KIAA1467 is a human protein-coding gene that produces what is currently classified as an uncharacterized protein . The designation "uncharacterized" indicates that the precise biological function of this protein has not yet been fully determined through experimental validation . The protein is also known by the alternative name FAM234B (family with sequence similarity 234 member B), suggesting its potential relationship to other proteins within the same family grouping .
Recombinant Human Uncharacterized protein KIAA1467 refers specifically to artificially produced versions of this protein created through various expression systems for research and characterization purposes. These recombinant versions enable scientists to study the protein's properties, interactions, and potential functions in controlled laboratory settings despite its endogenous function remaining undetermined .
KIAA1467 is classified as a member of the FAM234 family of proteins, specifically member B (FAM234B) . While the detailed three-dimensional structure of the protein has not been extensively characterized in the available literature, recombinant versions are produced and purified to high standards, suggesting the protein possesses stable structural characteristics amenable to in vitro production and analysis .
Recombinant Human Uncharacterized protein KIAA1467 can be produced through several different expression systems, each offering particular advantages for protein production. The available expression systems include:
| Expression Host | Advantages | Typical Applications |
|---|---|---|
| E. coli | High yield, cost-effective, rapid production | Basic biochemical studies, antibody production |
| Yeast | Post-translational modifications, higher eukaryotic system | Functional studies requiring some modifications |
| Baculovirus | Complex eukaryotic modifications, high yield | Structural studies, functional assays |
| Mammalian Cell | Full range of human-like post-translational modifications | Studies requiring native-like protein structure |
| Cell-Free Expression | Rapid production, avoids cellular toxicity issues | Quick screening, structural studies |
As documented in commercial product listings, recombinant KIAA1467 has been successfully produced in each of these expression systems, with purity levels consistently reaching or exceeding 85% as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) .
Recombinant KIAA1467 protein undergoes rigorous purification processes to ensure high quality for research applications. The standard purity level for commercial preparations is greater than or equal to 85% as determined by SDS-PAGE analysis . This analytical technique separates proteins based on their molecular weight, allowing for the assessment of sample purity and the identification of potential contaminants.
For antibodies developed against KIAA1467, even higher purity standards are implemented, with protein G purification resulting in preparations exceeding 95% purity . These high-purity preparations are essential for applications requiring specific detection of the target protein without cross-reactivity or background interference.
A variety of research reagents targeting KIAA1467 have been developed to facilitate its study. The primary categories include:
Recombinant Proteins:
Antibodies:
These reagents provide critical tools for researchers investigating the expression, localization, and function of KIAA1467 in various experimental systems.
The available antibodies against KIAA1467 have been validated for multiple experimental applications, enabling diverse approaches to studying this protein. These applications include:
| Application | Description | Information Provided |
|---|---|---|
| ELISA (EIA) | Quantitative detection of KIAA1467 in solution | Protein concentration, presence in samples |
| Western Blot (WB) | Detection of denatured protein by size | Molecular weight, expression levels |
| Immunohistochemistry (IHC) | Detection in fixed tissue sections | Tissue distribution, cellular localization |
| Immunofluorescence (IF) | Fluorescent detection in cells/tissues | Subcellular localization, co-localization studies |
These experimental techniques provide complementary approaches to investigating KIAA1467 expression, allowing researchers to examine its presence at the protein level across different biological contexts .
While the specific function of KIAA1467 remains uncharacterized, research into compounds that can indirectly activate its function suggests potential involvement in established signaling networks. These interactions may provide clues about the protein's physiological role and regulatory mechanisms .
KIAA1467 appears to be influenced by signaling cascades involving cyclic adenosine monophosphate (cAMP) and protein kinase pathways. Specific compounds that can indirectly enhance KIAA1467 activity operate through these established cellular signaling mechanisms, suggesting the protein may function within these regulatory networks .
Several compounds have been identified as potential indirect activators of KIAA1467 function through their effects on interconnected signaling pathways:
| Activator | Primary Target | Mechanism | Potential Effect on KIAA1467 |
|---|---|---|---|
| Forskolin | Adenylate cyclase | Increases cAMP levels, enhancing PKA activity | Indirect activation through PKA-dependent pathways |
| PMA (Phorbol 12-myristate 13-acetate) | Protein Kinase C (PKC) | Activates PKC, involved in numerous signaling pathways | Indirect influence through PKC-mediated signaling networks |
| SB 203580 | p38 MAPK | Inhibits p38 MAPK pathway | May enhance KIAA1467 activity through compensatory mechanisms |
The identification of these indirect activators provides valuable insights into the potential regulatory networks governing KIAA1467 function, suggesting it may be influenced by or participate in PKA and PKC signaling pathways .
