FIBP Human

What is the structural composition of FIBP Human protein?

FIBP Human Recombinant is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-364) with a molecular mass of 44.3kDa. When produced in E. coli for research purposes, it is typically fused to a 23 amino acid His-Tag at the N-terminus to facilitate purification through chromatographic techniques .

The protein is commonly supplied in 20mM Tris-HCl buffer (pH 8.0) with 10% glycerol. For optimal stability during long-term storage, researchers should store the protein at -20°C with the addition of a carrier protein (0.1% HSA or BSA) and avoid multiple freeze-thaw cycles that can compromise structural integrity .

What are the primary synonyms and alternative designations for FIBP?

Researchers should be aware of the following alternative designations when searching literature or databases:

• FGFIBP

• FIBP-1

• Acidic fibroblast growth factor intracellular-binding protein

• aFGF intracellular-binding protein

• FGF-1 intracellular-binding protein

These alternative nomenclatures reflect the protein's functional relationship with fibroblast growth factor signaling pathways.

What is the tissue distribution pattern of FIBP in normal human physiology?

FIBP demonstrates a differential expression pattern across human tissues. It is highly expressed in heart, skeletal muscle, and pancreas, while showing lower expression levels in brain, placenta, liver, and kidney . This tissue-specific expression pattern suggests specialized functions in different organ systems.

Methodologically, when analyzing FIBP expression across tissues, researchers should employ multiple detection techniques including qRT-PCR, western blotting, and immunohistochemistry for comprehensive validation. Proper normalization with tissue-specific reference genes is essential for accurate comparative analyses.

How is FIBP expression altered in malignancies compared to normal tissues?

FIBP exhibits significant upregulation across multiple cancer types compared to corresponding normal tissues. Analysis of The Cancer Genome Atlas (TCGA) and Genotype-Tissue Expression (GTEx) data demonstrates FIBP overexpression in 28 cancer types, including bladder cancer (BLCA), breast cancer (BRCA), acute myeloid leukemia (LAML), and numerous others .

What is the prognostic significance of FIBP expression in acute myeloid leukemia?

Clinical correlations reveal that FIBP expression is significantly associated with:

• Elevated white blood cell (WBC) count (p < 0.05)

• Increased peripheral blood (PB) blasts (p < 0.01)

• French-American-British (FAB) classifications (p < 0.01)

• Cytogenetic risk categories (p < 0.001)

These associations suggest FIBP may contribute to a more aggressive disease phenotype .

What molecular pathways and biological processes are associated with FIBP in cancer?

Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses of differentially expressed genes associated with FIBP in AML reveal involvement in multiple cancer-relevant processes . Key biological processes include:

• Leukocyte migration and chemotaxis

• Extracellular matrix organization

• Leukocyte cell-cell adhesion

• Myeloid leukocyte differentiation

• Endothelial cell proliferation

• T cell tolerance induction

The cellular component (CC) analysis indicates enrichment in transporter complexes, membrane regions, and membrane microdomains. Molecular function (MF) analyses highlight roles in G protein-coupled receptor binding, cytokine activity, and growth factor binding .

At the pathway level, FIBP-associated genes are enriched in cytokine-cytokine receptor interaction, cell adhesion molecules, and complement and coagulation cascade pathways .

What are the optimal methods for recombinant FIBP production and purification?

Recombinant FIBP Human production is typically achieved using E. coli expression systems . The methodology involves:

• Expression as a fusion protein with an N-terminal His-tag (23 amino acids) to facilitate purification

• Purification using proprietary chromatographic techniques

• Formulation in 20mM Tris-HCl buffer (pH 8.0) with 10% glycerol for stability

When working with recombinant FIBP, researchers should verify protein purity (>95% by SDS-PAGE is standard) and confirm biological activity. Storage recommendations include maintaining at 4°C if using within 2-4 weeks or at -20°C for longer periods, with the addition of carrier proteins (0.1% HSA or BSA) to prevent degradation .

How can researchers effectively analyze FIBP's interaction with binding partners?

To investigate FIBP's interactions with FGF-1 and other potential binding partners, researchers should employ multiple complementary techniques:

• Co-immunoprecipitation (Co-IP) followed by western blotting to detect physical interactions

• Proximity ligation assays for in-situ visualization of protein-protein interactions

• Label transfer methods (BioID, APEX) to identify interacting proteins in living cells

• Mass spectrometry-based approaches for unbiased interactome analysis

• Yeast two-hybrid or mammalian two-hybrid systems for direct binary interaction assessment

When analyzing FIBP-FGF-1 interactions specifically, researchers should account for FIBP's role in binding internalized FGF-1, distinguishing it from extracellular FGF-binding proteins . Functional validation through mutation of binding interfaces can confirm the specificity and significance of observed interactions.

