Recombinant Bovine UPF0444 transmembrane protein C12orf23 homolog
Description
Definition and Classification
Recombinant Bovine UPF0444 transmembrane protein C12orf23 homolog is a protein derived from bovine sources through recombinant expression systems. The designation "UPF0444" refers to its classification within the Uncharacterized Protein Family 0444, indicating that at the time of initial classification, its precise functions remained to be fully characterized. This protein is also identified by alternative gene names including TMEM263, C12orf23, and C5H12orf23 in bovine species .
As a transmembrane protein, it is structurally integrated into cellular membranes, suggesting potential roles in cellular communication, transport processes, or maintenance of membrane integrity. The "C12orf23" portion of its name reflects its homology to a human protein originally identified as being encoded by an open reading frame on chromosome 12.
Evolutionary Conservation
The significant conservation of this protein across diverse vertebrate species—including humans, bovines, mice, chickens, and amphibians such as Xenopus—suggests that it likely serves fundamental biological functions. This evolutionary preservation indicates selective pressure to maintain the protein's structure and function across species divergence, further emphasizing its potential biological importance .
Commercial availability of recombinant forms from multiple species, including bovine, human, mouse, chicken, Xenopus, and zebrafish variants, facilitates comparative studies across evolutionary lineages. Such conservation presents intriguing opportunities for researchers to investigate whether this protein participates in core cellular processes common across vertebrates.
Comparison Across Species
The conservation of UPF0444 transmembrane protein C12orf23 homologs extends across multiple vertebrate lineages, with commercial reagents available for numerous species as shown in Table 1.
This conservation pattern suggests the protein likely maintains similar core functions across these diverse species while potentially acquiring species-specific adaptations.
Recombinant Expression Systems
The recombinant bovine UPF0444 transmembrane protein C12orf23 homolog is primarily produced using cell-free expression systems according to commercial product information . Cell-free expression systems offer significant advantages for the production of membrane proteins, which can be challenging to express in cellular systems due to potential toxicity, improper folding, or aggregation issues.
For related proteins or partial sequences, alternative expression platforms may include Escherichia coli, yeast, baculovirus, or mammalian cell systems, as indicated for other homologs . Each expression system presents distinct advantages depending on the intended downstream applications and required protein conformations.
Purification and Quality Control
Standard purification approaches for the recombinant bovine protein typically involve affinity chromatography, particularly for tagged variants. According to product specifications, the recombinant protein is characterized by a purity level greater than or equal to 85% as determined by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) .
Comparable proteins from other species, such as the Xenopus tropicalis homolog, achieve even higher purity levels (>90%) as determined by similar analytical methods . This high level of purity is essential for research applications to ensure experimental results are not influenced by contaminants or degradation products.
Potential Biological Functions
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Membrane organization and structural integrity
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Transmembrane transport of specific molecules
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Cell signaling or receptor functions
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Organelle-specific membrane processes
Research Applications
The recombinant bovine UPF0444 transmembrane protein C12orf23 homolog finds applications primarily in fundamental research investigating protein structure, function, and potential roles in cellular processes. Current applications include:
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Immunological Studies: The availability of specific antibodies against this protein facilitates detection methods such as Western blotting, immunohistochemistry, and immunofluorescence for studying expression patterns and localization in bovine tissues .
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Functional Analysis: Small interfering RNA (siRNA) products targeting the corresponding gene enable knockdown studies to investigate the consequences of reduced protein expression in cellular models .
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Structural Investigations: Purified recombinant protein can serve as a starting material for biophysical and structural studies aimed at understanding the three-dimensional conformation.
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Interaction Studies: The protein may be used in binding assays to identify potential interaction partners, helping to place it within specific cellular pathways.
Functional Genomics Approaches
Modern functional genomics tools present powerful approaches to investigate the biological roles of this protein:
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CRISPR/Cas9-mediated gene editing could generate bovine cell lines lacking the TMEM263 gene, allowing assessment of phenotypic consequences.
