STH Antibody

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Description

Definition and Biology of STH Antibody

STH (Saitohin) antibody is a targeted immunological reagent used to detect the saitohin protein, a 13.7 kDa protein encoded by the intronic region of the MAPT (microtubule-associated protein tau) gene . This protein is implicated in neurodegenerative diseases such as frontotemporal dementia and tauopathies due to its association with tau protein aggregation .

Key Biological Characteristics of STH Protein

ParameterDetailSource
Molecular Weight13.7 kDa
Amino Acid Length128 residues
Subcellular LocalizationNucleus, Cytoplasm
Tissue ExpressionPlacenta, Muscle, Brain (Fetal/Adult)
SynonymsMAPT intronic transcript

Applications in Research

STH antibodies are primarily employed in immunodetection assays to study saitohin’s role in tau-related pathologies.

Common Applications

MethodPurposeAntibody TypeExample Suppliers
Western BlottingDetect STH protein in tissue lysatesMonoclonal (Mouse)OriGene (OTI1C12)
ImmunohistochemistryLocalize STH in brain tissue sectionsPolyclonal (Rabbit)MyBioSource
ELISAQuantify STH levels in biological fluidsMonoclonal/PolyclonalAntibodies-Online

Key Supplier Comparison

SupplierAntibody Clone/TypeImmunogen TargetApplications
OriGeneOTI1C12 (Monoclonal)Full-length STHWestern Blot
Antibodies-OnlinePolyclonal (Rabbit)AA 61-110Western Blot
MyBioSourceN/AN/AELISA, IHC

Product Specs

Buffer
Preservative: 0.03% ProClin 300; Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Product dispatch occurs within 1-3 business days of order receipt. Delivery times may vary depending on the purchase method and location. Please contact your local distributor for precise delivery estimates.
Synonyms
STH antibody; Saitohin antibody
Target Names
STH
Uniprot No.

Target Background

Gene References Into Functions

Saitohin (STH) Gene and Neurological Disease: A Summary of Research Findings

  • Association with Alzheimer's Disease: Multiple studies have investigated the association between STH polymorphisms (particularly the Q7R polymorphism) and Alzheimer's disease risk. While some studies suggest an association, particularly in late-onset disease and specific populations (e.g., Caucasians), others find no significant link. Meta-analyses have yielded mixed results, highlighting the need for further research to clarify the role of STH in Alzheimer's disease pathogenesis. (PMID: 28211174, 25305495, 20852909, 12032355, 12826738, 18850062)
  • Association with Parkinson's Disease: Research indicates a potential association between the rs6203857 polymorphism and increased Parkinson's disease risk. Additionally, some studies suggest an interaction effect between STH and other genes (e.g., MAPT) in modulating Parkinson's disease susceptibility. (PMID: 25168738, 25305495, 12932819, 16909000)
  • Association with other Neurodegenerative Diseases: Studies suggest potential links between STH polymorphisms and other neurodegenerative conditions, including frontotemporal lobar dementia, Huntington's disease, and schizophrenia. The involvement of STH in cognitive impairment, especially aspects of executive function, has also been explored. (PMID: 20852909, 25283873, 22187337, 21934306, 18300012, 16186110)
  • Cellular Function of Saitohin: Research suggests allele-specific effects of Saitohin on Abl-mediated phosphorylation, indicating a previously unknown cellular function. Furthermore, interactions with peroxiredoxin 6 have been noted. (PMID: 21769920, 16186110)
  • Inconclusive Findings: It's important to note that some studies have failed to find a significant association between STH polymorphisms and various neurodegenerative diseases. These inconsistencies highlight the complexity of gene-disease relationships and the need for further investigation. (PMID: 16909000, 18396294)

Note: Several PMIDs listed in the original text referenced observational studies or HuGE Navigator entries, which are included here for completeness. The specific details of these studies would need to be reviewed individually for context.

Database Links

HGNC: 18839

OMIM: 607067

KEGG: hsa:246744

STRING: 9606.ENSP00000443168

UniGene: Hs.661831

Subcellular Location
Cytoplasm. Nucleus.
Tissue Specificity
Highest expression in placenta, muscle, fetal brain, and adult brain, with lower expression in heart, kidney, stomach, testis, and adrenal gland. In the central nervous system, highest expression is in temporal lobe, hypothalamus, medulla and spinal cord,

Q&A

What is STh and why are antibodies against it significant in research?