KIAA1467 appears to be conserved across multiple species, suggesting important biological functions that have been maintained throughout evolution. Homologs of the human KIAA1467 protein have been identified in several other species:
Mouse: Identified as Kiaa1467 (alternative names: Fam234b, mKIAA1467, 8430419L09Rik)
Chicken: Referenced as "Uncharacterized protein KIAA1467 homolog" (gene identifier: RCJMB04_14d19)
Adelie penguin (Pygoscelis adeliae): Classified as "family with sequence similarity 234 member B"
The conservation of this protein across diverse vertebrate species suggests it may play a fundamental biological role that has been maintained through evolutionary history, despite its specific function remaining uncharacterized in current research literature.
The Adelie penguin homolog of KIAA1467 features an open reading frame (ORF) sequence of 1836 base pairs, encoding the protein-coding region . While detailed sequence comparisons between human KIAA1467 and its homologs in other species are not explicitly provided in the available search results, the consistent classification of these proteins within the FAM234B family suggests significant sequence similarity and likely functional conservation across species.
This evolutionary conservation provides an important context for understanding the potential significance of KIAA1467, as proteins maintained across diverse species often perform essential cellular functions that have been selected for throughout evolutionary history.
Despite the commercial availability of recombinant KIAA1467 and related research tools, the protein remains classified as "uncharacterized," indicating significant gaps in our understanding of its biological function . This classification reflects the current limitations in research regarding:
Precise biological function and physiological role
Detailed structural characterization
Comprehensive tissue expression patterns
Direct interaction partners and regulatory mechanisms
Involvement in specific disease processes or cellular pathways
These knowledge gaps represent important opportunities for future research to elucidate the functions of this evolutionarily conserved protein.
Based on the available information, several promising research directions could advance our understanding of KIAA1467:
Functional characterization through gene editing and knockdown studies
Detailed structural analysis using crystallography or cryo-electron microscopy
Protein interaction studies to identify binding partners
Investigation of tissue-specific expression patterns and regulation
Exploration of the signaling pathways influenced by the indirect activators
Comparative studies across species to identify conserved functional domains
The availability of recombinant proteins and specific antibodies provides essential tools to support these research directions , while the identified indirect activators offer potential experimental approaches for modulating KIAA1467 activity in functional studies .
KIAA1467 is the historical designation for a protein now officially known as FAM234B (family with sequence similarity 234 member B). It is a protein-coding gene that remains relatively uncharacterized in terms of its complete biological function. The gene has been assigned Gene ID 57613 in the NCBI database, with the most recent update recorded on March 26, 2025 . When designing experiments or searching literature, researchers should use both designations (KIAA1467 and FAM234B) to ensure comprehensive coverage, as older literature may exclusively reference the KIAA1467 designation while newer publications likely use the FAM234B nomenclature. This dual designation approach is particularly important when conducting systematic reviews or meta-analyses of existing research on this protein.
KIAA1467/FAM234B is located on the short arm of chromosome 12 at position p13.1 (12p13.1). The precise genomic coordinates in the current human genome assembly (NC_000012.12) are 13044381 to 13083449 . The gene contains 13 exons, making it a moderately complex gene structure. When designing primers for genomic PCR or CRISPR-Cas9 targeting strategies, researchers should account for this multi-exonic structure and consider the potential for alternative splicing. The genomic context may influence regulatory elements controlling expression; therefore, when studying transcriptional regulation, consider examining the flanking regions for potential promoter elements and transcription factor binding sites.
Based on recent computational predictions, KIAA1467/FAM234B is likely localized to three main subcellular compartments: the Golgi apparatus, cellular membranes, and the microtubule organizing center . This predicted localization pattern suggests potential involvement in protein trafficking, membrane dynamics, or cytoskeletal organization. When designing immunocytochemistry experiments, researchers should optimize protocols for these subcellular compartments, potentially using markers such as GM130 (Golgi), Na+/K+-ATPase (plasma membrane), or γ-tubulin (centrosome/MTOC) as co-localization references. Differential centrifugation and subcellular fractionation approaches would be valuable for biochemical validation of these localization predictions.
