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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KNAUER HPLC, UHPLC, preparative HPLC and GPC columns

 KNAUER offers about 6,000 columns for analytical HPLC and UHPLC applications as well as for purification tasks in the preparative scale. 

Columns for analytical HPLC, UHPLC, preparative HPLC and GPCIn the field of analytical HPLC columns we can offer a solution for nearly any analytical separation task. KNAUER offers about 6,000 columns for analytical HPLC and UHPLC applications as well as for purification tasks in the preparative scale.<h3>Which column do you need?</h3><h4>(U)HPLC of small molecules</h4>Silica gel based KNAUER columns for HPLC and UHPLC in the most often used separation modes:&nbsp;<ul><li>Reversed Phase (RP)</li><li>Normal Phase (NP)</li><li>Hydrophilic Interaction Liquid Chromatography (HILIC)</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_LC_Columns_1_b84b390b6b.jpg" alt="Knauer: LC RP Columns " srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_LC_Columns_1_b84b390b6b.jpg 245w," sizes="100vw" width="779" height="466"><h4>Enantioseparation of racemates</h4>Chiral HPLC columns - Available in a wide range of dimensions for analytical, preparative and SMB (simulated moving bed) applications, Eurospher II Chiral columns are the perfect choice for even the most challenging enantioseparation tasks.As chiral separations are not very well predictable, KNAUER offers a chiral screening service for your Samples.&nbsp;<h4>HPLC of sugars, organic acids and alcohols</h4>Ion exclusion and ligand exchange columns - Based on a sulfonated cross-linked styrenedivinylbenzene copolymer and available in several ionic forms (H, Ca, Pb and Ag). This particular cation exchanger is characterized by an outstanding density of functional groups, making it the ideal choice for your ion exclusion, size exclusion and ligand exchange chromatography.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_LC_Columns_4_with_precolumn_short_aaee66b110.jpg" alt="Knauer: LC Columns - 4 with precolumn-short" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_LC_Columns_4_with_precolumn_short_aaee66b110.jpg 245w," sizes="100vw" width="1330" height="580"><h4>HPLC of Biomolecules</h4>Analytical wide pore HPLC columns - The use of larger pore silica-based bonded phases leads to improvements in resolution, capacity and recovery of proteins and other biomolecules, due to a reduction in size exclusion mechanism and enhanced molecular diffusion rates. A pore size of 300 Å has become the accepted standard for wide pore silica gels because it has been found to be suitable for a broad range of molecular weight proteins, peptides and oligonucleotides. In general, peptides exceeding approximately 50 amino acids and oligonucleotides greater than 25 residues are preferentially analyzed on 300 Å materials.<h4>GPC/SEC columns</h4><ul><li>AppliChrom® GPC/SEC columns for biopolymers and aqueous&nbsp;polymers</li><li>AppliChrom® GPC columns for GPC analysis of organic molecules using THF, toluene, chloroform</li><li>AppliChrom GPC columns for GPC analysis organic (DMAc or DMF)</li><li>Optimized for DMSO-GPC applications</li><li>Special GPC/SEC-columns for aqueous analysis of neutral, anionic and additional cationic polymers</li></ul><h4>Preparative HPLC Column hardware</h4>Preparative HPLC columns can be offered with two different hardware types:<ul><li>Versatile standard flanged hardware for nearly any application task in batch chromatography</li><li>dAX Hardware with static and dynamic axial compression for an extended lifetime and multi-column chromatography like SMB processes</li></ul><h4>Analytical HPLC Column hardware</h4>Available analytical HPLC column dimensions - Analytical KNAUER columns with ID 3, 4 and 4.6 mm are available with and without integrated precolumn.Every KNAUER column is tested separately to guarantee highest quality. We highly recommend using a precolumn to protect the valuable main column and extend the lifetime significantly.&nbsp;Afraid that a precolumn adds volume to your system and deteriorates your results?KNAUER columns that are delivered with an integrated precolumn are also tested in this configuration so that the user can be sure about the function and quality. The same quality standards as for columns without integrated precolumn apply. KNAUER guarantees that there is no loss in performance when a precolumn is integrated properly.Exchanging the precolumn is very easy! Klick the button below to get an instruction.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_LC_Columns_available_dimensions_chart_0c73a3271d.jpg" alt="Knauer: LC Columns - available dimensions chart" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_LC_Columns_available_dimensions_chart_0c73a3271d.jpg 218w," sizes="100vw" width="755" height="541"><h4>FPLC columns</h4>Agarose nad dextran-based FPLC columns fo protein prurificationHigh-quality FPLC columns to reach your purification goal - KNAUER Sepapure® FPLC columns&nbsp;Sepapure® FPLC columns and resins for all common protein purification tasks: size exclusion chromatography (SEC), affinity chromatography (AC) and ion-exchange chromatography (IEX)<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_LC_Columns_SEPAPURE_Q_FF_2f1fef3613.jpg" alt="Knauer: LC Columns - SEPAPURE Q FF" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_LC_Columns_SEPAPURE_Q_FF_2f1fef3613.jpg 240w," sizes="100vw" width="947" height="616"><h3>KNAUER LC column brands</h3><h4>Eurospher I</h4><ul><li>HPLC columns for every day</li><li>Suited for a wide range of analytical, semi-preparative and process scale separations in normal phase and reversed phase mode.</li></ul><h4>Eurospher II:&nbsp;</h4><ul><li>Advanced HPLC / UHPLC columns</li><li>Eurospher II is introduced as the new workhorse for an even wider range of application areas, suitable for analytical, semi-preparative and process-scale separations.</li><li>The logical choice to take on routine analyses as well as the most ambitious chromatoraphy tasks.</li></ul><h4>Eurospher II Chiral</h4><ul><li>Enantioseparation of racemates</li><li>The chiral stationary phases (CSPs) of KNAUER’s Eurospher® II Chiral HPLC columns were designed to tackle a wide range of chiral separation tasks.</li></ul><h4>Eurosil Bioselect</h4><ul><li>HPLC columns for bioanalytics</li><li>Eurosil Bioselect columns feature a wide-pore stationary phase and were specifically designed to separate large biomolecules such as proteins and peptides.</li></ul><h4>Eurokat</h4><ul><li>HPLC columns for food analysis</li><li>Eurokat columns are valuable for food analysis and especially developed for the separation of organic acids, carbonhydrates, alcohols and even complex mixtures of these compounds.</li></ul>

