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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Watrex Streamline binary gradient HPLC system

Watrex Streamline™ binary gradient HPLC system consists of two P1 pumps, static mixer, CT1 column thermostat, PDA1 diode-array detector, AS1 auto-sampler, and Clarity PDA datastation.

Streamline™ binary gradient HPLC system consists of two <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/?s=streamline+p1+pump&amp;post_type=product&amp;dgwt_wcas=1?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">P1 pumps</a>, static mixer, <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/column-thermostats/streamline-ct1-columm-thermostat/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">CT1 column thermostat</a>, <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/?s=pda1&amp;post_type=product&amp;dgwt_wcas=1?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">PDA1 diode-array detector</a>, <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/sampling-devices/autosamplers/streamline-as1-autosampler/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">AS1 auto-sampler</a>, and Clarity PDA datastation.<h3>FEATURES</h3><ul><li>Optimized pump mechanics with parallel piston design offers excellent flow rate accuracy and gradient composition at all solvents ratios</li><li>Variable volume injection range 0.1 - 999.9 μl, high precision and reproducibility, and low carryover AS1 autosapler</li><li>Excellent signal-to-noise ratio of the PDA2 detector</li><li>Data acquisition, processing and instrument control is by <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/999">Clarity Chromatography Station*</a></li></ul><h3>COMPONENT SPECIFICATION</h3><ul><li>Gradient solvent delivery system consisting of two P1 HPLC pumps</li></ul><h5>COMPONENT P1 HPLC pumps</h5><ul><li>Flow Rates: 0,01 ml/min – 9,99 ml/min with step 0.01 ml/min (analytical)</li><li>Flow Rates: 0,10 ml/min – 40,0 ml/min (preparative)</li><li>Pressure: 42 MPa/6000 psi (analytical, stainless steel)</li><li>Pressure: 35 Mpa/5000 psi (analytical, PEEK)</li><li>Pressure: 10 Mpa/1500 psi (preparative)</li><li>Flow precision: ± 0,2% RSD @ 1mL/min. and 1,000 psi (analytical)</li><li>Flow accuracy: ± 1% @ 1mL/min. and 1,000 psi (analytical)</li><li>Pressure accuracy: ± 2% of full-scale, with 80:20 H2O/IPA @ 1000psi</li><li>Pulsation: better than ± 0.5% @ 1mL/min. and 1,000 psi (analytical)</li><li>Remote control: USB</li><li>Remote control: Start, Stop, Status, Error</li></ul><h5>COMPONENT - PDA1 detector</h5><ul><li>Wetted Materials: Stainless Steel/ PEEK*, teflon, Glass (*depending on configuration)</li><li>Light Source: Deuterium Lamp, Tungsten Lamp</li><li>Wavelength Range: 190 – 720 nm</li><li>Number of Diodes: 256</li><li>Baseline Noise: ± 1 x 10-5 AU (@240 nm, 2 sec. risetime)</li><li>Baseline Drift: less than 3 x 10-4 AU/h</li><li>Wavelength Accuracy: 0.5 nm</li><li>Mean Pixel Pitch: 2.2 nm</li><li>Resolution: 7 nm</li><li>Linearity: higher than 2.0 AU</li><li>Data Rate: 1 Hz – 100 Hz</li></ul><h5>COMPONENT - CT1 Column thermostat</h5><ul><li>Temperature range: 10 °C above ambient temperature to 100 °C</li><li>Temperature accuracy: max. 0,5 % of actual temperature</li><li>Temperature stability: RSD &lt; 0,4 %</li><li>Settability: 0,1 °C</li><li>Internal dimensions: 320 x 50 x 30 mm (L x W x H)</li><li>Compartment material: PTFE coated metal</li><li>Compartment connection: USB</li><li>Control: build-in color touch panel, datasystem</li></ul><h5>COMPONENT - AS1 autosampler: X-Y-Z-Operation; motor driven syringe, Capacity: 60 vials, Sample Loop: standard, 20μl, Reproducibility: Fix Volume: &lt; 0.5%, Variable Volume: &lt;1.0%, Carry-over: &lt;0.01% , Programmable wash.</h5><h5>COMPONENT - Clarity™ Chromatography Station: PDA data acquisition and evaluation, gradient, and autosampler control with pre-set methods for experimental settings. PC Win 10 Professional with LCD monitor .</h5><h3>Ordering information:</h3><h5>PN/Component:</h5><ul><li>SSG101-001 Streamline™ binary HPLC system (Includes P1m+P1s pumps, PDA1 detector, CT1 thermostat, AS1 autosampler, solvent rack, Clarity PC station)</li></ul><h5>Optional configurations:</h5><ul><li>SPDA99-201 Remove PDA1 diode-array detector from system</li><li>ST99-001 Remove CT1 column thermostat from system</li><li>SAS99-001 Remove AS1 autosampler from system</li><li>SUV90-001 Add UV1 Variable UV/Vis detector to system</li><li>SFC90-001 Add FC1 Fraction collector to system</li><li>SCT90-002 Add CT1i column thermostat with manual injector from system</li></ul>

