SPAC2F3.07c Antibody

Product Information and Availability

The SPAC2F3.07c antibody is commercially available from suppliers like Cusabio under product code CSB-PA522634XA01SXV. According to product listings, this antibody specifically targets the SPAC2F3.07c protein from Schizosaccharomyces pombe (strain 972 / ATCC 24843), commonly known as fission yeast. The antibody is typically provided in volumes of 2ml or 0.1ml, suitable for various laboratory applications .

The target protein is identified by UniProt accession number O14090, establishing standardized identification that enables researchers to cross-reference information about this protein across multiple databases and research platforms .

Target Protein Characteristics

The SPAC2F3.07c protein is classified as an "Uncharacterized Protein C2F3.07C" in Schizosaccharomyces pombe. According to available information, the full-length protein consists of 101 amino acids . For research purposes, recombinant versions of this protein are available with histidine tags (His-tagged) to facilitate protein purification and detection in experimental settings.

The recombinant form of this protein (catalog number RFL32818SF from Creative BioMart) is produced in Escherichia coli expression systems . These recombinant proteins serve important roles as positive controls in antibody validation, as antigens for raising new antibodies, or as reagents in protein interaction studies.

Western Blotting Applications

Western blotting represents one of the primary applications for antibodies in fission yeast research. While specific validation data for the SPAC2F3.07c antibody is not detailed in the available search results, similar antibodies for fission yeast proteins are typically employed in Western blotting at dilutions around 1:1000 .

In Western blotting protocols, the SPAC2F3.07c antibody would enable researchers to:

• Detect SPAC2F3.07c protein expression in cell lysates

• Monitor protein levels under various experimental conditions

• Verify knockout or knockdown efficiency in genetic studies

• Confirm protein size and potential post-translational modifications

Immunoprecipitation Studies

Immunoprecipitation (IP) is a valuable technique for isolating specific proteins and their interaction partners. In fission yeast research, IPs are commonly used to study protein complexes and modifications . The SPAC2F3.07c antibody could potentially be utilized for:

• Isolating the native SPAC2F3.07c protein from yeast cell extracts

• Identifying proteins that interact with SPAC2F3.07c (co-immunoprecipitation)

• Investigating post-translational modifications of the target protein

Standard IP protocols for fission yeast proteins typically include validation steps such as Western blotting of a fraction of the immunoprecipitated material to confirm successful isolation of the target protein .

Potential for Localization Studies

Although not explicitly mentioned in the search results for this specific antibody, immunofluorescence microscopy represents another potential application. This technique would allow researchers to visualize the subcellular localization of the SPAC2F3.07c protein, providing valuable insights into its potential function.

The subcellular distribution pattern of SPAC2F3.07c (whether nuclear, cytoplasmic, mitochondrial, or membrane-associated) could provide important clues about its biological role. For uncharacterized proteins, localization data often serves as the first step toward understanding protein function.

Antibody Generation Approaches

While the specific production method for the SPAC2F3.07c antibody is not detailed in the search results, established protocols for generating antibodies against fission yeast proteins typically involve:

1. Expression of recombinant protein antigens in bacterial systems

2. Purification using affinity chromatography techniques

3. Immunization of host animals

4. Screening and selection of antibody-producing cells

5. Antibody purification and validation

For example, the generation of antibodies against the fission yeast transcription factor Sre1 involved expressing recombinant antigen in E. coli with a polyhistidine tag, purifying via nickel-nitrilotriacetic acid-agarose, and immunizing either rabbits (for polyclonal antibodies) or mice (for monoclonal antibodies) .

Validation Strategies

Antibody validation is essential to ensure specificity and reliability in experimental applications. Standard validation approaches for fission yeast antibodies include:

1. Testing reactivity against recombinant target protein

2. Comparing detection between wild-type and gene deletion strains

3. Verifying the expected molecular weight by Western blotting

4. Confirming specific binding pattern in immunofluorescence studies

The search results describe validation of Sre1 antibodies through "loss of immunoreactivity in an sre1Δ strain" , demonstrating the importance of gene deletion strains in confirming antibody specificity.

Role in Characterizing Uncharacterized Proteins

The SPAC2F3.07c antibody represents an important tool for studying one of many uncharacterized proteins in the fission yeast proteome. Schizosaccharomyces pombe contains numerous open reading frames without assigned functions, and antibodies enable researchers to begin characterizing these proteins through expression analysis, localization studies, and interaction mapping.

The systematic characterization of previously uncharacterized proteins contributes to comprehensive understanding of fission yeast biology and can reveal novel components of established cellular pathways or entirely new functional modules.

Comparison with Other Fission Yeast Antibodies

The search results list several other antibodies against S. pombe proteins available through the same supplier, including SPAC1039.04, SPAC821.13c, SPAC821.03c, and others . This indicates ongoing research interest in developing reagents for studying the fission yeast proteome comprehensively.

The availability of antibodies targeting multiple uncharacterized proteins enables comparative studies that may reveal functional relationships or coordinated regulation among these proteins. For instance, proteins that co-localize or demonstrate similar expression patterns under specific conditions may function in related biological processes.

Integration with Fission Yeast Research

Fission yeast serves as an important model organism for studying fundamental cellular processes, including cell cycle regulation, stress responses, and gene expression. The search results mention specific examples of fission yeast protein research, such as studies of the Sty1 MAP kinase and the transcription factor Atf1 involved in stress responses .

As a research tool, the SPAC2F3.07c antibody contributes to this broader research landscape by enabling characterization of additional components in the fission yeast proteome. Understanding the function of uncharacterized proteins like SPAC2F3.07c may reveal new aspects of established cellular mechanisms or entirely novel biological functions.

Knowledge Gaps

The primary limitation evident from the search results is the uncharacterized nature of the SPAC2F3.07c protein itself. Without established knowledge of the protein's function, subcellular localization, or interaction partners, the full utility of the antibody in specific research contexts remains to be determined.

Additional knowledge gaps may include:

• Validated applications beyond standard Western blotting

• Cross-reactivity profiles with related proteins

• Optimal conditions for various experimental protocols

• Expression patterns under different physiological conditions

Future Research Opportunities

Future research utilizing the SPAC2F3.07c antibody could address these knowledge gaps and advance understanding of the target protein's function. Potential research directions include:

1. Expression profiling under various stress conditions and throughout the cell cycle

2. Subcellular localization studies using immunofluorescence microscopy

3. Identification of interaction partners through co-immunoprecipitation and mass spectrometry

4. Correlation of protein dynamics with phenotypes observed in genetic studies

5. Comparative analysis with homologous proteins in other yeast species or higher eukaryotes

Integration with Emerging Technologies

The search results mention the Patent and Literature Antibody Database (PLAbDab), which serves as an evolving reference for antibody sequences and structures . This highlights the ongoing advancement of antibody research resources.

Future technological developments that could enhance research involving the SPAC2F3.07c antibody might include:

• Advanced imaging techniques for better visualization of protein dynamics

• Integration with proteomics approaches for comprehensive characterization

• CRISPR-based tagging strategies to complement antibody-based detection

• Computational prediction of protein functions based on structural analysis