STh (heat-stable toxin h) is a small peptide toxin produced by enterotoxigenic bacteria that causes diarrheal disease. Antibodies against STh are critical for several reasons:

  • They serve as essential tools for developing vaccines against enterotoxigenic bacteria

  • They can neutralize the toxin, providing protection against disease

  • They function as research instruments for studying toxin structure and mechanism

  • They help quantify toxin levels in experimental and clinical samples

The development of specific and effective STh antibodies is challenging due to the toxin's small size and structural similarity to human endogenous peptides like guanylin and uroguanylin, which necessitates careful antibody engineering to avoid cross-reactivity .

How do STh antibodies differ structurally from other enterotoxin antibodies?

STh antibodies target a compact, disulfide-rich peptide toxin, which presents distinct challenges compared to antibodies against larger protein enterotoxins:

  • They must recognize a small structure with limited epitopes

  • They require exquisite specificity to avoid cross-reactivity with human endogenous peptides

  • They often need carrier protein conjugation for effective immunization

  • They typically require specialized assay methods for detection and characterization

Unlike antibodies against larger protein toxins that may recognize multiple epitopes, STh antibodies must target specific regions on a constrained structure, making epitope selection particularly important .

What are the basic principles of STh antibody detection in research settings?

Detection of STh antibodies relies on several key principles:

  • Competitive ELISA is the gold standard for measuring STh antibody responses

  • Percent inhibition is calculated using the formula: (1−(A−B)/(TA−B)) × 100, where A is sample absorbance, B is blank, and TA is total activity

  • The 50% inhibitory concentration (IC50) serves as a quantitative measure of antibody binding

  • Four-parameter logistic regression analysis is typically used to calculate IC50 values

  • Cross-reactivity assessment requires comparison of inhibition profiles against multiple antigens

These principles enable accurate characterization of antibody responses against STh and its variants in research settings .

What are the optimal techniques for purifying STh mutant peptides for antibody studies?

Based on the research literature, an effective purification protocol for STh mutant peptides includes:

  • Expression in E. coli BL21 Star™ (DE3) using IPTG induction in 2YT medium with glucose and kanamycin

  • Cell lysis via lysozyme treatment and ultrasonication

  • Initial purification using Ni-NTA chromatography

  • Cleavage from fusion partners (e.g., DsbC) using TEV protease

  • Secondary Ni-NTA purification to remove fusion partners

  • Final purification using either:

    • Reversed-phase chromatography for untagged peptides

    • Size-exclusion chromatography for tagged peptides

  • Confirmation of correct disulfide bridge connectivity using competitive ELISA

  • Mass verification using MALDI-TOF mass spectrometry

This multi-step approach ensures high purity and correct folding of STh peptides for downstream antibody studies .

How should competitive ELISA be optimized for STh antibody detection and cross-reactivity assessment?

Optimization of competitive ELISA for STh antibody analysis requires careful attention to several parameters:

  • Selection of appropriate coating antigen (typically native STh conjugated to a carrier protein)

  • Determination of optimal primary antibody dilution (50-70% of maximum binding)

  • Preparation of precise dilution series of competing antigens

  • Inclusion of proper controls: blank wells, total activity wells, and standards

  • Calculation of percent inhibition using the established formula

  • Determination of IC50 values via four-parameter logistic regression

  • For cross-reactivity studies:

    • Use of consistent reference concentration of STh across all peptides

    • Calculation of cross-reacting fractions by normalizing to STh inhibition

    • Statistical analysis of cross-reactivity patterns across multiple sera

These optimizations ensure reliable quantification of STh antibody responses and their cross-reactivity profiles .

What carrier proteins and conjugation strategies are most effective for STh antibody development?

