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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Linde Nitrogen 5.6 – Gas Cylinder

Linde Nitrogen 5.6 (≥99.9996%) for GC, analytics, and industry. Ultra-high purity gas for purging, protection, and carrier applications.

Nitrogen 5.6 from Linde is an ultra-high purity inert gas with a purity of ≥ 99.9996%, designed for demanding analytical, industrial, and research applications.Its extremely low impurity levels make it particularly suitable for gas chromatography and other analytical techniques where baseline stability and minimal interference are critical. Nitrogen 5.6 is also widely used as a protective, purge, and carrier gas in processes requiring reliable contamination control.Its versatility enables use across multiple industries as well as in advanced scientific research.<h4>Key Features</h4><ul><li>Ultra-high purity ≥ 99.9996% (5.6 grade)</li><li>Extremely low impurity levels</li><li>Chemically inert gas</li><li>Suitable for analytical applications (GC)</li><li>Stable and reproducible performance</li><li>Broad industrial and laboratory use</li></ul><h4>Technical Specifications</h4><ul><li>Gas: nitrogen (N₂)</li><li>Purity: ≥ 99.9996% (5.6 grade)</li><li>Supply form: pressurized gas cylinder<ul><li>10 L (200 bar)</li><li>50 L (200 bar)</li></ul></li></ul><h4>Applications</h4><ul><li>Protective and purge gas in metallurgy and metal processing</li><li>Chemical, food, and electronics industries</li><li>Carrier and protective gas in semiconductor manufacturing</li><li>Zero gas for analytical instruments</li><li>Purging gas in extrusion and system flushing</li><li>Carrier gas in gas chromatography (GC)</li><li>Cooling applications (e.g., shrink fitting)</li><li>Plastics processing</li><li>Construction and food industry</li><li>Biology, medicine, and research</li></ul>

Linde Nitrogen 4.6 – Gas Cylinder

Linde Nitrogen 4.6 (≥99.996%) for industry and analytics. Reliable inert gas for purging, protection, and calibration.

Nitrogen 4.6 from Linde is a high-purity inert gas with a purity of ≥ 99.996%, suitable for a wide range of industrial and analytical applications.Due to its chemical inertness, it is widely used as a protective and purge gas in processes where oxidation or contamination must be prevented. Nitrogen 4.6 is also suitable as a zero gas in analytical instrumentation, providing stable baseline conditions for accurate measurements.In industrial environments, it is commonly used as a cutting gas for laser and plasma cutting of standard materials.<h4>Key Features</h4><ul><li>Purity ≥ 99.996% (4.6 grade)</li><li>Chemically inert gas</li><li>Suitable for protective atmospheres</li><li>Stable performance in analytical applications</li><li>Versatile industrial use</li><li>Supplied in pressurized cylinders</li></ul><h4>Technical Specifications</h4><ul><li>Gas: nitrogen (N₂)</li><li>Purity: ≥ 99.996% (4.6 grade)</li><li>Supply form: pressurized gas cylinder<ul><li>20 l (200 bar)</li><li>50 l (200 bar)</li></ul></li></ul><h4>Applications</h4><ul><li>Protective and purge gas in metallurgy and metal processing</li><li>Chemical, food, and electronics industries</li><li>Carrier and protective gas in semiconductor manufacturing</li><li>Laser and plasma cutting gas</li><li>Zero gas for analytical and measurement systems</li></ul>

Linde Nitrogen 4.0 – Gas Cylinder

Linde Nitrogen 4.0 (≥99.99%) for industrial applications. Reliable inert gas for purging, protection, and cooling.