What approaches can be used to study FIBP's role in immune cell regulation?

Given FIBP's correlation with immune infiltrates in cancers, researchers can employ several methodologies to investigate its immunomodulatory functions:

• Flow cytometry to quantify immune cell populations in relation to FIBP expression

• Multiplex immunohistochemistry to maintain spatial context of immune infiltration

• FIBP gene knockout or knockdown in tumor cells followed by co-culture with immune cells

• Analysis of cytokine production in FIBP-manipulated experimental systems

Research has demonstrated that FIBP shows significant correlation with CD4, IL-10, and IL-2, indicating potential roles in T cell regulation . The relationship between FIBP and these immune markers suggests involvement in modulating anti-tumor immune responses, a direction warranting further investigation using the methodologies outlined above.

How can FIBP serve as a prognostic biomarker in clinical oncology?

FIBP shows promise as a prognostic biomarker, particularly in acute myeloid leukemia. Implementation strategies should consider:

• Quantitative assessment of FIBP expression using validated antibodies or RNA-based methods

• Integration with established prognostic factors through multivariate analysis

• Correlation with specific genetic alterations (e.g., NPM1 mutations)

• Stratification of patients based on FIBP expression thresholds

What therapeutic strategies can target FIBP-dependent cancer mechanisms?

Several approaches can be explored for targeting FIBP in cancer therapy:

• Small molecule inhibitors disrupting FIBP-FGF1 interaction

• RNA interference-based therapeutics (siRNA, antisense oligonucleotides)

• CRISPR-based gene editing to knock out FIBP in therapeutic settings

• Combination approaches targeting FIBP alongside complementary pathways

The finding that FIBP knockout enhances T cell antitumor efficacy through downregulation of cholesterol metabolism suggests potential synergy between FIBP inhibition and immunotherapy approaches. This represents a promising avenue for therapeutic development, particularly in malignancies where FIBP overexpression correlates with poor prognosis.

What challenges exist in translating FIBP research into clinical applications?

Translational challenges in FIBP-targeted therapy development include:

• Intracellular localization limiting accessibility to therapeutic agents

• Potential toxicity concerns given FIBP expression in critical normal tissues (heart, skeletal muscle)

• Compensatory mechanisms that might arise from pathway redundancy

• Need for biomarkers to identify patients most likely to benefit from FIBP-targeted approaches

Addressing these challenges requires systematic preclinical investigation using physiologically relevant models, careful toxicity assessment in normal tissues, and development of advanced delivery systems capable of reaching intracellular targets efficiently.

How does FIBP contribute to tumor microenvironment modulation?

FIBP's role in shaping the tumor microenvironment extends beyond cancer cells to influence stromal components. Research approaches should investigate:

• Effects on endothelial cell proliferation and angiogenesis

• Correlation with extracellular matrix organization and remodeling

• Modulation of immune cell infiltration patterns and function

• Communication between tumor cells and surrounding stroma through FIBP-dependent mechanisms

Gene enrichment analyses linking FIBP to biological processes including extracellular matrix organization, endothelial cell proliferation, and regulation of blood circulation suggest broader roles in tumor-stroma interaction that warrant detailed investigation through co-culture systems and in vivo models.

What is known about post-translational modifications of FIBP?

Post-translational modifications likely play important roles in regulating FIBP function, though this area remains incompletely characterized. Research methodologies should include:

• Mass spectrometry-based proteomics with enrichment for specific modifications

• Site-directed mutagenesis of putative modification sites

• Analysis of modification dynamics in response to cellular stimuli

• Identification of enzymes responsible for adding or removing modifications

Understanding the post-translational regulation of FIBP may reveal novel mechanisms for therapeutic intervention that could be more specific than targeting protein expression or interaction directly.

How do genetic variations in FIBP influence its function and disease associations?

Investigation of FIBP genetic variants represents an emerging research direction. Methodological approaches include:

• Genome-wide association studies (GWAS) and targeted sequencing in patient cohorts

• Functional characterization of variants through expression in cellular models

• Computational prediction tools for initial assessment of variant impact

• Correlation of variant status with clinical parameters and treatment response

The potential role of FIBP variants in disease susceptibility or treatment response could provide valuable insights for personalized medicine approaches in FIBP-associated malignancies.