FNTB Antibodies

Background

The FNTB gene codes the β subunit of Farniki transferase, which catalyzes the farniki reaction in post-translational modifications of proteins. By covalently attaching the farniki group to the C-terminal of specific proteins (such as the Ras superfamily GTPase), it promotes their anchoring to the cell membrane and participates in cell signal transduction, proliferation and survival regulation. This gene was identified in the early 1990s. The elucidation of its function revealed the key modification mechanism of RAS protein activation in tumorigenesis, laying the foundation for the subsequent development of farnesyltransferase inhibitors as anti-cancer targets. Continuous research on FNTB has deepened people's understanding of the molecular mechanisms of post-translational modification of proteins, cell membrane localization signals, and targeted cancer therapy.

Structure Function Application Advantage Our Products

Structure of FNTB

The β subunit of Farnesyltransferase encoded by the FNTB gene is a protein with a molecular weight of approximately 46 kDa. There is a certain degree of conservation and difference in molecular weight and sequence among different species.

Species	Human	Mouse	Rat	Yeast
Molecular Weight (kDa)	46	45.8	46.1	48
Primary Structural Differences	Catalytic oxidation of proteins such as RAS is crucial for signal transduction	Highly conserved in function, used in gene knockout models	Often used in the study of nerve and metabolism	Homologous gene RAM1 was an early functional model

This protein is composed of approximately 400 amino acids, and its three-dimensional structure presents a typical α/β folding conformation. The core region of the protein forms a highly conserved hydrophobic pocket, which is specifically designed for recognizing and binding substrate proteins containing the "CAAX" motif and farniki pyrophosphate (FPP) donors. Its active center is composed of a key zinc ion coordination domain and multiple acidic amino acid residues, which jointly catalyze the transfer of the Farnicki group from FPP to the cysteine residues of the substrate protein. This post-translational modification is crucial for the membrane localization and functional activation of many signaling proteins.

Fig. 1 The FNTB promotor region.¹

Key structural properties of FNTB:

Typical α/β fold domains
Conservative hydrophobic substrate binding pocket
Zinc ion coordination catalytic center

Functions of FNTB

The core function of the protein encoded by the FNTB gene is to catalyze the farnesylation modification of proteins. Its main physiological and pathological functions are as follows:

Function	Description
Post-translational modification of proteins	The catalytic Farnikki group is transferred from Farnikki pyrophosphate to the cysteine residues of target proteins containing the "CAAX" motif (such as RAS, nuclear lamina proteins).
Regulation of cell signal transduction	By promoting the anchoring of small G proteins such as RAS to the cell membrane and activating downstream pathways like MAPK, it drives cell proliferation and differentiation.
Tumorigenesis and development	Its excessive activation can lead to the continuous activation of RAS proteins and is one of the key driving factors for many cancers, such as pancreatic cancer and leukemia.
Fundamentals of Targeted Therapy	As an important target of anti-cancer drugs (farnesyltransferase inhibitors), it inhibits tumor growth by blocking abnormal signal transduction.
Cytoskeleton and nuclear membrane are stable	Modify the nuclear protein fiber layer, etc., involved in maintaining nuclear membrane skeleton structure and cell integrity.

The catalytic mechanism of this enzyme has a high degree of substrate specificity. Its reaction kinetics follows an ordered dual-substrate mechanism, first binding to pyranipyrophosphate, then recognizing protein substrates, and ultimately completing covalent modification. This characteristic makes it a key molecular switch for precisely regulating the life activities of cells.

Applications of FNTB and FNTB Antibody in Literature

1. Bachmann, Hagen Sjard, et al. "FNTB promoter polymorphisms are independent predictors of survival in patients with triple negative breast cancer." Cancers 14.3 (2022): 468. https://doi.org/10.3390/cancers14030468

This study for the first time discovered that the polymorphism of the FNTB gene promoter (such as -173 6G>5G, etc.) can serve as an independent prognostic marker for early triple-negative breast cancer and may affect gene transcriptional activity, providing a new basis for risk stratification through blood genotyping.

2. Ding, Jie, et al. "Overexpression of FNTB and the activation of Ras induce hypertrophy and promote apoptosis and autophagic cell death in cardiomyocytes." Journal of Cellular and Molecular Medicine 24.16 (2020): 8998-9011. https://doi.org/10.1111/jcmm.15533

This study reveals that overexpression of FNTB can induce myocardial cell hypertrophy and reduce their survival rate. The mechanism involves a decrease in mitochondrial membrane potential, an increase in apoptosis, and the activation of excessive autophagic flux. The related effects can be inhibited by Saliraci, suggesting that Farnesyltransferase may provide a new target for the future treatment of myocardial hypertrophy.

3. Zhai, Yirui, et al. "Silencing of spindle apparatus coiled-coil protein 1 suppressed the progression of hepatocellular carcinoma through farnesyltransferase-beta and increased drug sensitivity." Heliyon 10.14 (2024). https://doi.org/10.1016/j.heliyon.2024.e34484

This study reveals for the first time that SPDL1 promotes the progression of liver cancer by regulating the downstream target FNTB. Inhibiting SPDL1 can induce apoptosis, inhibit proliferation and migration, and enhance the sensitivity of targeted drugs, suggesting that the SPDL1/FNTB axis may become a new target for the treatment of liver cancer.

4. Deng, Dan-Xia, et al. "Prenylated PALM2 promotes the migration of esophageal squamous cell carcinoma cells through activating ezrin." Molecular & Cellular Proteomics 22.8 (2023). https://doi.org/10.1016/j.mcpro.2023.100593

This study reveals that the highly expressed palmitoylated protein PALM2 in esophageal cancer is modified by Farnesyltransferase (FNTA/FNTB), promoting its membrane localization and interacting with ezrin, thereby activating ezrin and enhancing the migration ability of cancer cells.

5. Zhu, Lin, et al. "Drug repositioning and ovarian cancer, a study based on Mendelian randomisation analysis." Frontiers in Oncology 14 (2024): 1376515. https://doi.org/10.3389/fonc.2024.1376515

This study, through Mendelian randomization analysis, found that FNTB is positively correlated with the risk of ovarian cancer, suggesting that traditional drugs such as farnesyltransferase inhibitors like lonafenib have potential therapeutic effects and providing a new direction for drug repositioning in ovarian cancer.

Creative Biolabs: FNTB Antibodies for Research

Creative Biolabs specializes in the production of high-quality FNTB antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom FNTB Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our FNTB antibodies, custom preparations, or technical support, contact us at email.

Reference

Bachmann, Hagen Sjard, et al. "FNTB promoter polymorphisms are independent predictors of survival in patients with triple negative breast cancer." Cancers 14.3 (2022): 468. https://doi.org/10.3390/cancers14030468