FGFR1 Human

Fibroblast Growth Factor Receptor 1 Fc Chimera Human Recombinant

Soluble FGFR-1a (IIIc) Fc Chimera Human Recombinant, incorporating a Xa cleavage site and the Fc domain of human IgG1, is produced in a baculovirus expression system. This chimeric protein is a heterodimeric, glycosylated polypeptide chain comprising 601 amino acids with a molecular weight of 170 kDa. The purification of FGFR1 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT18986
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.

FGFR1 Human, (22-285)

Fibroblast Growth Factor Receptor-1 Human Recombinant, (22-285 a.a.)

FGFR1 Human Recombinant, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 272 amino acids (22-285) with a molecular weight of 30.4 kDa. The protein appears at approximately 40-57 kDa on SDS-PAGE due to glycosylation. It is fused to an 8 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19070
Source

Sf9, Baculovirus cells. 

Appearance
Sterile Filtered colorless solution

FGFR1 Human, (22-374)

Fibroblast Growth Factor Receptor-1, (22-374 a.a.) Human Recombinant

Human FGFR1, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain comprising 361 amino acids (22-374a.a.). It has a molecular mass of 40.1 kDa. However, on SDS-PAGE, the apparent molecular size will be approximately 40-57 kDa. This protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT19160
Source
Insect Cells.
Appearance

The solution is colorless and sterile filtered.

FGFR1 Human, His

Fibroblast Growth Factor Receptor-1 Human Recombinant, His Tag

Recombinant human FGFR, expressed in Sf9 Baculovirus cells, is a single glycosylated polypeptide chain with a molecular weight of 40.4 kDa (appears as approximately 40-57 kDa on SDS-PAGE). This protein encompasses amino acids 22-376 and features an 8-amino acid His-tag fused to its C-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19265
Source

Sf9, Baculovirus cells. 

Appearance
A clear, colorless solution that has been sterile filtered.

FGFR1OP Human

FGFR1 Oncogene Partner Human Recombinant

Recombinant human FGFR1OP, produced in E.Coli, is a single, non-glycosylated polypeptide chain comprising 403 amino acids (amino acids 1-379) with a molecular weight of 43.5 kDa. It includes a 24 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19382
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

FGFR2 Human

Fibroblast Growth Factor Receptor 2 Fc Chimera Human Recombinant

Soluble FGFR-2a (IIIc) Fc Chimera Human Recombinant is a heterodimeric, glycosylated polypeptide chain with a molecular weight of 170 kDa. It comprises 602 amino acids and includes a Xa cleavage site fused with the Fc region of human IgG1. The protein is produced in a baculovirus expression system and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19477
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.

FGFR2 Human, (22-289)

Fibroblast Growth Factor Receptor-2 (22-289 a.a.) Human Recombinant

Produced in Sf9 insect cells using baculovirus expression system, FGFR2 is a single glycosylated polypeptide chain. This recombinant protein encompasses amino acids 22 to 289 and has a molecular weight of 56.8 kDa, including a 239 amino acid hIgG-His tag at the C-terminus. The purification process involves proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT19560
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

FGFR2 Human, His

Fibroblast Growth Factor Receptor-2 Human Recombinant, His Tag

Recombinant Human FGFR2, produced in Sf9 Baculovirus cells, is a single glycosylated polypeptide chain. It consists of 596 amino acids (22-378a.a.) with a molecular mass of 66.6 kDa. On SDS-PAGE, the apparent molecular size will be approximately 70-100 kDa. This protein is expressed with a 239 amino acid hIgG-His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19635
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

FGFR3 Human, His

Fibroblast Growth Factor Receptor-3 Human Recombinant, His Tag

Recombinant human FGFR3, produced in Sf9 insect cells using a baculovirus expression system, is a single glycosylated polypeptide chain. This protein consists of 592 amino acids (residues 23-375a.a.) and has a molecular weight of 65.1 kDa. Note that its apparent molecular size on SDS-PAGE may appear between 70-100 kDa.

This FGFR3 protein is expressed with a C-terminal 239 amino acid hIgG-His tag and purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT19705
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

FGFR3 Human

Fibroblast Growth Factor Receptor 3 Fc Chimera Human Recombinant

Soluble FGFR3 Human recombinant, a heterodimeric, glycosylated polypeptide chain containing 593 amino acids with a molecular weight of 170 kDa, is produced in Fc Chimera by fusing the protein with the Fc portion of human IgG1 using a Xa cleavage site.
Shipped with Ice Packs
Cat. No.
BT19772
Source
Insect Cells.
Appearance
The product appears as a sterile, white, lyophilized (freeze-dried) powder.
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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