FGFR1 Antibodies

Structure of FGFR1

FGFR1 is a transmembrane receptor protein with a molecular weight of approximately 90-130 kDa, and its specific molecular weight varies depending on different splicing isomers and the degree of glycosylation modification.

The FGFR1 protein is composed of 822 to 853 amino acids, and its extracellular region contains 2 to 3 immunoglobulin-like domains, which are responsible for specific binding to ligands. This receptor possesses a single transmembrane domain and a highly conserved intracellular tyrosine kinase domain, the latter of which undergoes autophosphorylation upon activation and initiates downstream signaling. Its tertiary structure forms a flexible hinge region, allowing conformational changes in the extracellular region to regulate receptor dimerization and signal activity.

Fig. 1 Schematic diagram of FGFRs and the structure of the FGFR extracellular domain.¹

Key structural properties of FGFR1:

• Extracellular region by 2-3 immunoglobulin structural domain
• Maintain receptor anchoring in a single transmembrane domain
• The highly conserved tyrosine kinase domain within the cell performs catalytic functions

Functions of FGFR1

The core function of the protein encoded by the FGFR1 gene is to mediate cell growth and differentiation signals. However, this receptor is also widely involved in a variety of pathophysiological processes, including bone development, metabolic regulation and tumorigenesis.

The signal activation of FGFR1 is characterized by typical ligand-dependent and dimerization features. Its signal intensity is precisely regulated by the receptor expression level, splicing variant form and negative feedback mechanism, and together with other tyrosine kinase receptors, it constitutes a complex cellular signaling network.

Applications of FGFR1 and FGFR1 Antibody in Literature

1. Wang, Xinyue, et al. "A novel rabbit anti-myoglobin monoclonal antibody's potential application in rhabdomyolysis associated acute kidney injury." International Journal of Molecular Sciences 24.9 (2023): 7822. https://doi.org/10.1007/s00432-021-03906-x

The article indicates that in low-grade gliomas with unknown driver genes, the detection rate of hotspot mutations in the FGFR1 gene N546K/K656E reaches 12%, making it the fifth most common variation in this type of tumor. However, there is no clear correlation between the immunohistochemical expression level of FGFR1 and the mutation status.

2. Lin, Yan, et al. "The FGFR1 signaling pathway upregulates the oncogenic transcription factor FOXQ1 to promote breast cancer cell growth." International Journal of Biological Sciences 19.3 (2023): 744. https://doi.org/10.7150/ijbs.74574

Studies have revealed that FGFR1 activates the transcription factor c-FOS through the MEK-ERK2 pathway, thereby upregulating the expression of the oncogene FOXQ1 and driving the growth of breast cancer. Targeting ERK2 or FOXQ1 can inhibit tumor progression induced by FGFR1 signaling.

3. Yellapragada, Venkatram, et al. "FGF8–FGFR1 signaling regulates human GnRH neuron differentiation in a time-and dose-dependent manner." Disease Models & Mechanisms 15.8 (2022): dmm049436. https://doi.org/10.1242/dmm.049436

Studies have shown that FGF8 regulates the directed differentiation of human stem cells into GnRH neurons through the FGFR1 receptor in a specific dose - and time-dependent manner. Inhibiting FGFR1 significantly reduces the expression of the key gene GNRH1, confirming that this pathway is indispensable in neuronal development.

4. Welander, Jenny, et al. "Activating FGFR1 mutations in sporadic pheochromocytomas." World journal of surgery 42.2 (2018): 482-489. https://doi.org/10.1007/s00268-017-4320-0

Research has found that activating mutations in the FGFR1 gene recur in sporadic pheochromocytoma, with an incidence rate of approximately 3.8%. This makes it the third proto-oncogene discovered in this tumor after RET and HRAS, revealing that abnormal activation of FGFR1 is one of the important pathogenic mechanisms.

5. Haq, Farhan, et al. "FGFR1 expression defines clinically distinct subtypes in pancreatic cancer." Journal of Translational Medicine 16.1 (2018): 374. https://doi.org/10.1186/s12967-018-1743-9

Research has found that in pancreatic cancer, the expression of FGFR1 protein is an independent good prognostic indicator. Immunohistochemical detection showed that the overall survival period of FGFR1-positive patients was significantly better than that of FGFR1-negative patients. This discovery helps define the subtypes of pancreatic cancer and provides a potential new treatment direction for FGFR1-positive patients.

Creative Biolabs: FGFR1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality FGFR1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom FGFR1 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 FGFR1 antibodies, custom preparations, or technical support, contact us at email.