BioTi™ Hardware</h3>Keep your mind at ease knowing that we’ve minimized the need for priming with a new titanium infused biocompatible hardware and frit that doesn’t interfere with protein or peptide integrity!<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Bio_Ti_Hardware_991fb53395.jpg" alt="Phenomenex: BioTi Hardware" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Bio_Ti_Hardware_991fb53395.jpg 245w," sizes="100vw" width="1378" height="426"><h3>4 Advanced Particle Platforms</h3>All four of the Biozen particle platforms were individually designed and built by Phenomenex to take advantage of integral levels of performance, ruggedness, and reproducibility for protein characterization applications. Individually, each platform differs in the proprietary processing techniques used to control particle size and morphology.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg" alt="Phenomenex: Advanced Particle Platforms" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg 245w," sizes="100vw" width="1439" height="868">

Phenomenex Biozen dSEC-1 LC columns

Phenomenex Biozen dSEC-1 is a high-resolution SEC column for peptide therapeutics, delivering fast, reproducible aggregate analysis with improved peak shape and compatibility with SEC-MS and SEC-MALS.

<h4>High-Resolution Aggregate Analysis for Peptide Therapeutics</h4>Biozen dSEC-1 columns are engineered to meet the growing demand for aggregate analysis in peptide therapeutics and mid-sized biologics. Packed with 90 Å small pore silica and featuring inert diol-based surface chemistry, dSEC-1 delivers enhanced resolution for low and high molecular weight peptide aggregates. Its robust design ensures reproducibility and compatibility with advanced workflows like SEC-MS and SEC-MALS.<h5>Robust Performance for Peptide Aggregate Analysis</h5><ul><li>High resolution for low/high MW peptide aggregates (1–50 kDa)</li><li>Reproducible, and fast analysis with extended column lifetime</li><li>Improved peak asymmetry by up to 40%</li><li>Recommended Use: Analysis of peptides, protein fragments, and small biologics with reduced analysis times and improved column lifetimes.</li></ul><h4>Aggregate and Monomer Separation in Liraglutide Formulations</h4><ul><li>Baseline resolution of monomer and two aggregates achieved in under 10 minutes</li><li>Exceptional reproducibility with retention time RSD ≤ 0.08% and peak area RSD ≤ 0.01%</li><li>Clear detection at low levels with S/N ratios of 13, 75, and 10,917 for aggregates and monomer</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_separation_in_liraglutide_formulations_3_b0d97cd01f.jpg" alt="Phenomenex: Aggregate and Monomer Separation in Liraglutide Formulations" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_separation_in_liraglutide_formulations_3_b0d97cd01f.jpg 245w," sizes="100vw" width="938" height="307"><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_separation_in_liraglutide_formulations_2_035bfea3bc.jpg" alt="Phenomenex: Aggregate and Monomer Separation in Liraglutide Formulations" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_separation_in_liraglutide_formulations_2_035bfea3bc.jpg 245w," sizes="100vw" width="1700" height="1050"><h3>Biozen SEC Proprietary Silica Particle Technology</h3>The Biozen dSEC columns are packed with low pore volume silica coupled with a proprietary hydrophilic diol-type bonded surface chemistry that prevents the silica surface from interacting with protein samples.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Biozen_SEC_Proprietary_Silica_Particle_Technology_502218b910.jpg" alt="Phenomenex: Biozen SEC Proprietary Silica Particle Technology" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Biozen_SEC_Proprietary_Silica_Particle_Technology_502218b910.jpg 245w," sizes="100vw" width="1448" height="469"><h4>Improved Column Lifetime and Performance Stability</h4>Phenomenex’s optimized SEC column loading technology has significantly improved the overall packing density and silica distribution of the columns leading to improved chromatographic lifetime and stability.<h4>New Standard for Platform SEC Methods</h4>Whether IgG2 or IgG4 isotypes, bispecifics, or Fc-Fusions, dSEC-2 provides excellent separation and sample recovery for many different classes of antibodies and related recombinant proteins.<h3>Phenomenex Biozen Biologics LC Columns</h3>With a new titanium BioTi™ biocompatible hardware to minimize priming, four particle platforms for optimal versatility and nine particle chemistries to maximize selectivity and sensitivity, Biozen UHPLC/HPLC columns for protein analysis are seamlessly designed to bring peace of mind to your analysis of biologics through:<ul><li>Charge Variant Analysis</li><li>Aggregate Analysis</li><li>Peptide Mapping</li><li>Intact Mass Analysis</li><li>Intact and Subunit Analysis</li><li>Glycan Analysis</li><li>Peptide Quantitation</li><li>Drug Antibody Ratio (DAR)</li><li>Oligonucleotide Characterization</li></ul><h3>Biocompatible Flow Path with BioTi™ Hardware</h3>Keep your mind at ease knowing that we’ve minimized the need for priming with a new titanium infused biocompatible hardware and frit that doesn’t interfere with protein or peptide integrity!<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Bio_Ti_Hardware_991fb53395.jpg" alt="Phenomenex: BioTi Hardware" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Bio_Ti_Hardware_991fb53395.jpg 245w," sizes="100vw" width="1378" height="426"><h3>4 Advanced Particle Platforms</h3>All four of the Biozen particle platforms were individually designed and built by Phenomenex to take advantage of integral levels of performance, ruggedness, and reproducibility for protein characterization applications. Individually, each platform differs in the proprietary processing techniques used to control particle size and morphology.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg" alt="Phenomenex: Advanced Particle Platforms" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Advanced_Particle_Platforms_a0959aca03.jpg 245w," sizes="100vw" width="1439" height="868">

Products from category GPC/SEC HPLC columns from Phenomenex - page 1

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