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Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein, CF

Bio-Techne includes R&D Systems | Catalog # 1268-PI

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1268-PI-010

Key Product Details

Source

NS0

Accession #

Conjugate

Unconjugated

Applications

Inhibition Activity

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

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.

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 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.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

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

  1. Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
  2. Barbour, K.W. et al. (2002) Genomics 80:515.
  3. 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

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein, CF

For research use only

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