| Product Name | G3BP1, 1-466aa, Human |
|---|---|
| Description | G3BP1 is one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. And it cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. Recombinant human G3BP1 protein, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | ATP dependent DNA helicase VIII, G3BP, G3BP1, GAP binding protein, GAP SH3 domain binding protein 1, HDH VIII, MGC111040, Ras GTPase activating protein binding protein 1, Ras GTPase activating protein SH3 domain binding protein, RasGAP associated endoribonuclease G3BP |
| Host | E. coli |
| Molecular Weight | 7.6 kDa (68aa), confirmed by MALDI-TOF |
| Amino Acid Sequence | MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQAVVS NDMEEHLEEP VAEPEPDPEP EPEQEPVSEI QEEKPEPVLE ETAPEDAQKS SSPAPADIAQ TVQEDLRTFS WASVTSKNLP PSGAVPVTGI PPHVVKVPAS QPRPESKPES QIPPQRPQRD QRVREQRINI PPQRGPRPIR EAGEQGDIEP RRMVRHPDSH QLFIGNLPHE VDKSELKDFF QSYGNVVELR INSGGKLPNF GFVVFDDSEP VQKVLSNRPI MFRGEVRLNV EEKKTRAARE GDRRDNRLRG PGGPRGGLGG GMRGPPRGGM VQKPGFGVGR GLAPRQVEHH HHHH |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in phosphate-buffered saline ( pH 7.4) containing 10% glycerol |
| Concentration | 0.25 mg/ml (determined by Bradford assay) |
| Purity | > 85% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Kurz, J.C., et al. (2000) Curr. Opin. Chem. Biol. 4: 553-558. van Eenennaam, H., et al. (2001) Mol. Biol. Cell. 12: 3680-3689. |
| Background | G3BP1 is one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. And it cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. Recombinant human G3BP1 protein, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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