| Product Name | NMRAL1, 1-299aa, Human |
|---|---|
| Description | NMRAL1 is a redox sensor protein that undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP+ levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. Recombinant human NMRAL1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | NmrA-like family domain containing 1, HSCARG, SDR48A1 |
| Host | Sf9 |
| Molecular Weight | 29.9 kDa (268aa) confirmed by MALDI-TOF (Molecular size on SDS-PAGE will appear higher) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSHMVDKKL VVVFGGTGAQ GGSVARTLLE DGTFKVRVVT RNPRKKAAKE LRLQGAEVVQ GDQDDQVIME LALNGAYATF IVTNYWESCS QEQEVKQGKL LADLARRLGL HYVVYSGLEN IKKLTAGRLA AAHFDGKGEV EEYFRDIGVP MTSVRLPCYF ENLLSHFLPQ KAPDGKSYLL SLPTGDVPMD GMSVSDLGPV VLSLLKMPEK YVGQNIGLST CRHTAEEYAA LLTKHTRKVV HDAKMTPEDY EKLGFPGARD LANMFRFYAL RPDRDIELTL RLNPKALTLD QWLEQHKGDF NLL |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.1M NaCl, 20% glycerol |
| Concentration | 0.5 mg/ml (determined by Bradford assay) |
| Purity | > 95% 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 | Gan.Q., et al. (2009) J. Cell. Sci. 122 (PT 22), 4081-4088 Lian,M., et al. (2009) J. Biol. Chem. 284 (27), 17998-18006 |
| Background | NMRAL1 is a redox sensor protein that undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP+ levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. Recombinant human NMRAL1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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