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Recombinant Mouse Serpina1a protein (rFc Tag)

种属

Mouse

纯度

>90 %, SDS-PAGE

标签

rFc Tag

生物活性

未测试

Cat no : Eg3047

Print datasheet

Synonyms

AAT, Alpha-1 protease inhibitor 1, Alpha-1-antiproteinase, Alpha-1-antitrypsin 1-1, Dom1



产品信息

纯度 >90 %, SDS-PAGE
内毒素 <0.1 EU/μg protein, LAL method
生物活性
Not tested
来源 HEK293-derived Mouse Serpina1a protein Glu25-Lys413 (Accession# P07758) with a rabbit IgG Fc tag at the C-terminus.
基因ID 20700
蛋白编号 P07758
预测分子量 69.5 kDa
SDS-PAGE 68-85 kDa, reducing (R) conditions
组分 Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
复溶 Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
储存条件
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
运输条件 The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

背景信息

Serpina1a alo known as Alpha-1-antitrypsin (A1AT), it is an acute phase serine proteinase inhibitor, which is synthesized and secreted as a glycoprotein by hepatocytes and alveolar macrophages in humans to protect tissue from degradation by endogenous neutrophil elastase (NE). Severe A1AT deficiency is a congenital disorder, which occurs due to certain missense point mutations in the serum protease inhibitor, member 1 (SERPINA1) gene. The most predominant of these mutations is the Z-mutation, accounting for >95% of clinical A1AT deficiency cases. This point mutation results in substitution of glutamic acid at position 342 with lysine (E342K), which destabilizes the adjacent reactive centre loop (RCL).

参考文献:

1. Eggenschwiler R. et al. (2019) Sci Rep. 9(1):7486. 2. Murphy MP. et al. (2024) Am J Physiol Lung Cell Mol Physiol. 327(4):L600-L606. 3. Zieger M. et al. (2022) Mol Ther Methods Clin Dev. 25:425-438.

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