

| 货号 | MV157021 |
|---|---|
| 品牌 | abinScience |
| 描述 |
Recombinant Mouse ACE2 Protein, C-Fc (MV157021) expressed in Mammalian Cells, spanning Gln18-Thr740. Purity: >90% by SDS-PAGE.
Highlights
|
| 表达系统 | Mammalian cells |
| Accession号 | Q8R0I0 |
| 蛋白长度 | Gln18-Thr740 |
| 应用 | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| 种属 | Mus musculus (Mouse) |
| 性质 | Recombinant |
| 内毒素水平 | Please contact with the lab for this information. |
| 纯度 | >90% as determined by SDS-PAGE. |
| 预测分子量 | 111.82 kDa |
| 状态 | Lyophilized |
| 保存溶液 | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| 重悬 | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| 运输 | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| 稳定性和存储 | 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. |
| 别名 | ACE-related carboxypeptidase, ACE2, ACEH, Angiotensin-converting enzyme 2, Angiotensin-converting enzyme homolog, Angiotensin-converting enzyme-related carboxypeptidase, EC:3.4.17.-, EC:3.4.17.23, Metalloprotease MPROT15, Processed angiotensin-converting enzyme 2 |
| 背景 | Angiotensin-converting enzyme 2 is a ~92 kDa protein. Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A. By cleavage of angiotensin II, may be an important regulator of heart function. 1. Crackower, MA. et al. (2002) Nature 417, 822-8. PMID: 12075344 2. Donoghue, M. et al. (2003) Journal of molecular and cellular cardiology 35, 1043-53. PMID: 12967627 3. Imai, Y. et al. (2005) Nature 436, 112-6. PMID: 16001071 4. Kowalczuk, S. et al. (2008) FASEB journal : official publication of the Federation of American Societies for Experimental Biology 22, 2880-7. PMID: 18424768 5. Camargo, SM. et al. (2009) Gastroenterology 136, 872-82. PMID: 19185582 6. Fairweather, SJ. et al. (2012) The Biochemical journal 446, 135-48. PMID: 22677001 |
| Note | For research use only |

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