Enzymes
Product List
FGFR1 Human
Fibroblast Growth Factor Receptor 1 Fc Chimera Human Recombinant
Soluble FGFR-1a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain containing 601 amino acids and having a molecular mass of 170 kDa. The FGFR1 is purified by proprietary chromatographic techniques.
FGFR1 Human, (22-285)
Fibroblast Growth Factor Receptor-1 Human Recombinant, (22-285 a.a.)
FGFR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 272 amino acids (22-285) and having a molecular mass of 30.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
FGFR1 Human, (22-374)
Fibroblast Growth Factor Receptor-1, (22-374 a.a.) Human Recombinant
FGFR1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 361 amino acids (22-374a.a.) and having a molecular mass of 40.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR1 Human is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
FGFR1 Human, His
Fibroblast Growth Factor Receptor-1 Human Recombinant, His Tag
FGFR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 363 amino acids (22-376) and having a molecular mass of 40.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
FGFR1OP Human
FGFR1 Oncogene Partner Human Recombinant
FGFR1OP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
FGFR2 Human
Fibroblast Growth Factor Receptor 2 Fc Chimera Human Recombinant
Soluble FGFR-2a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain containing 602 amino acids and having a molecular mass of 170 kDa.
The FGFR2 is purified by proprietary chromatographic techniques.
FGFR2 Human, (22-289)
Fibroblast Growth Factor Receptor-2 (22-289 a.a.) Human Recombinant
FGFR2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (22-289a.a.) and having a molecular mass of 56.8kDa.
FGFR2 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.
FGFR2 Human, His
Fibroblast Growth Factor Receptor-2 Human Recombinant, His Tag
FGFR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 596 amino acids (22-378a.a.) and having a molecular mass of 66.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
FGFR2 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
FGFR3 Human, His
Fibroblast Growth Factor Receptor-3 Human Recombinant, His Tag
FGFR3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 592 amino acids (23-375a.a.) and having a molecular mass of 65.1kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
FGFR3 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
FGFR3 Human
Fibroblast Growth Factor Receptor 3 Fc Chimera Human Recombinant
Introduction
Fibroblast Growth Factor Receptors (FGFRs) are a family of receptor tyrosine kinases that are activated by fibroblast growth factors (FGFs). These receptors play crucial roles in various biological processes, including cell growth, differentiation, and tissue repair. FGFRs are classified into four main types: FGFR1, FGFR2, FGFR3, and FGFR4. Each receptor type has multiple isoforms generated through alternative splicing, which allows for diverse functional outcomes.
Key Biological Properties: FGFRs possess intrinsic tyrosine kinase activity, which is essential for their signaling functions. Upon binding to FGFs, FGFRs undergo dimerization and autophosphorylation, leading to the activation of downstream signaling pathways.
Expression Patterns: FGFRs are expressed in a wide range of tissues, with each receptor type exhibiting distinct expression patterns. For example, FGFR1 is widely expressed in the brain, heart, and skeletal muscle, while FGFR2 is predominantly found in epithelial tissues.
Tissue Distribution: The distribution of FGFRs varies across different tissues. FGFR1 is abundant in the nervous system, FGFR2 in the skin and gastrointestinal tract, FGFR3 in cartilage, and FGFR4 in the liver and muscle.
Primary Biological Functions: FGFRs are involved in numerous biological functions, including embryonic development, tissue repair, angiogenesis, and metabolism. They play a pivotal role in regulating cell proliferation, differentiation, and survival.
Role in Immune Responses: FGFRs contribute to immune responses by modulating the activity of immune cells. They are involved in the regulation of cytokine production and the activation of immune signaling pathways.
Pathogen Recognition: While FGFRs are not directly involved in pathogen recognition, their role in tissue repair and immune modulation indirectly influences the body’s ability to respond to infections.
Mechanisms with Other Molecules and Cells: FGFRs interact with a variety of molecules, including heparan sulfate proteoglycans (HSPGs), which facilitate FGF binding and receptor activation. They also form complexes with co-receptors and adaptor proteins to propagate signaling.
Binding Partners: FGFRs bind to FGFs with high affinity. The interaction is stabilized by HSPGs, which enhance the binding specificity and strength.
Downstream Signaling Cascades: Upon activation, FGFRs initiate several downstream signaling cascades, including the MAPK/ERK, PI3K/AKT, and PLCγ pathways. These pathways regulate diverse cellular processes such as proliferation, differentiation, and survival.
Expression and Activity Control: The expression and activity of FGFRs are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms.
Transcriptional Regulation: FGFR gene expression is controlled by various transcription factors and regulatory elements that respond to cellular and environmental cues.
Post-Translational Modifications: FGFRs undergo several post-translational modifications, such as phosphorylation, glycosylation, and ubiquitination, which modulate their stability, localization, and activity.
Biomedical Research: FGFRs are extensively studied in biomedical research due to their involvement in numerous physiological and pathological processes. They serve as valuable models for understanding receptor tyrosine kinase signaling and its implications in health and disease.
Diagnostic Tools: FGFRs are used as biomarkers for the diagnosis and prognosis of various cancers. Alterations in FGFR expression or mutations are associated with specific cancer types, making them useful targets for diagnostic assays.
Therapeutic Strategies: FGFRs are targets for therapeutic interventions in cancer and other diseases. FGFR inhibitors and monoclonal antibodies are being developed to block aberrant FGFR signaling in tumors.
Development: FGFRs play critical roles in embryonic development, including the formation of the nervous system, limbs, and organs. They regulate cell fate decisions and tissue patterning.
Aging: FGFR signaling is implicated in the aging process, influencing tissue homeostasis and repair mechanisms. Dysregulation of FGFR activity is associated with age-related diseases.
Disease: Aberrant FGFR signaling is linked to various diseases, including cancer, skeletal disorders, and metabolic syndromes. Understanding FGFR function and regulation provides insights into disease mechanisms and potential therapeutic targets.
