FGFR4 Human

Fibroblast Growth Factor Receptor 4 Fc Chimera Human Recombinant

Soluble FGFR-4a (IIIc) Fc Chimera Human Recombinant is a genetically engineered protein comprising the extracellular domain of human FGFR-4a (IIIc) fused to the Fc region of human IgG1. This chimeric protein is produced in baculovirus-infected insect cells, resulting in a heterodimeric glycoprotein with an approximate molecular weight of 170 kDa. The purification process involves proprietary chromatographic techniques to ensure high purity. Key features: - Extracellular domain of human FGFR-4a (IIIc) fused to human IgG1 Fc. - Produced in baculovirus expression system. - Heterodimeric glycoprotein with a molecular weight of approximately 170 kDa. - Purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19861
Source
Insect Cells.
Appearance
White powder, lyophilized and sterile.

FGFR4 Human, His

Fibroblast Growth Factor Receptor-4 Human Recombinant, His Tag

Recombinant Human Fibroblast Growth Factor Receptor-4, expressed in Sf9 Baculovirus cells, is a single glycosylated polypeptide chain with a molecular weight of 39.5 kDa (containing 356 amino acids, spanning residues 22-369a.a.). However, it appears as a band with an apparent molecular weight of 40-57 kDa on SDS-PAGE. This discrepancy can be attributed to glycosylation. This protein is fused with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19973
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

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.

Biological Properties

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.

Biological Functions

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.

Modes of Action

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.

Regulatory Mechanisms

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.

Applications

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.

Role in the Life Cycle

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.

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