FBN1 Antibodies

Structure of FBN1

Fibrin-1 encoded by the FBN1 gene is a large glycoprotein with a molecular weight of approximately 350 kDa. This protein is mainly composed of epidermal growth factor-like domains and transforming growth factor - β -binding protein-like domains. The difference in the number of calcium-binding epidermal growth factor-like domains is the main factor leading to the subtle changes in molecular weight among different species.

Fibrin-1 assembles into an extracellular microfiber network through its unique linearly arranged domain. Each monomer contains multiple calcium-binding epidermal growth factor-like domains, which are stably folded through disulfide bonds, providing rigidity for the protein. Transforming growth factor - β -binding protein-like domains mediate protein-protein interactions, and the C-terminal region is crucial for the correct assembly of fibrils. This multi-domain organizational form enables fibrin-1 to simultaneously undertake the dual functions of structural support and signal regulation.

Fig. 1 3D structure prediction of FBN1.¹

Key structural properties of FBN1:

• Complex linear arrangement of multiple domains
• Calcium-binding EGF-like domains rich in cysteine
• Transforming growth factor β -binding protein-like domains mediate protein interactions

Functions of FBN1

The main function of the protein encoded by the FBN1 gene is to form the microfiber scaffold of the extracellular matrix and regulate the activity of growth factors. Its specific functions include:

This protein achieves conformational rigidity through its multiple calcium-binding EGF-like domains. This structural characteristic enables it to not only withstand physical tension but also precisely participate in signal regulation, demonstrating the dual characteristics of structural proteins and regulatory proteins.

Applications of FBN1 and FBN1 Antibody in Literature

1. Sun, Yonghong, et al. "MFAP2 promotes HSCs activation through FBN1/TGF‐β/Smad3 pathway." Journal of Cellular and Molecular Medicine 27.21 (2023): 3235-3246. https://doi.org/10.1111/jcmm.17884

The article indicates that in liver fibrosis, the expression of MFAP2 is upregulated and promotes the activation of hepatic stellate cells and collagen deposition by regulating FBN1. Inhibiting MFAP2 can slow down cell proliferation and induce apoptosis of activated stellate cells, thereby alleviating fibrosis, indicating its clinical therapeutic potential.

2. Åström Malm, Ida, Rachel De Basso, and Peter Blomstrand. "No differences in FBN1 genotype between men with and without abdominal aortic aneurysm." BMC Cardiovascular Disorders 23.1 (2023): 36. https://doi.org/10.1186/s12872-023-03068-3

This study explores the relationship between the FBN1 genotype and abdominal aortic aneurysm (AAA). The results showed that there was no significant difference in the distribution of FBN1 genotypes between the AAA group and the control group. However, among men carrying the FBN1-2/2 genotype, the central artery hardness of AAA patients was significantly higher than that of non-AAA patients.

3. Shimizu, Norihiro, et al. "Novel FBN1 intron variant causes isolated ectopia lentis via in-frame exon skipping." Journal of Human Genetics 70.4 (2025): 199-205. https://doi.org/10.1038/s10038-025-01318-0

The article indicates that in a Japanese IEL family, researchers discovered a novel intron mutation of the FBN1 gene (c.1327+3A>C). This mutation causes exon 11 of FBN1 to be skipped during transcription, resulting in the absence of its protein "hinge region" and ultimately triggering IEL, which provides new insights into the mechanism of FBN1-related diseases.

4. Dougarem, Djouhayna, et al. "A novel heterozygous intronic FBN1 variant contributes to aberrant RNA splicing in marfan syndrome." Molecular Genetics & Genomic Medicine 12.9 (2024): e70004. https://doi.org/10.1002/mgg3.70004

In this study, a novel non-classical splicing site variation c.443-3C>G of the FBN1 gene was identified in a Marfan syndrome family. This variation leads to two abnormal mRNA transcripts, triggering frameshift and in-frame insertions. Experiments have confirmed its pathogenicity, expanding the pathogenic variation spectrum of FBN1.

5. Wang, Tao, et al. "Acromicric dysplasia with stiff skin syndrome‐like severe cutaneous presentation in an 8‐year‐old boy with a missense FBN1 mutation: Case report and literature review." Molecular Genetics & Genomic Medicine 8.7 (2020): e1282. https://doi.org/10.1002/mgg3.1282

In this study, acrofacial dysplasia caused by A heterozygous missense mutation of c.5243G>A in the FBN1 gene was diagnosed in a Chinese child patient, accompanied by severe skin stiffness similar to scleroderma. This case reveals the pleiotropy of the FBN1 gene, where a single hotspot mutation can lead to complex clinical symptoms.

Creative Biolabs: FBN1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality FBN1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom FBN1 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 FBN1 antibodies, custom preparations, or technical support, contact us at email.