Watrex Streamline Isocratic HPLC system

Streamline™ isocratic HPLC system consists of one P1 pump, CT1i column thermostat with manual injector and UV1 UV/Vis detector.

Streamline™ isocratic HPLC system consists of one <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/?s=streamline+p1+pump&amp;post_type=product&amp;dgwt_wcas=1?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">P1 pump</a>, <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/column-thermostats/streamline-ct1-columm-thermostat/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">CT1 column thermostat </a>with manual injector and <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/?s=uv1+uv&amp;post_type=product&amp;dgwt_wcas=1?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">UV1 UV/Vis detector</a>. Modular concept offers easy and economical upgrades or configuration modifications such as additional detectors, autosampler or fraction collector.<h3>FEATURES</h3><ul><li>Optimized pump mechanics with parallel piston design offers excellent flow rate accuracy and low pulsation</li><li>Excellent signal-to-noise ratio of the UV1 detector</li><li>Data acquisition, processing and instrument control is done by Clarity Chromatography Station</li></ul><h3>COMPONENT SPECIFICATION</h3><h5>SPECIFICATIONS - P1 HPLC pump:</h5><ul><li>Flow Rates: 0.001 to 10.000 mL/min</li><li>Pressure: 0 to 6,000 psi (42 MPa)</li><li>Flow precision: &gt; 0.2% RSD</li><li>Flow accuracy: ± 1 % @ 1mL/min and 7 MPa,</li><li>Pressure accuracy: ± 2% of full-scale, with 80:20 H2O/IPA @ 7 MPa</li><li>Pulsation: ± 0.5 % @ 1mL/min and 7 MPa</li><li>Remote inputs: USB</li></ul><h5>SPECIFICATIONS - UV1 UV detector:</h5><ul><li>Light Source: Deuterium Lamp, Tungsten Lamp</li><li>Wavelength Range: 190 – 800 nm</li><li>Baseline Noise: 1 x 10-5 AU (@240 nm, 2 sec. risetime)</li><li>Baseline Drift: less than 3 x 10-4 AU/h</li><li>Wavelenghth Reproducibility: ± 0.1 nm</li><li>Linearity: better than 2.5 AU</li><li>Analog Output: 1x 1 V</li></ul><h5>SPECIFICATIONS - CT1 Column thermostat:</h5><ul><li>Temperature range: 10 °C above ambient temperature to 100 °C</li><li>Temperature accuracy: max. 0,5 % of actual temperature</li><li>Temperature stability: RSD &lt; 0,4 %</li><li>Settability: 0,1 °C</li><li>Internal dimensions: 320 x 50 x 30 mm (L x W x H)</li><li>Compartment material: PTFE coated metal</li><li>Compartment connection: USB</li><li>Control: build-in color touch panel, datasystem</li></ul><h5>SPECIFICATIONS - <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/999">Clarity™ Chromatography Station</a>:</h5><ul><li>Advanced data acquisition and evaluation, enables routine separations with pre-set methods for experimental settings. PC Win 10 Professional with LCD monitor included</li></ul><h3>Ordering information:</h3><h5>PN/Component:</h5><ul><li>SSI101-001 Streamline™ isocratic system (Includes P1 pump,UV1 detector, CT1i column thermostat with manual injector, solvent rack, Clarity datastation)</li><li>SUV99-001 Remove UV1 detector from system</li><li>ST99-002 Remove CT1i column thermostat with manual injector from system</li><li>SPDA90-001 Add PDA1 265 photodiode detector to system</li><li>SRI90-001 Add RI1 Refractive index detector to system</li><li>SAS90-001 Add AS1 Autosampler to system</li><li>SFC90-001 Add FC1 Fraction collector to system</li></ul>

Products from category HPLC focused on HPLC distributed by WATREX Prague - page 1

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