Serpin A1 Protein, Human, Recombinant (His)

Catalog No. TMPY-00915

Synonyms: PRO2275, SerpinA1, serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1, serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 1, α1AT, AAT, PI1, PI, MGC9222, MGC23330, A1A, alpha1AT, A1AT

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 (alpha1-antitrypsin), an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents (nystatin, filipin, MbetaCD (methyl-beta-cyclodextrin) 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 complete inhibition of oxLDL uptake by monocytes. Previous population studies have suggested that heterozygote status for the AAT gene (SerpinA1) is a risk factor for chronic rhinosinusitis with nasal polyposis (CRSwNP). 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. Its most important physiologic functions are the protection of pulmonary tissue from aggressive proteolytic enzymes and regulation of pulmonary immune processes.

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Serpin A1 Protein, Human, Recombinant (His)

Pack Size	Availability	Price/USD
100 μg	In stock	$ 451.00
200 μg	5 days	$ 798.00
500 μg	5 days	$ 1,690.00

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Biological Description

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Product Properties

References and Literature

Biological Information

Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The IC50 value is < 3.0 nM, as measured in 100μL reaction mixture containing 1.25 ng trypsin, 10 μM substrate, 50 mM Tris, 10 mM CaCl2, 0.15 M NaCl, pH 7.5.

Description

Species	Human
Expression System	HEK293
Tag	His
Accession Number	P01009-1
Synonyms	PRO2275, SerpinA1, serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1, serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 1, α1AT, AAT, PI1, PI, MGC9222, MGC23330, A1A, alpha1AT, A1AT
Construction	A DNA sequence encoding the human SerpinA1 (NP_000286.3) pre-protein (Met 1-Lys 418) was expressed with a C-terminal polyhistidine tag.
Protein Purity	> 95 % as determined by SDS-PAGE
Molecular Weight	Approxiamtely 45.7 kDa

Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method.
Formulation	Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage	Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Shipping	In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research 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 (alpha1-antitrypsin), an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents (nystatin, filipin, MbetaCD (methyl-beta-cyclodextrin) 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 complete inhibition of oxLDL uptake by monocytes. Previous population studies have suggested that heterozygote status for the AAT gene (SerpinA1) is a risk factor for chronic rhinosinusitis with nasal polyposis (CRSwNP). 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. Its most important physiologic functions are the protection of pulmonary tissue from aggressive proteolytic enzymes and regulation of pulmonary immune processes.

References and Literature

1. Khnlein T,et al.(2008) Alpha-1 antitrypsin deficiency: pathogenesis, clinical presentation, diagnosis, and treatment. Am J Med. 121(1): 3-9. 2. Camelier AA,et al.(2008) Alpha-1 antitrypsin deficiency: diagnosis and treatment. J Bras Pneumol. 34(7): 514-27. 3. Subramaniyam D,et al.(2010) Cholesterol rich lipid raft microdomains are gateway for acute phase protein, SERPINA1. Int J Biochem Cell Biol. 42(9): 1562-70. 4. Kilty SJ,et al.(2010) Polymorphisms in the SERPINA1 (Alpha-1-Antitrypsin) gene are associated with severe chronic rhinosinusitis unresponsive to medical therapy. Am J Rhinol Allergy. 24(1): e4-9.

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Keywords

Serpin A1 Protein, Human, Recombinant (His) MGC 23330 PRO2275 SerpinA1 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 1 MGC-23330 PRO 2275 α1AT AAT PI 1 PRO-2275 PI-1 MGC-9222 PI1 PI MGC9222 MGC23330 A1A alpha1AT MGC 9222 A1AT recombinant recombinant-proteins proteins protein