SULT1A2 Antibody, Biotin conjugated

Introduction to SULT1A2 Antibody, Biotin Conjugated

SULT1A2 Antibody, Biotin conjugated is an immunological reagent designed for the specific detection and analysis of the SULT1A2 protein in biological samples. This antibody targets specific amino acid sequences within the human SULT1A2 protein and is chemically linked to biotin molecules to facilitate detection through biotin-streptavidin interactions in various immunological assays. Different variants of this antibody are commercially available, targeting distinct epitopes within the SULT1A2 protein, particularly in the C-terminal region between amino acids 195-284 or 258-286 .

The biotin conjugation significantly enhances the utility of these antibodies in research applications by providing a strong, stable linkage for detection systems. The exceptional binding affinity between biotin and streptavidin (or avidin) makes these conjugated antibodies particularly valuable in sensitive detection methods where signal amplification is required.

Production and Host Systems

SULT1A2 antibodies with biotin conjugation are predominantly produced in rabbit host systems through immunization with synthetic peptides or recombinant protein fragments. The production typically involves immunizing rabbits with a KLH (Keyhole Limpet Hemocyanin) conjugated synthetic peptide corresponding to specific amino acid sequences from the C-terminal region of human SULT1A2 . These antibodies are polyclonal in nature, consisting of a heterogeneous mixture of immunoglobulins that recognize different epitopes within the target region .

Epitope Targeting and Specificity

The commercially available SULT1A2 antibodies with biotin conjugation target specific regions of the SULT1A2 protein:

These antibodies demonstrate specific reactivity against human SULT1A2, with limited or no reported cross-reactivity with other species or related sulfotransferase family members .

Purification and Quality Control

The biotin-conjugated SULT1A2 antibodies undergo rigorous purification processes to ensure high quality and specificity. They are typically affinity purified or protein G purified to a purity level exceeding 95% . This purification process removes non-specific antibodies and other contaminants that might interfere with experimental results, enhancing the signal-to-noise ratio in detection applications.

Immunoassay Applications

SULT1A2 antibodies with biotin conjugation are particularly valuable in enzyme-linked immunosorbent assays (ELISA), offering enhanced sensitivity through biotin-streptavidin amplification systems . The biotin conjugation allows for versatile detection strategies, including colorimetric, fluorescent, or chemiluminescent methods when paired with appropriate streptavidin-conjugated reporter molecules.

Western blotting (WB) represents another significant application, where these antibodies can detect denatured SULT1A2 protein separated by gel electrophoresis . The biotin conjugation facilitates signal amplification, improving detection limits for low-abundance proteins.

Experimental Considerations

For optimal results in immunoassays using biotin-conjugated SULT1A2 antibodies, researchers should consider several factors:

1. Sample preparation methods that preserve protein integrity

2. Potential endogenous biotin interference in certain biological samples

3. Blocking strategies to minimize non-specific binding

4. Appropriate controls to validate specificity and performance

Biological Significance of SULT1A2

Understanding the biological context of SULT1A2 is essential for meaningful application of these antibodies in research. SULT1A2 belongs to the sulfotransferase family and plays critical roles in various biological processes.

Enzymatic Function

SULT1A2 functions as a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as a sulfonate donor to catalyze the sulfate conjugation of various substrates, including catecholamines, phenolic drugs, and neurotransmitters . This enzymatic activity represents a critical detoxification pathway in human metabolism.

Role in Drug Metabolism

SULT1A2 is responsible for the sulfonation and activation of pharmaceutically relevant compounds such as minoxidil . This highlights its importance in pharmacokinetics and drug efficacy studies, where SULT1A2 antibodies can provide valuable insights into protein expression and localization.

Cancer Research Implications

Research indicates that SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products, potentially modulating cancer risk . Biotin-conjugated SULT1A2 antibodies therefore represent important tools in cancer research, enabling investigations into the role of this enzyme in carcinogenesis and its potential as a biomarker or therapeutic target.

Assay Optimization

Despite their utility, biotin-conjugated SULT1A2 antibodies require careful optimization for specific applications. Researchers should consider:

1. Appropriate dilution ratios for optimal signal-to-noise ratio

2. Incubation times and temperatures

3. Washing stringency to minimize background

4. Detection system compatibility with experimental design

Potential Interferences

Endogenous biotin in biological samples can potentially interfere with biotin-streptavidin detection systems. This is particularly relevant when working with tissues or cell types with high biotin content, such as liver, kidney, or brain tissues. Researchers should implement appropriate blocking strategies or consider alternative detection methods in such cases.

Future Research Directions

The continued development and application of SULT1A2 antibodies with biotin conjugation promise to advance our understanding of this enzyme's role in various physiological and pathological processes. Emerging technologies in antibody engineering and detection systems may further enhance the sensitivity, specificity, and versatility of these research tools.

Future research directions may include:

1. Development of antibodies targeting specific SULT1A2 variants or post-translational modifications

2. Application in multiplexed detection systems for comprehensive pathway analysis

3. Investigation of SULT1A2 as a biomarker in precision medicine approaches

4. Utilization in high-throughput screening for drug development