The open reading frame (ORF) of human KIAA1467/FAM234B consists of 1866 base pairs , which corresponds to a protein of approximately 622 amino acids. While the complete three-dimensional structure has not been definitively resolved, bioinformatic analyses suggest domain organizations that may inform functional studies. When working with recombinant systems, researchers should note that commercially available clones typically contain the full ORF, such as the expression-ready lentiviral construct that incorporates a mGFP tag for visualization and tracking . When designing truncation constructs to study domain-specific functions, careful consideration of predicted domain boundaries will be essential to avoid disrupting functional elements.
For mammalian expression, lentiviral vector systems have proven effective for KIAA1467/FAM234B expression. Commercially available constructs such as the pLenti-C-mGFP-P2A-Puro vector system offer several advantages :
| Vector Feature | Research Benefit | Methodological Consideration |
|---|---|---|
| mGFP Tag | Visualization of protein localization and trafficking | C-terminal tag may affect localization; verify with untagged construct |
| P2A-Puro | Selection marker for stable cell line generation | Maintain puromycin at optimal concentration (cell line dependent) |
| Lentiviral delivery | High transduction efficiency in diverse cell types | Requires BSL-2 safety practices; consider non-viral alternatives for sensitive applications |
For biochemical studies requiring larger protein quantities, bacterial or insect cell expression systems may be considered, though careful optimization of codon usage and potential inclusion of solubility-enhancing tags (MBP, SUMO) may be necessary due to the membrane association properties of the protein.
Given the limited characterization of this protein, a multi-pronged approach is recommended:
Transcript Detection: Design qRT-PCR primers spanning exon-exon junctions, preferably across exons that are conserved across potential splice variants. Consider RNAscope for spatial transcript detection in tissue sections.
Protein Detection: Commercial antibodies should be rigorously validated using positive controls (overexpression systems) and negative controls (CRISPR knockout cells). Western blotting protocols should be optimized for membrane proteins, potentially incorporating specialized detergents (CHAPS, DDM) for efficient extraction.
Functional Assays: Since KIAA1467/FAM234B is predicted to localize to the Golgi and membrane compartments, consider trafficking assays such as RUSH (Retention Using Selective Hooks) to study its dynamics in living cells.
When working with commercially available clones like the RC206342L4 construct , proper reconstitution and validation are critical:
Reconstitution Protocol:
Validation Steps:
Restriction enzyme digestion to confirm vector integrity
Sanger sequencing of the insert to verify sequence fidelity
Protein expression verification via Western blot and fluorescence microscopy (for GFP-tagged constructs)
Functional validation relevant to predicted localization (Golgi/membrane trafficking assays)
For sterile applications, filtration with a 0.22 μm filter is recommended as commercial plasmid preparations are not guaranteed sterile .
Given the predicted localization to multiple cellular compartments, a combination of approaches is recommended:
Proximity-Based Methods:
BioID or TurboID fusion constructs for proximity labeling in living cells
APEX2 fusion for electron microscopy-compatible proximity labeling
These approaches are particularly valuable for membrane-associated proteins where traditional co-IP methods may be challenging
Co-Immunoprecipitation Strategies:
Crosslinking protocols optimized for membrane proteins (DSP, DTSSP)
Detergent optimization panel to maintain protein-protein interactions while solubilizing membrane components
Sequential co-IP for complex isolation and analysis
Functional Validation:
FRET/BRET for direct interaction monitoring in living cells
Colocalization studies with super-resolution microscopy
Functional rescue experiments in knockout backgrounds
CRISPR-Cas9 Gene Editing:
Design multiple guide RNAs targeting early exons to ensure functional knockout
Consider conditional knockout strategies (floxed alleles) if constitutive knockout proves lethal
For precise modification, HDR templates can introduce specific mutations or tags at endogenous loci
RNAi Approaches:
siRNA pools targeting different regions to minimize off-target effects
shRNA for stable knockdown studies with appropriate non-targeting controls
Consider inducible systems for temporal control of knockdown
Overexpression Studies:
Wild-type overexpression to identify gain-of-function phenotypes
