sult1st1 Antibody

What is SULT1A1 and why is it significant for research?

SULT1A1 is a cytosolic sulfotransferase that catalyzes the sulfate conjugation of various compounds including catecholamines, phenolic drugs, and neurotransmitters. It functions as a homodimer (approximately 37-38 kDa) primarily expressed in brain, liver, skin, and lung tissues . This enzyme plays a critical role in:

• Xenobiotic detoxification and elimination

• Metabolism of pharmaceutical compounds

• Hormone regulation

• Potential activation of carcinogenic N-hydroxyarylamines

SULT1A1's involvement in these processes makes it a significant target for research in pharmacology, toxicology, and oncology .

What are the common applications for SULT1A1 antibodies in research?

SULT1A1 antibodies are primarily used in:

• Western blotting (detecting bands at approximately 37-38 kDa)

• Immunohistochemistry (IHC-P)

• Flow cytometry

• Simple Western assays

These applications help researchers detect and quantify SULT1A1 expression in various tissues and cell lines, particularly human liver tissue and HEK293 cells .

What tissue samples and cell lines serve as appropriate positive controls for SULT1A1 antibody experiments?

Based on validated research protocols:

These samples consistently show detectable levels of SULT1A1 expression and are recommended for validating antibody specificity and optimizing experimental conditions .

What are the optimal conditions for Western blot analysis using SULT1A1 antibodies?

For successful Western blot detection of SULT1A1:

• Sample preparation: Use reducing conditions and appropriate buffer systems (e.g., Immunoblot Buffer Group 8 has been validated)

• Antibody concentration: 1 μg/mL of affinity-purified polyclonal antibody is typically effective

• Secondary antibody: HRP-conjugated secondary antibodies at manufacturer-recommended dilutions (e.g., 1:50 for certain applications)

• Expected band size: Look for specific bands at approximately 37-38 kDa

• Membrane type: PVDF membranes have been successfully used for SULT1A1 detection

These parameters should be optimized for each laboratory and application as noted in scientific literature .

How can researchers effectively validate the specificity of their SULT1A1 antibodies?

A comprehensive validation approach includes:

• Multiple detection methods: Compare results across Western blot, IHC, and other applicable techniques

• Positive and negative controls: Include known SULT1A1-expressing tissues (liver) and low-expressing samples

• Molecular weight verification: Confirm band appearance at the expected 37-38 kDa

• Blocking peptide experiments: Demonstrate signal reduction when using specific blocking peptides

• Knockout/knockdown controls: When possible, include samples with SULT1A1 gene deletion or suppression

Statistical rigor in antibody validation is critical, as noted in research examining immunoblotting methods . Transparency in reporting validation parameters increases reproducibility across laboratories.

What storage conditions maintain optimal SULT1A1 antibody performance?

Based on manufacturer recommendations and research protocols:

• Short-term storage (up to 2 weeks): 2-8°C refrigeration

• Long-term storage (up to 12 months): -20°C to -70°C in small aliquots

• Avoid repeated freeze-thaw cycles

• Some preparations recommend reconstitution under sterile conditions

• Consider adding sodium azide (0.05-0.1% final concentration) to antibody solutions that don't already contain preservatives

Proper handling significantly impacts experimental reproducibility and antibody longevity.

How can researchers address SULT1A1 copy number variations in experimental design and data interpretation?

SULT1A1 exhibits significant copy number variations (CNVs) across populations:

Research approaches should:

• Consider genotyping subjects for SULT1A1 copy number using multiplex ligation-dependent probe amplification assays

• Stratify analysis based on copy number status

• Acknowledge that previous studies not accounting for CNVs may have misinterpreted SULT1A1 genotype-phenotype relationships

• Recognize that CNVs may explain inconsistent findings in case-control studies of SULT1A1 polymorphisms and disease risk

What considerations should be made when interpreting differences in SULT1A1 expression across ethnic populations?

When investigating population differences:

• Incorporate copy number analysis as standard practice

• Account for the higher frequency of increased SULT1A1 copy numbers in African-American subjects (63%) compared to Caucasians (26%)

• Note that approximately 5% of Caucasian subjects have a single SULT1A1 copy, while this genotype is rare in African-American populations

• Consider that ethnic differences in copy number may explain observed differences in SULT1A1 enzyme activity (e.g., higher basal platelet SULT1A1 activity in African-Americans)

These population differences have significant implications for pharmacogenetic studies and precision medicine approaches.

How can SULT1A1 antibodies be utilized in investigating drug metabolism phenotypes?