KNAUER Eurospher II 100 NH2 (U)HPLC Columns for NP & HILIC (USP L8)

Amino (NH2) bonded silica gel phases can be used in the normal phase (NP) and HILIC mode, but also for reversed phase (RP) mode.

Amino columns for Normal Phase and for HILIC applications (USP L8)Amino (NH2) bonded silica gel phases can be used in the normal phase (NP) and HILIC mode, but also for reversed phase (RP) mode. They show alternative normal phase selectivity to unbonded silica, especially for aromatics. Furthermore, the selectivity is influenced by hydrogen bond interactions with the analyte. Amino columns can also be used in the HILIC mode for carbohydrate analysis and for other polar compounds. Their weak anion-exchange properties can be used in the analysis of anions and organic acids.The amino group is bonded to the silica support via a propyl linker.<h5>Properties</h5><ul><li>Separation mechanism: Hydrophilic and ionic interactions</li><li>Ultra pure, spherical high performance HPLC phase based on silica gel</li><li>Amino modification (Aminopropyl)</li><li>4 % carbon content (without endcapping)</li></ul><h5>Key features</h5><ul><li>Multi mode column for RP, NP, HILIC and IC, Aminopropyl modification without endcapping, outstanding mechanical and chemical stability.</li></ul><h5>Recommended application areas</h5><ul><li>Most flexible phase in the Eurospher II family; can be used in three modes: normal phase, reversed phase and ion chromatography mode (weak anion exchanger); different selectivity to the silica packing; in reversed phase mode mainly used for analysis of carbohydrates.&nbsp;</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_NH_2_HILIC_NP_fbaa6027c0.webp" alt="KNAUER: NH2" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_NH_2_HILIC_NP_fbaa6027c0.webp 107w," sizes="100vw" width="290" height="421"><blockquote>Tip: A precolumn can help to protect your analytical column. Especially when working with highly matrix afflicted samples it is highly recommended to use precolumns.</blockquote>Stationary phase Eurospher II 100 NH2 is provided in these column types: analytical, semi-preparative and preparative.Eurospher II 100 NH2 Analytical Columns are available with these parameters:<ul><li>Column length (mm): 50, 100, 150, 250</li><li>Column ID (mm): 3, 4, 4.6</li><li>Particle size (µm): 3, 5</li></ul>Eurospher II 100 NH2 Semi-Preparative Standard Columns are available with these parameters:<ul><li>Column length (mm): 30, 50, 125, 150, 250</li><li>Column ID (mm): 8, 16</li><li>Particle size (µm): 5, 10</li></ul><h3>KNAUER (U)HPLC Columns</h3>Widest range of HPLC and UHPLC columns for all separation modes and applications.<ul><li>Safe Investment: Robust and reliable columns for attractive price&nbsp;</li><li>Separation Mode: Reversed Phase, HILIC, Normale</li><li>Simplicity: Easy purchase via our online store with fast delivery</li><li>Application: All-rounder for research or highly specialised for high-throughput analysis? We have the best column for your requirements.</li><li>Flexibility: Wide selection of column and particle sizes, for (U)HPLC applications up to 1000 bar</li></ul>KNAUER offers the perfect column for any small molecule separation. No matter which separation mode, molecule and the mobile phase, we offer a suitable (U)HPLC stationary phase. Choose from a wide range of modifications, particle sizes and column dimensions to suit your application. To elongate the lifetime of your column, you can choose to use a suitable precolumn.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_KNAUER_U_HPLC_C8_and_C8_A_Columns_083c60f401.webp" alt="KNAUER: KNAUER (U)HPLC Columns" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_KNAUER_U_HPLC_C8_and_C8_A_Columns_083c60f401.webp 182w," sizes="100vw" width="787" height="674">

