Code | CSB-EP781430DOA |
Abbreviation | Recombinant Mouse-ear cress GIF1 protein |
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Size | $388 |
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Recombinant Arabidopsis thaliana GRF1-interacting factor 1 (GIF1) is produced in an E. coli expression system, spanning the complete protein sequence from amino acids 1 to 210. The protein carries an N-terminal 6xHis-KSI tag, which appears to simplify purification and detection processes. SDS-PAGE analysis indicates purity levels above 85%, suggesting this recombinant GIF1 may be appropriate for various research applications. This product is intended for research use only.
GIF1, or GRF1-interacting factor 1, is a protein from Arabidopsis thaliana that seems to play an important role in regulating plant growth and development. It likely interacts with growth-regulating factors, potentially influencing pathways that are crucial for morphological adaptations and responses to environmental stimuli. Studying GIF1's interactions and functions might provide valuable insights into plant biology and could aid researchers exploring plant developmental processes.
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.
1. Protein-Protein Interaction Studies with GRF Transcription Factors
This recombinant GIF1 protein can be used to investigate its interactions with Growth-Regulating Factor (GRF) transcription factors in Arabidopsis thaliana through in vitro binding assays. The N-terminal 6xHis-KSI tag allows for purification and immobilization in pull-down experiments designed to identify and characterize GRF binding partners. Co-immunoprecipitation studies using the tagged GIF1 may help researchers map the specific domains involved in GRF-GIF1 complex formation. These interaction studies appear fundamental for understanding the molecular mechanisms of plant growth regulation and transcriptional control networks.
2. Antibody Development and Validation
The purified recombinant GIF1 protein serves as what appears to be an ideal antigen for generating specific antibodies against Arabidopsis GIF1. The high purity level (>85%) and full-length nature of the protein likely ensure comprehensive epitope coverage for both polyclonal and monoclonal antibody production. These antibodies can subsequently be validated using the same recombinant protein in Western blot, ELISA, and immunofluorescence applications. The His-tagged protein also seems to make possible the development of sandwich ELISA assays for quantitative detection of GIF1 in plant extracts.
3. Biochemical Characterization and Structural Studies
This recombinant protein makes possible detailed biochemical analysis of GIF1 properties including thermal stability, pH sensitivity, and cofactor requirements. Researchers can apply the purified protein to analytical techniques such as dynamic light scattering, circular dichroism spectroscopy, and mass spectrometry to characterize its biophysical properties. Size exclusion chromatography experiments may help determine the oligomerization state of GIF1 in solution. These studies could provide foundational data for understanding GIF1 structure-function relationships in plant biology research.
4. His-Tag Affinity-Based Functional Assays
The N-terminal 6xHis-KSI tag makes possible the development of nickel-affinity based assays to study GIF1 function and regulation. The tagged protein can be immobilized on nickel-coated surfaces for screening potential small molecule modulators or identifying novel protein partners through affinity chromatography. Pull-down assays using the His-tagged GIF1 might isolate associated protein complexes from Arabidopsis cell lysates for mass spectrometry analysis. These tag-assisted approaches appear to support high-throughput screening and discovery of GIF1-interacting molecules in plant research applications.
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