

| カタログ番号 | HC184012 |
|---|---|
| 説明 |
Recombinant Human ISCU Protein, N-His (HC184012) expressed in E. coli, spanning His36-Lys167. Purity: >90% by SDS-PAGE.
Highlights
|
| 発現システム | E. coli |
| アクセッション番号 | Q9H1K1 |
| タンパク質長 | His36-Lys167 |
| アプリケーション | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| 種 | Homo sapiens (Human) |
| 性質 | Recombinant |
| エンドトキシンレベル | Please contact with the lab for this information. |
| 純度 | >90% as determined by SDS-PAGE. |
| 予測分子量 | 16.52 kDa |
| 形態 | Lyophilized |
| 保存バッファー | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. データシートのハードコピーまたはロット固有のCOAに記載された具体的なバッファー情報を参照してください。 |
| 再構成 | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| 発送 | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| 安定性と保存 | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| 別名 | ISCU, Iron-sulfur cluster assembly enzyme ISCU, NIFUN, NifU-like N-terminal domain-containing protein, NifU-like protein |
| 背景 | Iron-sulfur cluster assembly enzyme ISCU is a ~17 kDa protein. Mitochondrial scaffold protein, of the core iron-sulfur cluster (ISC) assembly complex, that provides the structural architecture on which the [2Fe-2S] clusters are assembled. The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (Probable). 1. Freibert, SA. et al. (2021) Nature communications 12, 6902. PMID: 34824239 2. Bridwell-Rabb, J. et al. (2014) Biochemistry 53, 4904-13. PMID: 24971490 3. Cai, K. et al. (2018) Journal of inorganic biochemistry 183, 107-116. PMID: 29576242 4. Fox, NG. et al. (2018) Biochimie 152, 211-218. PMID: 30031876 5. Cai, K. et al. (2013) The Journal of biological chemistry 288, 28755-70. PMID: 23940031 |
| 注意事項 | For research use only |
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