The choice of carrier protein significantly impacts the immunogenicity and specificity of STh antibody responses:

Carrier SystemAdvantagesConsiderationsTypical Application
Mi3 nanoparticles with SpyCatcherMultivalent display, enhanced immunogenicityRequires SpyTag fusionVaccine candidates
Bovine Serum Albumin (BSA)Well-established, consistently immunogenicMay require chemical conjugationResearch antibodies
DsbC fusion partnersEnsures proper disulfide formationRequires enzymatic cleavageExpression/purification
SpyTag-tagged systemsSite-specific conjugationRequires SpyCatcher carriersControlled orientation

The research indicates that mi3 nanoparticles are particularly effective for presenting STh epitopes in a multivalent format, enhancing B-cell activation and antibody production, while BSA conjugates have also proven effective when combined with appropriate adjuvants .

How do mutations in STh affect antibody neutralization capacity and cross-reactivity profiles?

Mutations in STh can profoundly impact antibody neutralization properties:

  • Single mutations (e.g., A14T) can maintain substantial antigenicity while reducing unwanted bioactivity

  • Double mutations (e.g., L9A/A14T) can further modify peptide properties while preserving key epitopes

  • Some mutations create neoepitopes that elicit antibodies with altered neutralization profiles

  • Neutralizing capacity does not always correlate directly with binding affinity

  • Mutations can significantly affect cross-reactivity with human endogenous peptides

Research demonstrates that sera raised against STh mutants typically show at least partial neutralizing activity toward native STh, indicating preservation of key neutralizing epitopes despite structural modifications .

What are the quantitative parameters for assessing STh antibody cross-reactivity with human endogenous peptides?

Cross-reactivity with human endogenous peptides requires careful quantitative assessment:

Target PeptideTypical Cross-ReactivityAcceptable RangeImplications
STp (porcine variant)Mean: 1.05 (range 0.99-1.08)>0.90Desired cross-protection
Uroguanylin (human)Mean: 0.16 (range 0.12-0.21)<0.20Potential autoimmunity risk
Guanylin (human)Mean: 0.14 (range 0.11-0.19)<0.20Potential autoimmunity risk

Individual sera can show higher levels (>0.2) of unwanted cross-reactivity, emphasizing the importance of:

  • Screening multiple individual sera rather than pooled samples

  • Setting acceptance criteria for maximum allowable cross-reactivity

  • Monitoring cross-reactivity across different immunization protocols

These parameters help researchers balance cross-protection against STh variants while minimizing potential autoimmune risks .

How can neoepitopes in mutant STh variants be leveraged for improved vaccine design?

Neoepitopes in mutant STh variants offer strategic opportunities for vaccine development:

  • Identification of mutations that create new epitopes while preserving neutralizing capacity

  • Development of mutant-specific antibody assays to characterize these neoepitopes

  • Selection of mutants that direct the immune response away from epitopes shared with human peptides

  • Strategic combination of multiple mutants to broaden epitope coverage

  • Carrier protein selection that optimally presents these neoepitopes

The presence of neoepitopes in double mutant STh variants suggests that strategic mutations can reshape the antibody response, potentially improving vaccine efficacy while reducing unwanted cross-reactivity. This approach represents a cutting-edge strategy in enterotoxigenic bacterial vaccine development .

What statistical approaches are most appropriate for analyzing STh antibody binding and neutralization data?

Robust statistical analysis of STh antibody data requires:

  • For IC50 calculation:

    • Four-parameter logistic regression with appropriate constraints

    • Reporting of confidence intervals to indicate precision

    • Comparison to reference standards in each assay

  • For cross-reactivity analysis:

    • Calculation of cross-reacting fractions normalized to reference STh inhibition

    • Reporting of ranges and means to characterize variability

    • Use of paired statistical tests when comparing the same sera against different antigens

    • ANOVA with Tukey's multiple comparison test for significance determination

  • For neutralization data:

    • Calculation of IC90 values for functional protection assessment

    • Correlation analysis between binding affinity and neutralization capacity

    • Assessment of neutralization breadth across toxin variants

These statistical approaches ensure reliable interpretation of complex antibody response data, critical for advancing STh antibody research .

How can researchers resolve contradictory findings in STh antibody cross-reactivity studies?

