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Recombinant Human Fibroblast Growth Factor Receptor 1, Fc-tagged

Cat.No. : FGFR1-01H
Product Overview : Recombinant Human Soluble FGFR-1a (IIIc) Fc Chimera 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 FGFR1 is purified by proprietary chromatographic techniques.
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Cat. No. : FGFR1-01H
Description : Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ß isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
Source : Insect Cells
Physical 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.
Formulation : CD331 was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.
Solubility : It is recommended to reconstitute the lyophilized bFGF-R in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Biological Activity : Determined by its ability to inhibit human FGF acidic-dependent proliferation on R1 cells. The ED50 for this effect is typically at 15.0-30.0 ng/ml.
Storage : Lyophilized FGFR1A although stable at room temperature for 3 weeks, should be stored desiccated below -18℃. Upon reconstitution FGFR1 should be stored at 4℃ between 2-7 days and for future use below -18℃. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Gene Name : FGFR1 fibroblast growth factor receptor 1 [ Homo sapiens ]
Synonyms : FGFR1; fibroblast growth factor receptor 1; CEK; FLG; OGD; FLT2; KAL2; BFGFR; CD331; FGFBR; HBGFR; N-SAM; FLJ99988; fms-related tyrosine kinase 2; H2; H3; H4; H5; N-SAM; CD331; Pfeiffer syndrome; FGFR-1; bFGF-R; EC 2.7.10.1; Fms-like tyrosine kinase 2; c-fgr; CD_antigen; OTTHUMP00000190881; soluble FGFR1 variant 1; FMS-like tyrosine kinase 2; hydroxyaryl-protein kinase; heparin-binding growth factor receptor; basic fibroblast growth factor receptor 1; OTTHUMP00000190874; OTTHUMP00000190878; OTTHUMP00000190879; c-fgr; soluble FGFR1 variant 2
Gene ID : 2260
mRNA Refseq : NM_015850
Protein Refseq : NP_056934
MIM : 136350
UniProt ID : P11362
Chromosome Location : 8p11.2-p11.1
Pathway : MAPK signaling pathway; MAPK signaling pathway; Melanoma; Pathways in cancer; Prostate cancer; Regulation of actin cytoskeleton; Axon guidance; Signaling by FGFR
Function : ATP binding; fibroblast growth factor receptor activity; fibroblast growth factor receptor activity; heparin binding; nucleotide binding; protein binding; receptor activity; transferase activity

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (5)

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How does DEFB103A interact with the human microbiome? 06/10/2022

DEFB103A plays a role in maintaining a balanced microbiome by exerting selective antimicrobial activity. Understanding this interaction is crucial for potential applications in microbiome-related disorders.

Can DEFB103A be used as a diagnostic marker for certain diseases? 05/01/2022

Research suggests that altered levels of DEFB103A expression may be associated with certain diseases. However, its specific use as a diagnostic marker requires further validation.

Are there any side effects or concerns associated with the therapeutic use of DEFB103A? 04/25/2022

While research is ongoing, potential side effects and concerns related to the therapeutic use of DEFB103A or its analogs need to be thoroughly investigated, including any possible immunogenicity.

How does DEFB103A contribute to the immune system? 02/08/2018

DEFB103A plays a crucial role in the innate immune system by acting as an antimicrobial peptide. It helps defend the body against a wide range of pathogens, including bacteria, viruses, and fungi.

What specific clinical conditions are associated with DEFB103A deficiency? 05/25/2017

DEFB103A deficiency has been linked to an increased susceptibility to various infections, particularly those affecting the skin and mucosal surfaces.

Customer Reviews (3)

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Reviews
05/01/2021

    FGFR1, a calcium-dependent phospholipid-binding protein, plays a crucial role in various cellular processes, making it a valuable tool for investigation.

    12/25/2018

      When combined with the support and quality assurance provided by the manufacturer, researchers can confidently utilize FGFR1 protein to unravel the intricate mechanisms underlying cellular processes, ultimately advancing scientific knowledge.

      07/24/2017

        The manufacturer can contribute to the research process by providing top-quality FGFR1 protein that meets rigorous standards of purity, stability, and reliability.

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