Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 1268-PI
Key Product Details
Product Specifications
Source
Mouse myeloma cell line, NS0-derived human Serpin A1/alpha 1-Antitrypsin protein
Glu25-Lys418, with a C-terminal 10-His tag
Glu25-Lys418, with a C-terminal 10-His tag
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
Glu25
Predicted Molecular Mass
46 kDa
SDS-PAGE
60 kDa, reducing conditions
Activity
Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002).
The IC50 value is approximately <5.0 nM, as measured under the described conditions.
The IC50 value is approximately <5.0 nM, as measured under the described conditions.
Reviewed Applications
Read 1 review rated 3 using 1268-PI in the following applications:
Scientific Data Images for Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein, CF
Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein Enzyme Activity
Recombinant Human Serpin A1/alpha-1-Antitrypsin (Catalog # 1268-PI) is measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002).Formulation, Preparation and Storage
1268-PI
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and CaCl2 with Trehalose. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile 50 mM Tris, 10 mM CaCl2 and 150 mM NaCl, pH 7.5. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: Serpin A1/alpha 1-Antitrypsin
Serpin A1 is the archetypal member of the Serpin superfamily of the serine protease inhibitors (1). As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in the liver and secreted into the bloodstream with the major function to protect tissues against neutrophil elastase. A severe serpin A1 deficiency leads to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma (2). The deficiency is caused by point mutations in naturally occurring serpin A1 variants (over 70 are known). For example, the Z variant (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe serpin A1 deficiency (3).
References
- Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
- Barbour, K.W. et al. (2002) Genomics 80:515.
- Lomas, D.A. et al. (2002) Biochem. Soc. Trans. 30:89.
Alternate Names
A1AT, alpha 1-Antitrypsin, alpha 1-Proteinase Inhibitor
Entrez Gene IDs
5265 (Human)
Gene Symbol
SERPINA1
UniProt
Additional Serpin A1/alpha 1-Antitrypsin Products
Product Documents for Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein, CF
Product Specific Notices for Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein, CF
For research use only
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