When faced with contradictory cross-reactivity findings, researchers should:

  • Examine methodological differences:

    • ELISA coating conditions and antigen presentation

    • Calculation methods for cross-reactivity ratios

    • Reference concentration selection

  • Consider biological variables:

    • Immunization protocols and adjuvant differences

    • Individual versus pooled sera analysis

    • Animal model variations

  • Implement resolution strategies:

    • Head-to-head comparison using standardized protocols

    • Epitope mapping to identify binding site differences

    • Functional neutralization assays to assess biological relevance

    • Multi-laboratory validation studies

The literature reveals that cross-reactivity can vary substantially between individual sera and experimental conditions, making methodological standardization essential for resolving contradictory findings .

What controls are essential for validating STh antibody specificity and functionality?

A comprehensive control strategy for STh antibody research includes:

  • Binding specificity controls:

    • Pre-immune sera to establish baseline

    • Irrelevant toxin antibodies to confirm specificity

    • Carrier protein-only immunization to control for carrier effects

    • Absorption studies with native and mutant peptides

  • Cross-reactivity controls:

    • Human guanylin and uroguanylin competition

    • Structurally similar but functionally distinct peptides

    • Concentration gradients to establish inhibition curves

  • Functional validation controls:

    • Correlation between binding and neutralization

    • Cell-based functional assays

    • In vivo protection models where applicable

  • Technical controls:

    • Multiple replicates for statistical robustness

    • Inter-assay calibration standards

    • Positive and negative control sera

These controls ensure the reliability and interpretability of STh antibody data, which is critical for advancing both basic research and vaccine development .

How are advanced structural biology techniques enhancing our understanding of STh antibody interactions?

Cutting-edge structural biology approaches are transforming STh antibody research:

  • X-ray crystallography and cryo-electron microscopy:

    • Visualization of antibody-STh complexes at atomic resolution

    • Identification of critical binding residues and interaction surfaces

    • Rational design of improved STh immunogens

  • Hydrogen-deuterium exchange mass spectrometry:

    • Mapping of antibody epitopes in solution

    • Determination of binding dynamics and conformational changes

    • Analysis of how mutations affect epitope accessibility

  • Computational modeling:

    • Prediction of antibody-antigen interactions

    • Virtual screening of potential STh variants

    • Simulation of antibody binding energetics

These advanced techniques are revealing unprecedented details about STh-antibody interactions, enabling rational design of next-generation vaccine candidates with optimal epitope presentation and minimal cross-reactivity with human peptides .

What high-throughput approaches are being developed for STh antibody developability assessment?

Novel high-throughput (HT) methodologies are accelerating STh antibody research:

  • Integrated HT workflows implemented at early discovery stages include:

    • In silico analysis for preliminary screening

    • Parallel expression and purification systems

    • Automated binding and functional assays

    • Data management systems for complex datasets

  • Key HT assays predicting developability parameters:

    • Colloidal properties assessment (aggregation, self-interaction)

    • Post-translational modification analysis

    • Thermostability screening

    • Fragmentation/clipping prediction

  • Benefits of HT approaches:

    • Require minimal material (100 μgs)

    • Enable screening of hundreds to thousands of candidates

    • Accelerate candidate selection

    • Reduce risks in development

These HT methodologies ensure that only robust antibody molecules progress to development stages, significantly improving the efficiency of STh antibody research and vaccine development .

How can STh antibody research inform broader vaccine development strategies against enterotoxigenic bacteria?

STh antibody research provides valuable insights for broader vaccine development:

  • Multi-target approaches:

    • Combining STh antibodies with antibodies against other virulence factors

    • Development of multivalent vaccines targeting multiple enterotoxins

    • Balanced immune responses against multiple antigens

  • Platform technologies:

    • Carrier protein systems optimized for small peptide antigens

    • Nanoparticle presentation strategies for enhanced immunogenicity

    • Novel adjuvant formulations specific for toxin neutralization

  • Translational considerations:

    • Correlation of in vitro neutralization with in vivo protection

    • Bridging studies between animal models and human responses

    • Population-specific immune response variations

By addressing the unique challenges of STh antibody development, researchers are establishing principles and methodologies applicable to other small peptide toxins and difficult vaccine targets, advancing the broader field of vaccine research against enterotoxigenic pathogens .

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