Nitrogen 4.0 from Linde is a technically pure inert gas with a purity of ≥ 99.99%, designed for a wide range of industrial and technological applications.Due to its chemical inertness, it is widely used as a protective and purging gas in processes where oxidation or unwanted reactions must be prevented. Nitrogen 4.0 is also suitable as a universal cooling medium and is applied across various industrial and research processes.Its robust and versatile performance makes it a cost-effective solution for applications where ultra-high purity is not required.<h4>Key Features</h4><ul><li>Purity ≥ 99.99% (4.0 grade)</li><li>Chemically inert gas</li><li>Suitable for protective and purging applications</li><li>Versatile industrial use</li><li>Suitable as a cooling medium</li><li>Cost-effective solution</li></ul><h4>Technical Specifications</h4><ul><li>Gas: nitrogen (N₂)</li><li>Purity: ≥ 99.99% (4.0 grade)</li><li>Supply form: pressurized gas cylinder<ul><li>10 L (200 bar)</li><li>20 L (200 bar)</li><li>50 L (200 bar)</li><li>50 L (300 bar)</li></ul></li></ul><h4>Applications</h4><ul><li>Protective gas in metallurgical, chemical, food, and electrochemical industries</li><li>Purging gas for pipes and tanks</li><li>Cooling applications (e.g., shrink fitting, plastics processing)</li><li>Construction, food industry, biology, and medicine</li><li>Welding applications (root protection and oxidation prevention)</li></ul>

Linde Nitrogen 5.3 – Gas Cylinder

Linde Nitrogen 5.3 (≥99.999%) for GC, analytics, and industry. High-purity inert gas for purging, protection, and carrier applications.

Nitrogen 5.3 from Linde is a high-purity inert gas with a purity of ≥ 99.999%, suitable for demanding analytical, industrial, and research applications.Its low impurity levels make it ideal as a carrier gas in gas chromatography and as a working gas for analytical instruments. It is also widely used as a protective, purge, and flushing gas in processes requiring a stable inert environment with minimal contamination risk.Nitrogen 5.3 offers an optimal balance between high purity and cost efficiency for a wide range of applications.<h4>Key Features</h4><ul><li>High purity ≥ 99.999% (5.3 grade)</li><li>Low trace impurity levels</li><li>Chemically inert gas</li><li>Suitable for analytical applications (GC)</li><li>Stable and reproducible performance</li><li>Versatile industrial and laboratory use</li></ul><h4>Technical Specifications</h4><ul><li>Gas: nitrogen (N₂)</li><li>Purity: ≥ 99.999% (5.3 grade)</li><li>Supply form: pressurized gas cylinder<ul><li>50 L (200 bar)</li><li>50 L (300 bar)</li></ul></li></ul><h4>Applications</h4><ul><li>Protective and purge gas in metallurgy and metal processing</li><li>Chemical, food, and electronics industries</li><li>Carrier and protective gas in semiconductor manufacturing</li><li>Zero gas for analytical instruments</li><li>Flushing gas for industrial systems</li><li>Carrier gas in gas chromatography (GC)</li><li>Cooling applications (e.g., shrink fitting)</li><li>Plastics processing</li><li>Construction and food industry</li><li>Biology, medicine, and research</li></ul>

Linde Nitrogen 6.0 – Gas Cylinder

Linde Nitrogen 6.0 (≥99.9999%) for GC, semiconductors, and research. Ultra-high purity inert gas for demanding analytical and industrial applications.

Nitrogen 6.0 from Linde is an ultra-high purity inert gas with a purity of ≥ 99.9999%, designed for the most demanding analytical, laboratory, and industrial applications.Its extremely low level of trace impurities makes it ideal for high-sensitivity analytical techniques such as gas chromatography, as well as for semiconductor manufacturing and advanced research. It ensures maximum stability, minimal contamination, and excellent reproducibility.Nitrogen 6.0 is the preferred choice wherever gas purity is critical and precise control of process conditions is required.<h4>Key Features</h4><ul><li>Ultra-high purity ≥ 99.9999% (6.0 grade)</li><li>Extremely low trace impurity levels</li><li>Chemically inert gas</li><li>Ideal for analytical and semiconductor applications</li><li>High stability and reproducibility</li><li>Suitable for high-end applications</li></ul><h4>Technical Specifications</h4><ul><li>Gas: nitrogen (N₂)</li><li>Purity: ≥ 99.9999% (6.0 grade)</li><li>Supply form: pressurized gas cylinder<ul><li>10 l (200 bar)</li><li>50 l (200 bar)</li></ul></li></ul><h4>Applications</h4><ul><li>Protective and purge gas in metallurgy and metal processing</li><li>Chemical, food, and electronics industries</li><li>Carrier and protective gas in semiconductor manufacturing</li><li>Zero gas for analytical instruments</li><li>Flushing gas for industrial systems</li><li>Carrier gas in gas chromatography (GC)</li><li>Cooling applications (e.g., shrink fitting)</li><li>Plastics processing</li><li>Construction and food industry</li><li>Biology, medicine, and research</li></ul>

Linde Food Grade Nitrogen – Gas Cylinder

Food grade nitrogen from Linde for MAP packaging, inerting, and food protection. Prevents oxidation and extends product shelf life.

