FGFR2 Antibodies

Background

FGFR2 is a transmembrane tyrosine kinase receptor protein, mainly distributed in epithelial cells, osteoblasts and various organ tissues during embryonic development. This gene participates in key biological processes such as cell proliferation, differentiation, migration and tissue repair by specifically binding to fibroblast growth factor (FGF), and particularly plays a core regulatory role in bone development, cranial suture closure and organ formation. Unlike the oxygen storage function of myoglobin, FGFR2 transmits extracellular signals to the nucleus by activating downstream signaling pathways such as RAS/MAPK and PI3K/AKT. This gene was first identified in the 1980s. Its mutations are closely related to a variety of genetic diseases, such as Apert syndrome and Crouzon syndrome (often caused by point mutations in exon 7 or 9). As an important model in developmental biology and oncology research, the structural and functional studies of FGFR2 have continuously driven the development of targeted drugs and the progress of precision medicine.

Structure Function Application Advantage Our Products

Structure of Myoglobin

FGFR2 is a transmembrane protein with a molecular weight of approximately 92 kDa. Its precise molecular weight varies slightly among different species due to differences in amino acid sequences.

Species	Human	Mouse	Rat	Bovine
Molecular Weight (kDa)	92.0	91.5	91.8	92.2
Primary Structural Differences	Contains 822 amino acids, with three Ig sample structure domain	With the human high homology, highly conserved across the membrane area	Similar to the structure of intracellular tyrosine kinase domain	Specific mutations, interspecific carboxyl terminal sequence

This protein is composed of an extracellular ligand-binding region, a single transmembrane segment and an intracellular tyrosine kinase region. Its extracellular part contains 2 to 3 immunoglobulin-like (Ig-like) domains, which are responsible for specifically recognizing FGF ligands. The activation of FGFR2 depends on the dimerization and autophosphorylation processes. A highly conserved "DXGXKGE" motif is involved in the formation of the ATP binding loop and is crucial for kinase activity. Key amino acids such as Lys517 are involved in ATP localization, while Asn549 and Asp551 residues directly catalyze phosphate transfer. Its tertiary structure undergoes conformational changes under ligand induction, thereby regulating the specificity and intensity of downstream signaling pathways.

The FGFR Family: Structure and Function. Fig. 1 Structural and Functional Overview of the FGFR Family.¹

Key structural properties of FGFR2:

Extracellular region contains 2-3 sample immunoglobulin (Ig - like) structural domain
Single transmembrane helical structure
Intracellular area highly conservative tyrosine kinase domain structure

Functions of FGFR2

The main function of the protein encoded by the FGFR2 gene is to mediate cell signal transduction and regulate growth and development. However, it is also widely involved in a variety of pathophysiological processes, including tissue repair and cancer occurrence.

Function	Description
Regulation of cell proliferation	After activation, FGFR2 promotes the division of target cells through the MAPK and PI3K-AKT pathways, especially playing a key role in embryonic development and osteogenesis.
Tissue differentiation and morphogenesis	It participates in bone formation, cranial suture closure and limb development, and coordinates the differentiation and spatial configuration establishment of various tissue types.
Damage repair support	Regulate the processes of wound healing, angiogenesis and tissue regeneration in adult tissues.
Tumorigenesis and development	Mutated or abnormally expressed FGFR2 can lead to persistent proliferation signals and is closely related to various cancers such as gastric cancer and breast cancer.
Metabolism and homeostasis regulation	By influencing FGF signaling pathway, it participates in phosphate metabolism and vitamin D regulation and other physiological processes.

The ligand binding characteristics of FGFR2 are characterized by multi-factor co-activation (such as the need for FGF and heparin sulfate proteoglycan to bind together), and its signal intensity is strictly bidirectionally regulated (such as the regulation of negative feedback mechanisms and receptor splicing variants). Compared with single-ligand-binding proteins, it places more emphasis on the context dependence and multi-functionality of the signaling pathway.

Applications of FGFR2 and FGFR2 Antibody in Literature

1. Zingg, Daniel, et al. "Truncated FGFR2 is a clinically actionable oncogene in multiple cancers." Nature 608.7923 (2022): 609-617. https://doi.org/10.1038/s41586-022-05066-5

The article indicates that the truncated mutation of exon 18 (E18) of the FGFR2 gene is a potent oncogenic driver variation, which can produce a stable FGFR2ΔE18 protein and become a potential biomarker for FGFR-targeted therapy.

2. Tojjari, Alireza, et al. "Deciphering the FGFR2 code: innovative targets in gastric cancer therapy." Current Oncology 31.8 (2024): 4305-4317. https://doi.org/10.3390/curroncol31080321

The article indicates that overexpression of FGFR2 in gastric cancer is associated with a poor prognosis, especially in diffuse type. Currently, small molecule inhibitors and monoclonal antibody drugs targeting FGFR2 have entered clinical trials, which are expected to bring new treatment options to patients.

3. Ferrarese, Luca, et al. "Inflammatory mediators suppress FGFR2 expression in human keratinocytes to promote inflammation." Molecular and Cellular Biology 44.11 (2024): 489-504. https://doi.org/10.1080/10985549.2024.2399766

The article indicates that the deletion of FGFR2 can cause human keratinocytes to overexpress interferon genes and pro-inflammatory cytokines under homeostasis and inflammation. In the lesions of patients with atopic dermatitis, the expression of FGFR2 is significantly down-regulated, suggesting that its down-regulation may exacerbate the inflammatory phenotype.

4. Piloto, Ana Margarida, et al. "Plastic antibodies tailored on quantum dots for an optical detection of myoglobin down to the femtomolar range." Scientific reports 8.1 (2018): 4944. https://doi.org/10.3892/mmr.2023.13113

This study focused on black women in southern Africa, analyzing the relationship between four SNP loci of the FGFR2 gene and the risk of breast cancer. The results showed that these loci related to the European population had no significant association with the risk of breast cancer in this population. Only the C/C homozygous genotype of rs2981578 was associated with invasive lobular carcinoma, indicating that there are population differences in the genetic risk of breast cancer.

5. Mieczkowski, Kamil, et al. "FGF7/FGFR2–JunB signalling counteracts the effect of progesterone in luminal breast cancer." Molecular oncology 16.15 (2022): 2823-2842. https://doi.org/10.1002/1878-0261.13274

The article indicates that FGFR2 signaling antagonizes the regulation of estrogen receptor (ER) function by progesterone (P4) through the JunB pathway, thereby influencing the growth of ER+ breast cancer cells and tamoxifen response. This mechanism is particularly significant in premenopausal patients and can provide a basis for targeted therapy.

Creative Biolabs: FGFR2 Antibodies for Research

Creative Biolabs specializes in the production of high-quality FGFR2 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom FGFR2 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 FGFR2 antibodies, custom preparations, or technical support, contact us at email.

Reference

Tojjari, Alireza, et al. "Deciphering the FGFR2 code: innovative targets in gastric cancer therapy." Current Oncology 31.8 (2024): 4305-4317. https://doi.org/10.3390/curroncol31080321