FABP4 Human, His
Description
Introduction to FABP4
Fatty Acid-Binding Protein 4 (FABP4), also known as adipocyte FABP (A-FABP) or aP2, is a cytoplasmic lipid chaperone primarily expressed in adipocytes and macrophages . It plays a pivotal role in regulating lipid metabolism, inflammatory responses, and cellular signaling pathways . Elevated circulating FABP4 levels are strongly associated with metabolic disorders (e.g., obesity, insulin resistance, type 2 diabetes) and cardiovascular diseases, including atherosclerosis and hypertension .
FABP4 Human, His – Definition and Production
FABP4 Human, His refers to a recombinant human FABP4 protein engineered with a polyhistidine (His) tag for purification and research applications. Key features include:
This recombinant protein is widely used in biochemical assays, structural studies, and drug discovery .
Key Functional Interactions
The His tag does not interfere with ligand binding or protein-protein interactions in validated assays .
Table 1: Key Studies Utilizing Recombinant FABP4
Biomarker Potential
-
Circulating FABP4 levels predict cardiovascular mortality (HR: 4.96 for highest tertile) .
-
Elevated FABP4 correlates with left ventricular dysfunction and carotid atherosclerosis .
Therapeutic Targeting
-
Small-Molecule Inhibitors: BMS309403 blocks fatty acid binding, improving insulin sensitivity .
-
Monoclonal Antibodies: Humanized anti-FABP4 antibodies (e.g., 12G2) suppress tumor growth in breast cancer models .
Future Directions
FABP4’s dual role in metabolic regulation and inflammation positions it as a multifaceted therapeutic target. Ongoing research focuses on:
Product Specs
Q&A
Basic Research Questions
-
What is the primary function of FABP4 in human metabolism?
FABP4 primarily facilitates fatty acid transport across cellular membranes, playing a crucial role in lipid metabolism. It binds to long-chain fatty acids and participates in their intracellular trafficking. Beyond simple transport, FABP4 is involved in glucose metabolism regulation, with studies demonstrating its direct regulation of hepatic glucose synthesis by increasing the expression of gluconeogenic enzymes including glucose-6-phosphatase and phosphoenolpyruvate carboxykinase 1 . Methodologically, researchers can investigate FABP4's metabolic functions through knockout mouse models, which show altered lipid profiles with increased short-chain fatty acids and decreased long-chain fatty acids .
-
How does FABP4 expression differ between genders and age groups?
Studies reveal significant gender and age-related differences in FABP4 expression. Research from the Kuwait Diabetes Epidemiology Program demonstrated significantly higher FABP4 concentrations in female participants compared to males (18.8 ng/mL vs. 14.4 ng/mL, p < 0.001) . Additionally, individuals over 50 years old exhibited higher concentrations than those under 50 (19.3 ng/mL vs. 16.2 ng/mL, p < 0.001) . Multivariate regression analysis confirmed these associations, with FABP4 levels negatively associated with male gender (β: −3.85, 95% CI: −4.92, −2.77, p < 0.001) and positively associated with age (β: 0.14, 95% CI: 0.096, 0.183, p < 0.001) . These differences must be considered when designing research studies and interpreting FABP4 data.
-
What relationships exist between FABP4 and markers of obesity?
FABP4 demonstrates strong positive correlations with multiple obesity markers. Current research has established significant associations between FABP4 levels and BMI (r = 0.496, p < 0.001), hip circumference (r = 0.463, p < 0.001), and waist circumference (r = 0.436, p < 0.001) . These associations remain significant even after adjusting for age, gender, and ethnicity. Methodologically, researchers can assess these relationships through multivariate regression analysis while controlling for demographic variables. The table below summarizes key correlations between FABP4 and obesity markers:
Obesity Marker Correlation Coefficient (r) p-value BMI 0.496 <0.001 Hip Circumference 0.463 <0.001 Waist Circumference 0.436 <0.001 -
How is FABP4 associated with glycemic indices?
FABP4 shows significant positive associations with multiple glycemic indices, making it relevant for diabetes research. Analysis reveals positive correlations between FABP4 and HbA1c (r = 0.126, p < 0.001), fasting blood glucose (r = 0.184, p < 0.001), fasting insulin (r = 0.326, p < 0.001), and HOMA-IR (r = 0.333, p < 0.001) . When investigating these relationships, researchers should employ multivariate statistical approaches to account for confounding variables such as obesity metrics, as FABP4's relationship with glycemic control may be partially mediated by adiposity.
Product Science Overview
FABP4 is composed of a β-barrel structure that forms the lipid-binding site, and two α-helices that act as a lid on the β-barrel . This structure allows FABP4 to bind long-chain fatty acids and retinoic acid, facilitating their transport and metabolism within cells . The protein plays a crucial role in lipid transport, metabolism, insulin resistance, and angiogenesis .
The expression of FABP4 is induced by long-chain fatty acids and peroxisome proliferator-activated receptor γ (PPARγ) agonists . It is involved in various metabolic processes, and its dysregulation is associated with several metabolic disorders. For instance, knockout studies in mice have shown that the absence of FABP4 prevents the development of atherosclerosis and increases insulin sensitivity .
Elevated levels of FABP4 have been observed in patients with conditions such as colorectal cancer and rheumatoid arthritis . This makes FABP4 a potential biomarker for these diseases. Additionally, its role in metabolic processes makes it a target for therapeutic interventions aimed at treating metabolic disorders.
Recombinant human FABP4, tagged with a His tag, is produced in Escherichia coli (E. coli) and is typically used in research applications such as ELISA, Western blot (WB), and immunoprecipitation (IP) . The His tag facilitates the purification of the protein using standard chromatography techniques . This recombinant protein retains the functional properties of the native protein, making it a valuable tool for studying the biological functions and interactions of FABP4.