Food grade nitrogen from Linde is a high-purity inert gas designed for use in the food and beverage industry. It complies with all relevant regulations for food-contact applications.Nitrogen is primarily used to displace oxygen, preventing oxidation, microbial growth, and product degradation. Its inert nature helps extend shelf life while preserving product quality, taste, and appearance.It is suitable for a wide range of applications, including modified atmosphere packaging and beverage inerting.<h4>Key Features</h4><ul><li>Food-grade quality compliant with regulations</li><li>Inert gas with no impact on taste or odor</li><li>Prevents oxidation and microbial growth</li><li>Extends shelf life of products</li><li>Suitable for MAP packaging and inerting</li><li>Colorless and odorless</li></ul><h4>Technical Specifications</h4><ul><li>Gas: nitrogen (N₂)</li><li>Grade: food grade</li><li>Supply form: gas cylinder<ul><li>20 L (200 bar)</li><li>50 L (200 bar)</li></ul></li></ul><h4>Applications</h4><h5>Food Industry:</h5><ul><li>Modified Atmosphere Packaging (MAP)</li><li>Oxygen displacement during packaging</li><li>Storage of oils and fats to prevent oxidation</li><li>Cryogenic cooling and freezing (liquid nitrogen)</li></ul><h5>Beverage Industry:</h5><ul><li>Inerting of beverages and equipment</li><li>Wine preservation and storage</li><li>Shelf-life extension of beverages</li></ul>

Organomation 6 Position N-EVAP Nitrogen Evaporator

Compact nitrogen evaporator for up to 6 samples with precise flow control, heated bath options, and wide sample compatibility.

The Organomation 6 Position N-EVAP is a compact and cost-effective sample concentrator designed for simultaneous evaporation of up to 6 samples. Based on the proven N-EVAP technology developed in the 1970s, it ensures reliable and reproducible solvent evaporation using nitrogen gas within a heated bath.The system supports a wide range of sample sizes – 10–30 mm OD as standard, and up to 30–56 mm OD with an optional holder. The circular rotating design allows easy front access to all samples.<h4>Key Features</h4><ul><li>Evaporation of up to 6 samples simultaneously</li><li>Adjustable nitrogen flow: 0–10 L/min</li><li>Individually adjustable needle valves for precise control</li><li>Circular rotating sample holder for easy access</li><li>Wide sample diameter range: 10–56 mm OD (with optional holder)</li><li>Stainless steel bath construction for durability</li><li>Water or dry bath configurations available</li><li>High temperature limit switch for safety</li><li>Phthalate-free silicone tubing to prevent contamination</li><li>Efficient nitrogen usage with minimal waste</li></ul><h3>Technical Specifications</h3><h4>General</h4><ul><li>Number of positions: 6</li><li>Sample holder layout: Circular</li><li>Gas manifold: Single ring</li><li>Gas flow meter: 0–10 L/min</li><li>Standard sample OD: 10–30 mm</li><li>Optional sample OD: 30–56 mm</li><li>Gas input pressure: 20–30 psig</li><li>With regulator: 30–160 psig</li></ul><h4>Dimensions</h4><ul><li>Water bath: 33 × 28 × 79 cm</li><li>Dry bath: 33 × 28 × 70 cm</li><li>Reduced height: 33 × 28 × 61 cm</li></ul><h4>Needles</h4><ul><li>Length: 4 in (≈10 cm)</li><li>Gauge: 19 ga</li><li>Material: stainless steel + chrome-plated brass hub</li></ul><h4>Heating – Water Bath</h4><ul><li>Temperature range: 30–90 °C</li><li>Power: 550 W</li><li>Controller: mechanical thermostat</li><li>Accuracy: ±2 °C</li></ul><h4>Heating – Dry Bath</h4><ul><li>Temperature range: 40–130 °C</li><li>Power: 500 W</li><li>Medium: aluminum / glass beads</li><li>Accuracy: ±2 °C</li></ul>

Organomation 20 Position Auto N-EVAP Nitrogen Evaporator

The 20 Position Auto N-EVAP enables automated, safe evaporation of up to 20 samples with digital control and pneumatic sample handling.

