Recombinant Absidia glauca Actin-1 (ACT1) is produced in E. coli and expressed as a partial-length protein (1-140 amino acids). The protein carries an N-terminal 6xHis-tag and a C-terminal Myc-tag, which streamline purification and detection processes. SDS-PAGE analysis confirms that the protein achieves a purity level exceeding 85%, suggesting reliable performance in research applications.
Actin-1 from Absidia glauca appears to be a key component of the cytoskeleton, playing what seems to be a crucial role in cell structure and motility. Actin proteins are integral to various cellular processes. These include maintaining cell shape, enabling intracellular transport, and supporting cell division. Such functions make actin an important focus in studies related to cell biology and dynamics.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
Absidia glauca Actin-1 (ACT1) is a cytoskeletal protein that requires precise folding, proper ATP-binding domain formation, specific tertiary structure, and polymerization capability for its functional activity. The E. coli expression system cannot provide the eukaryotic folding environment or post-translational modifications required for actin functionality. The partial fragment (1-140aa) represents only the N-terminal region and lacks critical C-terminal domains essential for actin polymerization, cofilin binding, and full functional activity. The dual N-terminal 6xHis-tag and C-terminal Myc-tag may sterically interfere with the protein's functional domains and structural integrity. The probability of correct folding with functional actin activity is extremely low.
1. Antibody Development and Characterization
This application has limited utility. While antibodies can be generated against this specific 1-140aa region, they will not recognize conformational epitopes of full-length actin and may not bind native actin in fungal cells. The immune response may predominantly target the foreign tags.
2. Biochemical Characterization of Fungal Actin Properties
Basic biophysical analysis can be performed, but will not reflect native actin properties. It provides only a basic characterization of this fragment. The 140aa fragment is too short to form functional actin domains, and the results will describe an artificial peptide rather than actin biochemistry. The tags will dominate the physical properties.
Final Recommendation & Action Plan
This 140aa actin fragment with dual tags is fundamentally unsuitable for meaningful actin research due to its partial nature (representing only ~37% of the full-length protein) and inability to form functional actin domains. The protein should not be used for functional studies as they would yield scientifically invalid results. For reliable actin research, use a full-length protein expressed in eukaryotic systems that supports proper folding, ATP-binding capability, and polymerization competence.