Domain deletion/mutation studies to identify functional regions
Expression of orthologous proteins for evolutionary conservation studies
Given that KIAA1467/FAM234B is listed in variation databases such as ClinVar and dbVar , systematic analysis of variants is an important research direction:
| Resource | Application | Methodological Approach |
|---|---|---|
| ClinVar | Identification of clinically significant variants | Genotype-phenotype correlation studies; functional validation of variants |
| dbVar | Structural variation analysis | PCR, MLPA, or NGS approaches to validate CNVs |
| Variation Viewer | Comprehensive variant visualization | In silico prediction of variant effects; prioritization for functional studies |
When investigating variants, researchers should consider:
Frequency in population databases (gnomAD, 1000 Genomes)
Conservation across species (PhyloP, GERP scores)
Predicted functional impact (SIFT, PolyPhen, CADD)
Location within predicted functional domains
Experimental validation of variants of uncertain significance
The predicted localization of KIAA1467/FAM234B to the Golgi apparatus, membrane compartments, and microtubule organizing center suggests potential involvement in several fundamental cellular processes:
Protein Trafficking:
Secretory pathway transport (ER-to-Golgi or Golgi-to-plasma membrane)
Endocytic recycling pathways
Experimental approaches: RUSH system trafficking assays, FRAP studies, cargo transport assays
Membrane Dynamics:
Membrane curvature generation or sensing
Membrane fusion or fission events
Experimental approaches: Liposome binding assays, membrane remodeling assays, reconstitution in GUVs
Cytoskeletal Organization:
Microtubule nucleation or anchoring
Centrosome function during cell division
Experimental approaches: Microtubule regrowth assays, centrosome duplication studies, live-cell imaging during mitosis
A comprehensive tissue expression profiling strategy should incorporate:
Transcript-Level Analysis:
Bulk RNA-seq across multiple tissues/cell types
Single-cell RNA-seq for cellular resolution
Spatial transcriptomics for regional expression patterns
Protein-Level Analysis:
Immunohistochemistry with validated antibodies
Tissue microarrays for high-throughput screening
Tissue proteomics with enrichment for membrane fractions
Functional Analysis:
Tissue-specific conditional knockout models
Cell type-specific expression manipulation (Cre-LoxP systems)
Organoid models for developmental expression studies
Understanding the evolutionary context of KIAA1467/FAM234B can provide valuable insights into its fundamental functions:
Ortholog Identification:
Search for orthologs across model organisms (mouse, zebrafish, Drosophila, C. elegans)
Phylogenetic analysis to determine evolutionary conservation
Domain conservation analysis across species
Functional Conservation Testing:
Cross-species complementation studies
Domain swapping experiments between orthologs
Comparative localization studies in different model systems
Evolutionary Rate Analysis:
dN/dS ratios to identify selection pressures
Identification of rapidly evolving regions vs. constrained domains
Correlation with species-specific adaptations or functions
Several cutting-edge approaches show particular promise for advancing understanding of proteins like KIAA1467/FAM234B:
Structural Biology Approaches:
Cryo-EM for membrane protein structures
AlphaFold2/RoseTTAFold predictions combined with experimental validation
Hydrogen-deuterium exchange mass spectrometry for dynamic structural insights
Functional Genomics:
Genome-wide CRISPR screens to identify genetic interactions
Systematic interactome mapping using approaches like BioID-MS
Pooled CRISPR activation/inhibition screens for pathway placement
Advanced Imaging:
Live-cell super-resolution microscopy for dynamic localization studies
Lattice light-sheet microscopy for extended live imaging with minimal phototoxicity
Correlative light and electron microscopy for ultrastructural context
A systematic functional discovery workflow might include:
Initial Characterization Phase:
Definitive subcellular localization
Expression profiling across tissues/conditions
Preliminary phenotypic analysis of knockout/knockdown
Mechanistic Investigation Phase:
Comprehensive interactome mapping
Structure-function relationship studies
Conditional/tissue-specific manipulation
Physiological Relevance Phase:
Model organism studies
Disease-relevant contexts
Integration with systems-level data
When publishing findings on uncharacterized proteins, researchers should consider contributing to community resources like ProteomeXchange, the Human Protein Atlas, and appropriate model organism databases to accelerate collective understanding.