For pharmacogenomic applications:

• Combine antibody-based protein quantification with genotyping for comprehensive phenotype assessment

• Correlate SULT1A1 protein expression with enzymatic activity measurements

• Investigate tissue-specific expression patterns to understand drug metabolism capacity

• Consider that SULT1A1 antibodies can help identify individuals with varying sulfation capacity, which may predict response to drugs metabolized through this pathway (e.g., minoxidil)

• Design studies that correlate protein expression with functional outcomes in drug metabolism

What are common sources of variability in SULT1A1 antibody experiments and how can they be addressed?

Common challenges include:

• Genetic variability: SULT1A1 copy number differences and polymorphisms affect expression levels and potentially epitope recognition

• Tissue-specific expression: Expression varies significantly across tissues, requiring appropriate positive controls

• Antibody cross-reactivity: SULT1A1 shares sequence homology with other sulfotransferase family members

• Sample processing: Variations in protein extraction and sample preparation affect detection

Recommended solutions:

• Implement standardized protocols with detailed documentation

• Include multiple biological and technical replicates

• Use multiple antibodies targeting different epitopes of SULT1A1

• Perform careful antibody titration to determine optimal concentration

• Include genotype analysis when possible to account for genetic variation

How can researchers distinguish between SULT1A1 and other closely related sulfotransferase family members?

To ensure specificity:

• Select antibodies raised against unique regions of SULT1A1 (e.g., C-terminal regions) that have minimal sequence homology with other SULT family members

• Perform parallel experiments with antibodies specific to other SULT family members (SULT1B1, SULT1E1) to establish distinct expression patterns

• Consider complementary molecular approaches such as RT-PCR with isoform-specific primers

• Use recombinant SULT proteins as controls to verify antibody specificity

• When available, employ SULT1A1 knockout or knockdown models as negative controls

Researchers should be particularly careful to distinguish between SULT1A1, SULT1B1, and SULT1E1, as these have distinct substrate preferences but may be co-expressed in some tissues .

What statistical approaches are recommended for quantitative analysis of immunoblotting data for SULT1A1?

For rigorous quantitative analysis:

• Include appropriate sample sizes based on power calculations (literature reviews indicate many immunoblotting studies use inadequate sample sizes)

• Implement normalization strategies using housekeeping proteins or total protein staining

• Perform at least three independent biological replicates

• Consider using parametric tests (t-test, ANOVA) only after confirming data normality

• Report exact p-values rather than significance thresholds

• Include detailed methodology on image acquisition and quantification

A scoping review of statistical methods in immunoblotting revealed that many studies use inappropriate statistical approaches or fail to disclose their methods adequately . Transparent reporting of statistical procedures is essential for reproducibility.

How might SULT1A1 antibodies contribute to understanding the role of this enzyme in metabolic disorders?

Recent research suggests promising avenues:

• Investigating adipose tissue SULT1A1 expression in relation to metabolic phenotypes

• Exploring the connection between SULT1A1 activity and browning of white adipose tissue

• Examining how SULT1A1 levels correlate with body weight regulation and obesity resistance

• Developing tissue-specific conditional knockout models to clarify the role of SULT1A1 in different metabolic tissues

• Correlating SULT1A1 protein levels with metabolomic profiles

Emerging evidence indicates that Sult1a1 deletion in mice reduces body weight and increases browning of white adipose tissue, suggesting potential metabolic implications worthy of further investigation with antibody-based techniques .

What emerging applications exist for SULT1A1 antibodies in studying gut microbiota-host metabolic interactions?

SULT1A1 antibodies can facilitate research on:

• Detection of SULT1A1 expression in intestinal tissues in response to microbiome alterations

• Investigation of SULT1A1's role in metabolizing microbiota-derived metabolites such as 4-ethylphenol (4-EP)

• Examination of how microbial metabolites influence SULT1A1 expression and activity in the gut and liver

• Correlation of SULT1A1 levels with gut permeability and metabolite translocation

Recent research has identified SULT1A1's role in O-sulfonating 4-EP, a dietary tyrosine-derived metabolite produced by gut bacteria, with potential implications for brain function and development .

How can researchers leverage SULT1A1 antibodies in developing predictive biomarkers for drug response?

Promising applications include:

• Development of immunohistochemical assays to predict drug metabolism capacity in patient samples

• Correlation of SULT1A1 expression levels with clinical outcomes for drugs metabolized by this enzyme

• Integration of protein expression data with genetic information for more comprehensive pharmacogenomic profiling

• Investigation of SULT1A1 expression changes in response to drug exposure or disease states

• Exploration of SULT1A1 as a predictive biomarker for minoxidil response in hair loss treatment