FGFR2 Human, His

Fibroblast Growth Factor Receptor-2 Human Recombinant, His Tag
Cat. No.
BT19635
Source
Sf9, Baculovirus cells.
Synonyms

EC 2.7.10, FGFR-2, BFR-1, CD332, BBDS, CEK3, ECT1, TK14, TK25, CFD1, KSAM, JWS, Fibroblast Growth Factor Receptor 2, Keratinocyte Growth Factor Receptor, Bacteria-Expressed Kinase, EC 2.7.10.1, K-SAM, KGFR, BEK, Protein Tyrosine Kinase, Receptor Like 14, BEK Fibroblast Growth Factor Receptor, Craniofacial Dysostosis 1, Jackson-Weiss Syndrome, Pfeiffer Syndrome, Crouzon Syndrome, CD332 Antigen.

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined 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

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.

Product Specs

Introduction
Fibroblast Growth Factors (FGFs) are a family of at least 18 structurally related proteins involved in many physiological and pathological cellular processes. These processes include cell growth, differentiation, angiogenesis, wound healing, and tumorigenesis. FGFs exert their biological activities through a family of type I transmembrane tyrosine kinase receptors. These receptors dimerize and autophosphorylate upon ligand binding. There are four distinct genes encoding closely related FGF receptors: FGFR-1, -2, -3, and -4. Alternative splicing of mRNAs results in multiple forms of FGFR-1 to -3. A common splicing event for FGFR-1 and -2 produces receptors containing all three Ig domains (alpha isoform) or only IgII and IgIII (beta isoform). Only the alpha isoform has been found for FGFR-3 and FGFR-4. Further splicing events for FGFR-1 to -3 involve the C-terminal half of the IgIII domain. Two mutually exclusive alternative exons in this region generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A secreted FGF-binding protein called the IIIa isoform has also been reported for FGFR-1. This isoform comprises the N-terminal half of the IgIII domain and some intron sequences. Mutations in FGFR-1 to -3 have been identified in patients with birth defects involving craniosynostosis.
Description
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.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
FGFR2 protein solution is provided at a concentration of 1 mg/ml in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), store the vial at 4°C. For extended storage, freeze at -20°C. It's recommended to add a carrier protein (0.1% HSA or BSA) for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 95.0% by SDS-PAGE analysis.
Synonyms

EC 2.7.10, FGFR-2, BFR-1, CD332, BBDS, CEK3, ECT1, TK14, TK25, CFD1, KSAM, JWS, Fibroblast Growth Factor Receptor 2, Keratinocyte Growth Factor Receptor, Bacteria-Expressed Kinase, EC 2.7.10.1, K-SAM, KGFR, BEK, Protein Tyrosine Kinase, Receptor Like 14, BEK Fibroblast Growth Factor Receptor, Craniofacial Dysostosis 1, Jackson-Weiss Syndrome, Pfeiffer Syndrome, Crouzon Syndrome, CD332 Antigen.

Source
Sf9, Baculovirus cells.
Amino Acid Sequence

RPSFSLVEDT TLEPEEPPTK YQISQPEVYV AAPGESLEVR CLLKDAAVIS WTKDGVHLGP NNRTVLIGEY LQIKGATPRD SGLYACTASR TVDSETWYFM VNVTDAISSG DDEDDTDGAE DFVSENSNNK RAPYWTNTEK MEKRLHAVPA ANTVKFRCPA GGNPMPTMRW LKNGKEFKQE HRIGGYKVRN QHWSLIMESV VPSDKGNYTC VVENEYGSIN HTYHLDVVER SPHRPILQAG LPANASTVVG GDVEFVCKVY SDAQPHIQWI KHVEKNGSKY GPDGLPYLKV LKHSGINSSN AEVLALFNVT EADAGEYICK VSNYIGQANQ SAWLTVLPKQ QAPGREKEIT ASPDYLELEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

Product Science Overview

Structure and Function

FGFR2 consists of an extracellular region with three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment, and a cytoplasmic tyrosine kinase domain . The extracellular portion of FGFR2 interacts with FGFs, initiating a cascade of downstream signals that influence mitogenesis and differentiation . FGFR2 is known to bind to acidic, basic, and keratinocyte growth factors, depending on the isoform .

Recombinant FGFR2 with His Tag

The recombinant form of FGFR2, tagged with a His (histidine) tag, is produced using various expression systems, such as baculovirus . The His tag facilitates the purification and detection of the protein. The recombinant FGFR2 is often used in research to study its role in cellular processes and its involvement in various diseases .

Role in Diseases

Mutations in the FGFR2 gene are associated with several genetic disorders, including Crouzon syndrome, Pfeiffer syndrome, Apert syndrome, Jackson-Weiss syndrome, Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome, and syndromic craniosynostosis . These mutations can lead to abnormal receptor function, resulting in altered cellular signaling and developmental abnormalities .

Applications in Research

Recombinant FGFR2 with a His tag is widely used in research to investigate its role in various physiological and pathological processes. It is particularly valuable in studying cancer, as FGFR2 is implicated in several types of cancer, including lung and breast cancers . Researchers use recombinant FGFR2 to explore its involvement in angiogenesis, mitogenesis, osteogenesis, myogenesis, carcinogenesis, and tissue repair after injury .

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