The Organomation 20 Position Auto N-EVAP is the most advanced nitrogen evaporator developed by Organomation. It combines the classic N-EVAP system with timed automation and optional nitrogen self-generation.The instrument operates in both automatic and manual modes using an integrated pneumatic system. In automatic mode, samples are removed from the heating bath at the end of the cycle, reducing the risk of sample loss or damage.A digital control system provides precise control of gas flow and bath temperature, ensuring safe and reproducible evaporation of up to 20 samples simultaneously.<h4>Key Features</h4><ul><li>Automatic and manual operation modes</li><li>Capacity of up to 20 samples</li><li>Automatic sample removal after cycle completion</li><li>Digital control of temperature and timing</li><li>Nitrogen flow up to 25 L/min</li><li>Built-in pressure reducing regulator</li><li>Dual nitrogen filtration system</li><li>Pneumatic sample lift (gas piston)</li><li>Safety cover and circuit breaker</li><li>Precision needle valve control</li><li>Phthalate-free high-pressure tubing</li><li>Reduced risk of sample loss through automation</li></ul><h4>Available Model</h4><h5>Automatic 20 Position N-EVAP – Water Bath</h5><ul><li>Catalog number: 11220-A</li><li>Bath type: Water</li><li>Number of positions: 20</li><li>Dimensions: 49 × 46 × 92 cm</li><li>Temperature range: 30–100 °C</li><li>Total wattage: 1100 W</li></ul><h5>Standard Features</h5><ul><li>Adjustable flow meter: 0–25 L/min</li><li>Built-in pressure reducing regulator</li><li>Dual nitrogen filters</li><li>Digital temperature controller (LED)</li><li>Electronic timer</li><li>High temperature limit switch</li><li>Safety cover</li><li>Circuit breaker</li><li>High-pressure phthalate-free tubing</li><li>Precision variable valve technology</li><li>Gas piston lift mechanism</li><li>Set of 20 needles (4" × 19 gauge)</li></ul><h4>Options</h4><ul><li>220v wiring harness</li><li>Z-Purge / positive pressure purge case</li><li>Acid resistant coating on instrument and needles</li></ul><h4>Technical Specifications</h4><h4>General</h4><ul><li>Number of positions: 20</li><li>Sample holder layout: Circular</li><li>Gas manifold: Single Ring</li><li>Gas flow rate: 0–25 L/min</li><li>Sample size range: 10–30 mm OD</li><li>Nitrogen input pressure: 30–110 psig</li><li>Acid resistant coating: Optional</li></ul><h4>Needles</h4><ul><li>Size: 102 mm × 19 ga (4")</li><li>Material: stainless steel with plated brass hub</li></ul><h4>Sample Lift Mechanism</h4><ul><li>Type: Gas piston</li><li>Function: automatic lifting/removal of samples</li></ul><h4>Control System</h4><ul><li>Digital temperature control (LED display)</li><li>Electronic timer for gas and heating</li></ul><h4>Heating Specifications</h4><ul><li>Model: 11196</li><li>Medium: Water</li><li>Inside dimensions: 11 × 11 × 5.5 in</li><li>Outside dimensions: 49 × 46 × 18 cm</li><li>Power: 1100 W</li><li>Temperature range: 30–100 °C</li><li>Controller: digital electronic</li><li>Accuracy: ±2 °C</li></ul><h4>Accessories</h4><ul><li>Nitrogen generator (20 L/min)</li><li>Pasteur pipette adapters</li><li>Pressure reducing regulator 0–160 psi</li><li>High temperature silicone fluid</li><li>Various needle sizes and gauges</li></ul><h4>Replacement Parts</h4><ul><li>NA1955 – Nitrogen generator</li><li>NA0603 – Needles 4" × 19 ga</li><li>NA0636 – Pasteur pipette adapter</li></ul>

Organomation 9 Position MULTIVAP Nitrogen Evaporator

The MULTIVAP 9 Position enables rapid evaporation of large-volume samples using a high-temperature dry block and efficient row-based nitrogen control.