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Proteomics studies could identify interaction partners, placing this protein within specific cellular networks.
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Transcriptomics analysis following protein knockdown could reveal affected pathways and downstream genes.
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Cellular localization studies using fluorescently tagged variants would determine precise subcellular distribution, providing functional clues.
Translational Research Potential
Investigation of this protein's role in bovine health and disease could yield valuable insights for veterinary medicine and animal science. Additionally, comparative studies between bovine and human homologs might reveal conserved functions relevant to human health, potentially identifying new therapeutic targets for conditions involving transmembrane protein dysfunction.
Product Specs
Note: We prioritize shipping the format currently in stock. However, if you have specific requirements for the format, please indicate them during order placement. We will fulfill your request whenever possible.
Note: All our proteins are shipped with standard blue ice packs. If you require dry ice shipping, please inform us in advance, as additional fees will apply.
Generally, the shelf life for liquid form is 6 months at -20°C/-80°C. For lyophilized form, the shelf life is 12 months at -20°C/-80°C.
Target Background
Q&A
What is UPF0444 transmembrane protein C12orf23 homolog?
UPF0444 transmembrane protein C12orf23 homolog, also known as transmembrane protein 263 (TMEM263), is a membrane-spanning protein initially identified in chromosomal region 12 in humans with homologs present across various species. In bovine systems, this protein is encoded by the TMEM263 gene (alternate gene names: C12orf23, C5H12orf23) and represents a conserved transmembrane protein whose precise biological function remains under investigation . The protein belongs to the UPF (Uncharacterized Protein Family) classification, specifically UPF0444, indicating a protein family with conserved sequence but incompletely characterized function.
What is the amino acid sequence and structural properties of this protein?
The complete bovine TMEM263 protein shares significant homology with other mammalian variants. While the exact bovine sequence is not fully detailed in the search results, the homologous Xenopus tropicalis version consists of 114 amino acids with the sequence: MSQTEKIEEAVPSYLCEEPPEGTVKDHPQQQPGMISRVTGGIFSMTKGAVGATIGGVAWIGGKSYEVTKTAVTSVPSIGVGIVKGSVSAVTGSVAAVGSVVSSKVSGKKKDKSD . Structural analysis suggests multiple transmembrane domains characteristic of integral membrane proteins, with hydrophobic regions spanning the lipid bilayer.
What expression systems are available for this recombinant protein?
Recombinant bovine UPF0444 transmembrane protein C12orf23 homolog can be expressed in multiple heterologous systems, including:
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E. coli bacterial expression systems
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Yeast-based expression platforms
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Baculovirus-insect cell systems
The choice of expression system significantly impacts protein folding, post-translational modifications, and functional characteristics, with mammalian systems generally providing the most native-like protein conformation for bovine proteins.
What are optimal storage conditions for maintaining protein stability?
Optimal storage of recombinant bovine UPF0444 transmembrane protein involves multiple considerations to preserve structural integrity and biological activity:
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Long-term storage: -20°C to -80°C in appropriate buffer containing glycerol
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Working aliquots: 4°C for up to one week
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Avoid repeated freeze-thaw cycles which can compromise protein structure
For lyophilized preparations, proper reconstitution in deionized sterile water to a concentration of 0.1-1.0 mg/mL is recommended, with addition of 5-50% glycerol (final concentration) for enhanced stability .
How can researchers verify protein quality and purity?
Quality control for recombinant bovine UPF0444 transmembrane protein typically involves multiple analytical approaches:
When working with this protein, researchers should independently verify purity via SDS-PAGE before experimental use, particularly when investigating novel functional properties.
What experimental approaches are suitable for studying protein-protein interactions?
For investigating interactions between bovine UPF0444 transmembrane protein and potential binding partners, several complementary techniques can be employed:
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Co-immunoprecipitation with tagged recombinant protein as bait
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Pull-down assays using purified recombinant protein
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Proximity labeling methods (BioID, APEX) for identifying neighboring proteins
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FRET/BRET approaches for real-time interaction monitoring in live cells
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Surface plasmon resonance for quantitative binding kinetics
When designing such experiments, consider using approaches similar to those applied in studies of importin α binding partners, which have successfully identified specific protein interactions through complementary methodologies .