KNAUER Eurospher II 100 Si (U)HPLC Columns for NP & HILIC (USP L3)

Unmodified Silica gel materials were the first ones used for chromatography. This is the reason the mode is called "normal phase" (NP).

Si columns for Normal Phase and HILIC applications (USP L3)Unmodified Silica gel materials were the first ones used for chromatography. This is the reason the mode is called "normal phase" (NP). They are still used in HPLC, although reversed phase (RP) is by far the most often used HPLC mode today.<h5>A wide range of porous Si materials are available, characterized by:</h5><ul><li>Surface area</li><li>Pore size</li><li>Particle size</li><li>Purity</li><li>Metal content</li></ul><h5>Properties</h5><ul><li>Separation mechanism: Hydrophilic interactions</li><li>Ultra pure, spherical high performance HPLC phase based on silica gel</li><li>No modification, no endcapping, with 0 % carbon content</li></ul><h5>Key features</h5><ul><li>High-class HPLC phase perfectly suited to take on routine analyses as well as the most ambitious chromatography tasks, outstanding mechanical and chemical stability.</li></ul><h5>Recommended application areas</h5><ul><li>Wide range of different applications, i.e. SEC (size exclusion chromatography) but also for normal phase HPLC and HILIC; good choice for analytical and preparative purposes to separate polar compounds.</li></ul><blockquote>Tip: Normal phase (NP) stationary phases have been the first phases for chromatography and that is why their properties of polarity were determined as ’’normal’’. The stationary phase of a NP column has polar properties and is commonly used with nonpolar solvents as hexane or heptane. The other way round a reversed phase (RP) column has covalent charcteristics and is used with more polar eluents, like mixtures of acetonitrile and water.</blockquote>Stationary phase Eurospher II 100 Si is provided in these column types: analytical, semi-preparative and preparative.Eurospher II 100 Si Analytical Columns are available with these parameters:<ul><li>Column length (mm): 50, 100, 150, 250</li><li>Column ID (mm): 3, 4, 4.6</li><li>Particle size (µm): 3, 5</li></ul>Eurospher II 100 Si Semi-Preparative Standard Columns are available with these parameters:<ul><li>Column length (mm): 30, 50, 125, 150, 250</li><li>Column ID (mm): 8, 16</li><li>Particle size (µm): 5, 10</li></ul><h3>KNAUER (U)HPLC Columns</h3>Widest range of HPLC and UHPLC columns for all separation modes and applications.<ul><li>Safe Investment: Robust and reliable columns for attractive price&nbsp;</li><li>Separation Mode: Reversed Phase, HILIC, Normale</li><li>Simplicity: Easy purchase via our online store with fast delivery</li><li>Application: All-rounder for research or highly specialised for high-throughput analysis? We have the best column for your requirements.</li><li>Flexibility: Wide selection of column and particle sizes, for (U)HPLC applications up to 1000 bar</li></ul>KNAUER offers the perfect column for any small molecule separation. No matter which separation mode, molecule and the mobile phase, we offer a suitable (U)HPLC stationary phase. Choose from a wide range of modifications, particle sizes and column dimensions to suit your application. To elongate the lifetime of your column, you can choose to use a suitable precolumn.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_KNAUER_U_HPLC_C8_and_C8_A_Columns_083c60f401.webp" alt="KNAUER: KNAUER (U)HPLC Columns" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_KNAUER_U_HPLC_C8_and_C8_A_Columns_083c60f401.webp 182w," sizes="100vw" width="787" height="674">

Products focused on LC columns from KNAUER - page 6

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