The Organomation 9 Position MULTIVAP is a high-temperature dry block nitrogen evaporator designed for large volume sample evaporation.The system features a rectangular 3×3 gas distribution manifold and a dual post lifting assembly, allowing easy adjustment of needles or pipettes. Nitrogen is directed onto the sample surface, enabling rapid solvent evaporation and efficient sample concentration.Each row of three positions can be individually switched on/off, allowing significant nitrogen savings when processing fewer samples.The system operates with a heated aluminum dry block (30–120 °C) or as an ambient (unheated) version.<h4>Key Features</h4><ul><li>Up to 9 samples simultaneously (3×3 layout)</li><li>High-temperature dry block: 30–120 °C</li><li>Ambient (unheated) version available</li><li>Direct nitrogen delivery onto sample surface</li><li>Row-based gas control (3 samples per row)</li><li>Nitrogen flow range: 0–25 L/min</li><li>Built-in pressure regulator</li><li>Digital temperature control and timer</li><li>Dual spring hoist lifting system</li><li>Includes 50 mm OD beakers</li><li>Custom inserts available for different sample sizes</li><li>Compatible with organic solvents</li><li>Optional acid-resistant configuration</li></ul><h4>Available Models</h4><h5>9 Position MULTIVAP – Dry Block</h5><ul><li>Catalog number: 11809</li><li>Heating type: Dry block</li><li>Number of positions: 9</li><li>Dimensions: 41 × 36 × 76 cm</li><li>Temperature range: 30–120 °C</li><li>Power: 900 W</li></ul><h5>9 Position MULTIVAP – No Heating</h5><ul><li>Catalog number: 11809-O</li><li>Heating type: None</li><li>Number of positions: 9</li><li>Dimensions: 33 × 38 × 66 cm</li><li>Temperature: Ambient</li></ul><h4>Standard Features</h4><ul><li>Adjustable flow meter: 0–25 L/min</li><li>Gas distribution manifold (3×3)</li><li>Nitrogen filter</li><li>Built-in pressure reducing regulator</li><li>Electronic timer</li><li>Digital temperature controller (LED)</li><li>Safety control cover plate</li><li>High temperature limit switch</li><li>Dual band hoist spring assembly</li><li>9 beakers (50 mm OD included)</li></ul><h4>Options</h4><ul><li>220v wiring harness</li><li>Z-Purge / positive pressure purge case</li><li>Acid resistant coating</li><li>Pasteur pipette adapters instead of needles</li><li>Manifold and stand only (no heating platform)</li></ul><h3>Technical Specifications</h3><h4>General</h4><ul><li>Number of positions: 9</li><li>Layout: Rectangular (3×3)</li><li>Spacing: 5.87 cm</li><li>Standard vessels: 50 mm OD beakers</li><li>Optional tube range: 16–40 mm OD</li><li>Gas flow: 0–25 L/min</li><li>Flow control: per row (3 samples)</li><li>Gas input pressure: 30–110 psig</li><li>Acid resistant coating: Optional</li></ul><h4>Needles</h4><ul><li>Size: 102 mm × 16 ga</li><li>Material: stainless steel</li><li>Needle guide: optional for tubes</li></ul><h4>Lift Mechanism</h4><ul><li>Type: Dual pulley &amp; band springs</li><li>Function: adjustable needle height</li></ul><h4>Heating Specifications</h4><ul><li>Model: 9156</li><li>Type: Aluminum dry block</li><li>Dimensions: 41 × 36 × 15 cm</li><li>Power: 900 W</li><li>Temperature range: 30–120 °C</li><li>Controller: digital electronic (LED)</li><li>Accuracy: ±2 °C</li></ul><h4>Accessories</h4><ul><li>Nitrogen generator</li><li>Custom inserts&nbsp;</li><li>Pasteur pipette adapters</li><li>Luer plugs</li><li>Various needle sizes and gauges</li></ul>

Organomation 30 Position MULTIVAP Nitrogen Evaporator

The MULTIVAP 30 Position enables high-throughput evaporation of up to 30 samples with a heated dry block, efficient gas control, and custom inserts.

