Recombinant Human SerpinA1/A1AT Protein (His Tag)

Specifications

Catalog number

PKSH031695-01

Size / count

100 µg

Dry ice

No

Hazardous

No

Discontinued

No

Background

SerpinA1, also known as Alpha-1 antitrypsin (AAT), is a prototype member of the Serpin superfamily of the serine protease inhibitors. This serine protease inhibitor blocks the protease, neutrophil elastase. Alpha-1 antitrypsin is mainly produced in the liver and acts as an antiprotease. Its principal function is to inactivate neutrophil elastase, preventing tissue damage. SerpinA1, an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. It association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents and oxidized low-density lipoprotein (oxLDL) and conversely, enhanced by free cholesterol. Furthermore, SerpinA1/monocyte association per se depletes lipid raft cholesterol as characterized by the activation of extracellular signal-regulated kinase 2, formation of cytosolic lipid droplets, and a complete inhibition of oxLDL uptake by monocytes. Alpha-1 antitrypsin deficiency is a recently identified genetic disease that occurs almost as frequently as cystic fibrosis. It is caused by various mutations in the SerpinA1 gene, and has numerous clinical implications. Alpha-1 antitrypsin deficiency is an inherited disease affecting the lung and liver. In the liver, alpha-1 antitrypsin deficiency may manifest as benign neonatal hepatitis syndrome; a small percentage of adults develop liver fibrosis, with progression to cirrhosis and hepatocellular carcinoma.

Synonyms

A1A; A1AT; AAT; Alpha-1 Protease Inhibitor; Alpha-1-Antiproteinase; Alpha-1-Antitrypsin; MGC23330; MGC9222; PI; PI1; PRO2275; SERPINA1; Serpin A1; alpha1AT

UniProt

P01009

Accession Number

NP_000286.3

Expression System

HEK293 Cells

Tag

C-His

Sequence

Met 1-Lys 418

Applications

Enzyme

Field of Research

Cardiovascular; Cancer; metabolism

Endotoxin

< 1.0 EU per μg of the protein as determined by the LAL method.

Purity

> 97 % as determined by reducing SDS-PAGE.

Bioactivity

Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK (Dnp) -NH2 (Anaspec, Catalog#27114) . The IC50 value is < 3.0 nM, as measured in 100μL reaction mixture containing 1. 25 ng trypsin (Sigma, Catalog#T1426), 10 μM substrate, 50 mM Tris, 10 mM CaCl2, 0.15 M NaCl, pH 7.5.

Reconstitution

Please refer to the printed manual for detailed information.

Shipping Conditions

This product is provided as lyophilized powder which is shipped with ice packs.

Storage Conditions

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Calculated Molecular Weight

45.7 kDa

Observed Molecular Weight

55-60 kDa

Species

Human