FGFR4 Human

Fibroblast Growth Factor Receptor 4 Fc Chimera Human Recombinant
Cat. No.
BT19861
Source
Insect Cells.
Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Soluble FGFR-4a (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 and having a molecular mass of 170 kDa.
The FGFR4 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
The fibroblast growth factor (FGF) family consists of at least 18 structurally related proteins with diverse roles in physiological and pathological processes, such as cell growth, differentiation, angiogenesis, wound healing, and tumor development. FGFs exert their biological effects by binding to and activating a family of type I transmembrane tyrosine kinase receptors known as FGF receptors (FGFRs). Upon ligand binding, FGFRs dimerize and undergo autophosphorylation, initiating downstream signaling cascades. Currently, four distinct genes encoding highly similar FGFRs (FGFR1-4) have been identified. All four FGFR genes encode proteins with a conserved structure, including an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acidic region located between IgI and IgII domains, a transmembrane domain, and a split tyrosine kinase domain. Alternative splicing of FGFR1-3 mRNAs results in the generation of multiple receptor isoforms. One common splicing event affects FGFR1 and FGFR2, leading to isoforms containing either all three Ig domains (designated as the 'a' isoform) or only IgII and IgIII domains (designated as the 'b' isoform). In contrast, only the 'a' isoform has been observed for FGFR3 and FGFR4. Further splicing events involving FGFR1-3 occur in the C-terminal half of the IgIII domain, which is encoded by two mutually exclusive exons. These events generate FGFRs with alternative IgIII domains (IIIb and IIIc). Notably, a secreted FGFR1 isoform called IIIa has been reported, consisting of the N-terminal half of the IgIII domain and some intronic sequences. This isoform functions as an FGF-binding protein. Mutations in FGFR1-3 genes have been linked to birth defects characterized by craniosynostosis. Ongoing research aims to elucidate the intricate expression patterns of these receptors and their specific interactions with various FGF ligands.
Description
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.
Physical Appearance
White powder, lyophilized and sterile.
Formulation
CD334 was lyophilized from a sterile solution at a concentration of 1 mg/mL, without any additional additives.
Solubility
To reconstitute the lyophilized FGFR-4, it is recommended to dissolve it in sterile PBS at a minimum concentration of 100 µg/mL. The reconstituted solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized FGFR4 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. After reconstitution, FGFR4 should be stored at 4°C for 2-7 days. For extended storage, it is advisable to store it at temperatures below -18°C. To ensure optimal stability during long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA) to the reconstituted solution. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of FGFR-4 is greater than 90%, as determined by the following methods: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis. (b) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The biological activity of FGFR-4 is assessed by its ability to inhibit human acidic fibroblast growth factor (FGF-acidic)-induced proliferation in R1 cells. The half-maximal effective concentration (ED50) for this inhibitory effect typically falls within the range of 15.0-30.0 ng/mL.
Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
Source
Insect Cells.

Product Science Overview

Structure and Function

FGFR4 consists of three extracellular immunoglobulin-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain . The extracellular domains are responsible for binding to fibroblast growth factors (FGFs), which are a family of 18 glycoproteins . Upon binding to FGFs, FGFR4 undergoes dimerization and autophosphorylation, leading to the activation of downstream signaling pathways that regulate cellular processes .

FGFR4 Fc Chimera

The FGFR4 Fc Chimera is a recombinant protein that combines the extracellular domain of FGFR4 with the Fc region of human immunoglobulin G1 (IgG1) . This fusion protein is designed to enhance the stability and solubility of FGFR4, making it suitable for various research applications. The Fc region also allows for easy purification using protein A or G affinity chromatography .

Expression and Purification

The recombinant FGFR4 Fc Chimera is typically expressed in mammalian cell lines, such as NS0 cells . The protein is then purified using affinity chromatography, followed by size-exclusion chromatography to ensure high purity and homogeneity . The final product is lyophilized and can be reconstituted in phosphate-buffered saline (PBS) for use in experiments .

Applications in Research

FGFR4 Fc Chimera is widely used in research to study the role of FGFR4 in various biological processes and diseases. It is particularly useful in investigating the mechanisms of FGFR4 signaling and its involvement in cancer . FGFR4 is upregulated in multiple tumors, including pituitary, breast, pancreatic, hepatocellular, prostate, and gynecological cancers . It functions as an oncogene in breast cancer and is implicated in drug resistance in colorectal cancer . Therefore, FGFR4 Fc Chimera serves as a valuable tool for developing targeted therapies and understanding cancer progression .

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