The Organomation 30 Position MULTIVAP is a high-capacity dry block nitrogen evaporator designed for parallel evaporation of up to 30 samples.The system features a rectangular 5×6 gas distribution manifold and a dual post lifting assembly. Nitrogen is directed onto the sample surface, enabling rapid solvent evaporation and efficient concentration.Each row of 5 samples can be independently switched on/off, allowing significant nitrogen savings when processing fewer samples.The system operates with a heated aluminum dry block (30–120 °C) or as an ambient (unheated) version. Custom-made inserts and blocks ensure optimal heat transfer for specific sample sizes.<h4>Key Features</h4><ul><li>Up to 30 samples simultaneously (5×6 layout)</li><li>High-temperature dry block: 30–120 °C</li><li>Ambient (no heating) version available</li><li>Direct nitrogen blowdown onto sample surface</li><li>Row-based gas control (5 samples per row)</li><li>Nitrogen flow: 0–25 L/min</li><li>Built-in pressure regulator</li><li>Digital temperature control and timer</li><li>Dual spring hoist system</li><li>Custom inserts for optimized heat transfer</li><li>Compatible with organic solvents</li><li>Optional acid-resistant version</li></ul><h4>Available Models</h4><h5>30 Position MULTIVAP – Dry Block</h5><ul><li>Catalog number: 11830</li><li>Heating type: Dry block</li><li>Number of positions: 30</li><li>Dimensions: 41 × 36 × 76 cm</li><li>Temperature range: 30–120 °C</li><li>Power: 900 W</li></ul><h5>30 Position MULTIVAP – No Heating</h5><ul><li>Catalog number: 11830-O</li><li>Heating type: None</li><li>Number of positions: 30</li><li>Dimensions: 33 × 38 × 66 cm</li><li>Temperature: Ambient</li></ul><h4>Standard Features</h4><ul><li>Adjustable flow meter: 0–25 L/min</li><li>Gas distribution manifold (5×6)</li><li>Nitrogen filter</li><li>Built-in pressure reducing regulator</li><li>Digital temperature controller (LED)</li><li>Electronic timer</li><li>Safety control cover plate</li><li>High temperature limit switch</li><li>Dual band hoist spring assembly</li></ul><h4>Options</h4><ul><li>220v wiring harness</li><li>Z-Purge / positive pressure purge case</li><li>Acid resistant coating</li><li>Pasteur pipette adapters instead of needles</li><li>Manifold and stand only (no heating platform)</li></ul><h3>Technical Specifications</h3><h4>General</h4><ul><li>Number of positions: 30</li><li>Layout: Rectangular (5×6)</li><li>Spacing: 3.33 cm</li><li>Sample diameter range: 16–30 mm OD</li><li>Gas flow: 0–25 L/min</li><li>Flow control: per row (5 samples)</li><li>Gas input pressure: 30–110 psig</li><li>Acid resistant coating: Optional</li></ul><h4>Needles</h4><ul><li>Size: 102 mm × 19 ga</li><li>Material: stainless steel</li><li>Needle guide: optional</li></ul><h4>Lift Mechanism</h4><ul><li>Type: Dual pulley &amp; band springs</li><li>Function: adjustable needle height</li></ul><h4>Heating Specifications</h4><ul><li>Model: 9156</li><li>Type: Aluminum dry block</li><li>Dimensions: 41 × 36 × 15 cm</li><li>Power: 900 W</li><li>Temperature range: 30–120 °C</li><li>Controller: digital electronic (LED)</li><li>Accuracy: ±2 °C</li></ul><h4>Accessories</h4><ul><li>Nitrogen generator</li><li>Custom inserts</li><li>Pasteur pipette adapters (not compatible with needle guide)</li><li>Luer plugs</li><li>Various needle sizes and gauges</li></ul>

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