Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE |
background | Four distinct genes encoding closely related FGF receptors, FGF R1-4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid‑box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain.FGFR3 is tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. |
molecular weight | The protein has a predicted MW of 37.09 kDa. Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Biotinylated Mouse FGFR3 alpha (IIIb) Protein (Primary Amine Labeling) 2002
$900.00 – $2,000.00
Summary
- Expression: HEK293
- Pure: Yes (SDS-PAGE)
- Amino Acid Range: Pro22-Val349
Biotinylated Mouse FGFR3 alpha (IIIb) Protein (Primary Amine Labeling) 2002
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Four distinct genes encoding closely related FGF receptors, FGF R1-4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain.FGFR3 is tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. |
Protein names Phosphatidylinositol 3-kinase regulatory subunit alpha (PI3-kinase regulatory subunit alpha) (PI3K regulatory subunit alpha) (PtdIns-3-kinase regulatory subunit alpha) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha) (PI3-kinase subunit p85-alpha) (PtdIns-3-kinase regulatory subunit p85-alpha) |
Protein family PI3K p85 subunit family |
Mass 83598Da |
Function Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (PubMed:17626883, PubMed:19805105, PubMed:7518429). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348923). {ECO:0000269|PubMed:17626883, ECO:0000269|PubMed:19805105, ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:7518429}. |
Tissues Isoform 2 is expressed in skeletal muscle and brain, and at lower levels in kidney and cardiac muscle. Isoform 2 and isoform 4 are present in skeletal muscle (at protein level). {ECO:0000269|PubMed:8628286}. |
Structure Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts (via SH2 domains) with CCDC88A/GIV (tyrosine-phosphorylated form); the interaction enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (PubMed:21954290). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with PIK3R2; the interaction is dissociated in an insulin-dependent manner (By similarity). Interacts with XBP1 isoform 2; the interaction is direct and induces translocation of XBP1 isoform 2 into the nucleus in a ER stress- and/or insulin-dependent but PI3K-independent manner (PubMed:20348923). Interacts with FER. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with PTK2/FAK1 (By similarity). Interacts with phosphorylated TOM1L1. Interacts with phosphorylated LIME1 upon TCR and/or BCR activation. Interacts with SOCS7. Interacts with RUFY3. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity (By similarity). Interacts with phosphorylated LAT, LAX1 and TRAT1 upon TCR activation. Interacts with CBLB. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with IRS1 and phosphorylated IRS4, as well as with NISCH and HCST. Interacts with FASLG, KIT and BCR. Interacts with AXL, FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with FGR and HCK. Interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts with ERBB4 (phosphorylated). Interacts with NTRK1 (phosphorylated upon ligand-binding). Interacts with FAM83B; activates the PI3K/AKT signaling cascade (PubMed:23676467). Interacts with APPL1 and APPL2 (By similarity). Interacts with SRC (PubMed:28903391). Interacts with ALOX5; this interaction bridges ALOX5 with CD40 after CD40 ligation in B cells and leads to the production of reactive oxygen species (ROS) (PubMed:21200133). Interacts with TYK2 (PubMed:10995743). Interacts with nephrin NPHN1; the interaction is reduced by high glucose levels (PubMed:28955049). Interacts with CASP8 (phosphorylated on Tyr-380) (PubMed:27109099). Interacts with CD28 (PubMed:7568038). {ECO:0000250|UniProtKB:P23727, ECO:0000250|UniProtKB:P26450, ECO:0000250|UniProtKB:Q63787, ECO:0000269|PubMed:10086340, ECO:0000269|PubMed:10528161, ECO:0000269|PubMed:10739672, ECO:0000269|PubMed:10867024, ECO:0000269|PubMed:10995743, ECO:0000269|PubMed:11087752, ECO:0000269|PubMed:11526404, ECO:0000269|PubMed:11567151, ECO:0000269|PubMed:11912194, ECO:0000269|PubMed:12359715, ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:18721752, ECO:0000269|PubMed:19286672, ECO:0000269|PubMed:19805105, ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:21200133, ECO:0000269|PubMed:21954290, ECO:0000269|PubMed:23676467, ECO:0000269|PubMed:27109099, ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:28955049, ECO:0000269|PubMed:7537849, ECO:0000269|PubMed:7541045, ECO:0000269|PubMed:7568038, ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8276809, ECO:0000269|PubMed:8628286, ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:9038210, ECO:0000269|PubMed:9178760, ECO:0000269|PubMed:9489702, ECO:0000269|PubMed:9553137, ECO:0000269|PubMed:9687533}.; (Microbial infection) Interacts with HIV-1 Nef to activate the Nef associated p21-activated kinase (PAK). This interaction depends on the C-terminus of both proteins and leads to increased production of HIV. {ECO:0000269|PubMed:12009866}.; (Microbial infection) Interacts with HCV NS5A. {ECO:0000269|PubMed:12186904}.; (Microbial infection) Interacts with herpes simplex virus 1 UL46; this interaction activates the PI3K/AKT pathway. {ECO:0000269|PubMed:21228233}.; (Microbial infection) Interacts with herpes simplex virus 1 UL46 and varicella virus ORF12; this interaction activates the PI3K/AKT pathway. {ECO:0000269|PubMed:23192871}. |
Post-translational modification Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation. {ECO:0000269|PubMed:11087752, ECO:0000269|PubMed:11526404}.; In adipose tissue, polyubiquitinated by the BCR(KBTBD2) E3 ubiquitin ligase complex; recognized by KBTBD2 through the SH2 domains, undergoes 'Lys-48'-linked polyubiquitination leading to its degradation. {ECO:0000269|PubMed:27708159}.; Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated by CSF1R. Phosphorylated by ERBB4. Phosphorylated on tyrosine residues by TEK/TIE2. Dephosphorylated by PTPRJ. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear (By similarity). Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR. {ECO:0000250, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:18348712}. |
Domain The SH3 domain mediates the binding to CBLB, and to HIV-1 Nef. |
Target Relevance information above includes information from UniProt accession: P27986 |
The UniProt Consortium |
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Biotinylated Mouse FGFR3 alpha (IIIb) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. |
Publications
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