How does the bovine UPF0444 transmembrane protein compare with homologs from other species?
Comparative analysis reveals evolutionary conservation across vertebrate species with functionally significant variations:
These comparative data suggest functional conservation with species-specific adaptations, providing valuable research opportunities for evolutionary and functional studies.
What is known about the cellular localization and trafficking of this protein?
While specific localization data for bovine UPF0444 transmembrane protein is limited in the provided search results, transmembrane proteins typically undergo specific trafficking pathways. Researchers investigating this protein should consider:
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Utilizing fluorescently-tagged constructs to track subcellular localization
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Employing cell fractionation studies to determine membrane association
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Investigating potential nuclear localization signals and import mechanisms, considering the established importin α-mediated nuclear transport pathways
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Examining post-translational modifications that might regulate localization
Research approaches similar to those used for studying importin-mediated protein transport could provide insights into the trafficking mechanisms of this transmembrane protein .
What are common challenges when working with transmembrane proteins like UPF0444?
Transmembrane proteins present distinct experimental challenges requiring specialized approaches:
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Solubility issues: The hydrophobic transmembrane domains can cause aggregation during purification and handling. Maintain appropriate detergent concentrations throughout experimental procedures.
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Functional reconstitution: For activity assays, reconstitution into appropriate lipid environments or membrane mimetics may be necessary to preserve native conformation.
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Structural analysis limitations: Traditional structural determination methods often yield poor results with transmembrane proteins. Consider specialized approaches like cryo-EM or NMR with isotopic labeling.
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Expression system selection: Prokaryotic systems may not provide proper folding or post-translational modifications. For functional studies, mammalian expression systems often provide superior results despite lower yields.
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Buffer optimization: Detergent selection, ionic strength, pH, and glycerol concentration all significantly impact protein stability and should be empirically optimized.
How can researchers differentiate between specific and non-specific effects in functional studies?
When investigating the biological function of recombinant bovine UPF0444 transmembrane protein:
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Include appropriate negative controls (empty vector, unrelated transmembrane protein)
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Perform concentration-dependent experiments to establish dose-response relationships
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Utilize competing peptides or antibodies to demonstrate specificity
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Employ genetic approaches (siRNA, CRISPR) to confirm findings from protein addition/inhibition studies
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Compare results across multiple experimental systems and cell types
Particularly challenging is distinguishing specific interactions from non-specific membrane associations, requiring rigorous controls and complementary methodological approaches.
What are promising research applications for bovine UPF0444 transmembrane protein?
Based on current understanding and available tools, several research directions appear particularly promising:
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Comparative analysis with human C12orf23 homolog to elucidate evolutionarily conserved functions
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Investigation of protein-protein interaction networks using pull-down assays and mass spectrometry
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Examination of potential roles in cellular signaling pathways
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Analysis of tissue-specific expression patterns and their physiological significance
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Exploration of potential roles in developmental processes based on expression in model organisms like Xenopus
The protein has been implicated in RNA processing, chromosome organization, and chromatin modification pathways based on interaction studies of related proteins , suggesting potential nuclear functions despite its transmembrane classification.
What technological advances might enhance research with this protein?
Emerging technologies likely to advance research with bovine UPF0444 transmembrane protein include:
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Cryo-electron microscopy for high-resolution structural determination
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Advanced mass spectrometry techniques for improved interaction profiling
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Single-molecule imaging approaches for tracking protein dynamics
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CRISPR-based genomic engineering for studying function in native contexts
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Computational modeling for predicting functional domains and interaction sites
Integration of these technological approaches with traditional biochemical and cell biological methods will provide comprehensive insights into the biological function of this relatively uncharacterized transmembrane protein.
